|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
43-592 |
0e+00 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 606.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 43 PLVYRTIGQQLELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARA 122
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 123 GLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEISDADTGKIRSEKFPHLRSVIIDSNDSLKGA 202
Cdd:PRK08315 92 GAILVTINPAYRLSELEYALNQSGCKALIAADGFKDSDYVAMLYELAPELATCEPGQLQSARLPELRRVIFLGDEKHPGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 203 LRFDDFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFH 281
Cdd:PRK08315 172 LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLtEEDRLCIPVPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 AFGVIISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVdlvntqKKLQVP------LGRIKKAVTGGA 355
Cdd:PRK08315 252 CFGMVLGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTALYGVPTMFI------AELDHPdfarfdLSSLRTGIMAGS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 356 IVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRG 434
Cdd:PRK08315 326 PCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 435 YTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPD 514
Cdd:PRK08315 406 YSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPD 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 515 ERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAfKAKETELKAAR 592
Cdd:PRK08315 486 EKYGEEVCAWIILRPG---ATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM-MIEELGLQAAK 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
229-577 |
0e+00 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 581.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFS 307
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLtEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 PKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVI 387
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 388 FQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVP-FGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVL 466
Cdd:cd05917 161 TQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 467 EANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAK 546
Cdd:cd05917 241 DEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG---AELTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|.
gi 24581924 547 GKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
29-579 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 525.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 29 MPSLiSHKHHIGKDPLVYRTIGQQLELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN 108
Cdd:PRK12583 1 MPQP-SYYQGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 109 YLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEISDADTGKIRSEKFPHL 188
Cdd:PRK12583 80 CAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACERLPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 189 RSVIIDSNDSLKGALRFDDFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL 268
Cdd:PRK12583 160 RGVVSLAPAPPPGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 269 -EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRI 347
Cdd:PRK12583 240 tEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 KKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQP 427
Cdd:PRK12583 320 RTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 428 GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEA 507
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 508 HVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPG---HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-587 |
6.48e-163 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 472.37 E-value: 6.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 49 IGQQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVG 128
Cdd:COG0318 1 LADLLRRAAARHPDRPALV--FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 129 LNPAYQGPEIAYCLNKVNVKAIIApetfktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddf 208
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 209 ldlasksereevakmqksilpesaCNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVII 287
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLtPGDVVLVALPLFHVFGLTV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 288 SIMAALTKGATMVLPAaGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQ 367
Cdd:COG0318 159 GLLAPLLAGATLVLLP-RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 368 VLNVEaVHSVYGLTETTAVIFQSlPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEK 447
Cdd:COG0318 238 RFGVR-IVEGYGLTETSPVVTVN-PEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 448 TKETIGnDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRL 527
Cdd:COG0318 316 TAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 528 EEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKETE 587
Cdd:COG0318 395 RPGAEL---DAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
47-579 |
9.36e-146 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 430.87 E-value: 9.36e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYyeilrdicpeisdadtgkIRSEKFPHLRSVII----DSNDSLKGA 202
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGLFLGVDY------------------SATTRLPALEHVVIceteEDDPHTEKM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 203 LRFDDFLDLASKSEREEvakmqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFH 281
Cdd:PRK07656 145 KTFTDFLAAGDPAERAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLtEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 AFGVIISIMAALTKGATMvLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQL 361
Cdd:PRK07656 219 VFGYKAGVNAPLMRGATI-LPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 362 IKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGY 441
Cdd:PRK07656 298 LERFESELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 442 HDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEV 521
Cdd:PRK07656 378 YDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 522 CAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK07656 458 KAYVVLKPG---AELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
53-485 |
7.72e-120 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 361.24 E-value: 7.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVsCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:pfam00501 1 LERQAARTPDKTALE-VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFKtqnyyeilrdicPEISDADTGKIRSEKfphlRSVIIDSNDSLKGALRFDDFLDLA 212
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVK----LVLVLDRDPVLKEEPLPEEAKPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SKSEREEVAKmqksilPESACNIQFTSGTTGNPKAACLTHHNFVNN-----GIHVGNRNELEGERICVQVPMFHAFGVII 287
Cdd:pfam00501 144 VPPPPPPPPD------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANvlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 288 SIMAALTKGATMVLPAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDV 365
Cdd:pfam00501 218 GLLGPLLAGATVVLPPGFpaLDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNvEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYHDD 444
Cdd:pfam00501 298 RELFG-GALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 24581924 445 EEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRG 485
Cdd:pfam00501 377 PELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
45-585 |
1.10e-117 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 359.12 E-value: 1.10e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 45 VYRTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVG--LWapNYLHWYLGMMGAARA 122
Cdd:PRK06187 4 YPLTIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAvfDW--NSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 123 GLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKtqnyyeilrdicPEISdadtgKIRsEKFPHLRSVIIDSNDSLKG- 201
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFV------------PLLA-----AIL-PQLPTVRTVIVEGDGPAAPl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 202 ---ALRFDDFLDLASkSEREEVAkmqksILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQV 277
Cdd:PRK06187 142 apeVGEYEELLAAAS-DTFDFPD-----IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLsRDDVYLVIV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 278 PMFHAFGVIISIMAALTkGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIV 357
Cdd:PRK06187 216 PMFHVHAWGLPYLALMA-GAKQVIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 358 SPQLIKDVRQVLNVEAVHsVYGLTETTAVIfqslpgdssdvvlnSVGHLTDHI-----------------EAKVVDAEGR 420
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQ-GYGMTETSPVV--------------SVLPPEDQLpgqwtkrrsagrplpgvEARIVDDDGD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 421 CVP--FGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFL 498
Cdd:PRK06187 359 ELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDAL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 499 NAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLV 578
Cdd:PRK06187 438 YGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATL---DAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
....*..
gi 24581924 579 EAFKAKE 585
Cdd:PRK06187 515 EQYAEGK 521
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
49-578 |
1.18e-117 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 357.26 E-value: 1.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 49 IGQQLELSASNFGDVEAiVSCHeGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVG 128
Cdd:cd05936 1 LADLLEEAARRFPDKTA-LIFM-GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 129 LNPAYQGPEIAYCLNKVNVKAIIAPETFKtqnyyeilrdicpeisdadtgkirsekfphlrsviidsnDSLKGAlrfddf 208
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVSFT---------------------------------------DLLAAG------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 209 ldlASKSEREEVAkmqksilPESACNIQFTSGTTGNPKAACLTHHNFVNN---GIHVGNRNELEGERICVQVPMFHAFGV 285
Cdd:cd05936 114 ---APLGERVALT-------PEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAWLEDLLEGDDVVLAALPLFHVFGL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 IISIMAALTKGATMVL-PAagFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD 364
Cdd:cd05936 184 TVALLLPLALGATIVLiPR--FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 365 VRQVLNVEAVHSvYGLTETTAVIFQSLPGDSSdvVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDD 444
Cdd:cd05936 262 FEELTGVPIVEG-YGLTETSPVVAVNPLDGPR--KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 445 EEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAY 524
Cdd:cd05936 339 PEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAF 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24581924 525 VRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLV 578
Cdd:cd05936 418 VVLKEG---ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
233-573 |
3.21e-111 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 336.18 E-value: 3.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 CNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGvIISIMAALTKGATMVLPAaGFSPKDS 311
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLtEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLP-KFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIFqSL 391
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVA-TG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 392 PGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGnDRWLRTGDQFVLEANGY 471
Cdd:cd04433 159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDE-DGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 472 GRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAH 551
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADL---DAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 24581924 552 FKVPRYVIPIDAFPKTTSGKIQ 573
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
53-574 |
2.03e-98 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 306.46 E-value: 2.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:cd17631 1 LRRRARRHPDRTALV--FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLnkvnvkaiiapetfktqnyyeilrdicpeisdADTGkirsekfphlrsviidsndslkGALRFDDFldla 212
Cdd:cd17631 79 LTPPEVAYIL--------------------------------ADSG----------------------AKVLFDDL---- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 sksereevakmqksilpesaCNIQFTSGTTGNPKAACLTHHNFVNNGI-HVGNRNELEGERICVQVPMFHAFGVIISIMA 291
Cdd:cd17631 101 --------------------ALLMYTSGTTGRPKGAMLTHRNLLWNAVnALAALDLGPDDVLLVVAPLFHIGGLGVFTLP 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 292 ALTKGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVrQVLNV 371
Cdd:cd17631 161 TLLRGGTVVILRK-FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL-QARGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 372 EaVHSVYGLTETTAVIFqSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKET 451
Cdd:cd17631 239 K-FVQGYGMTETSPGVT-FLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 452 IGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGv 531
Cdd:cd17631 317 FRDG-WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG- 394
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24581924 532 dpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd17631 395 --AELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
65-573 |
7.77e-98 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 306.83 E-value: 7.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNK 144
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 145 VNVKAII-APETFKTqnyyeilrdicpeISDADTGKIRSEKfphlrsvIIDSNDSLKGALRFDDFLDLASKSErEEVAKM 223
Cdd:cd05911 81 SKPKVIFtDPDGLEK-------------VKEAAKELGPKDK-------IIVLDDKPDGVLSIEDLLSPTLGEE-DEDLPP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELE---GERICVQVPMFHAFGvIISIMAALTKGATMV 300
Cdd:cd05911 140 PLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgsNDVILGFLPLYHIYG-LFTTLASLLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 -LPaaGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYG 379
Cdd:cd05911 219 iMP--KFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETTAVIFQSLPGDssdVVLNSVGHLTDHIEAKVVDAEGR-CVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWL 458
Cdd:cd05911 297 MTETGGILTVNPDGD---DKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 459 RTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTA 538
Cdd:cd05911 374 HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG---EKLTE 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 24581924 539 ETLKAYAKGKLAHFKVPRY-VIPIDAFPKTTSGKIQ 573
Cdd:cd05911 451 KEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
62-579 |
1.42e-94 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 298.46 E-value: 1.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 62 DVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYC 141
Cdd:cd05926 2 DAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 142 LNKVNVKAIIAPetfktqnyyeilrdicpeiSDADTGKIRSEkfPHLRSVIIDSNDSLKGALRFDDFLDLASKSEREEVA 221
Cdd:cd05926 82 LADLGSKLVLTP-------------------KGELGPASRAA--SKLGLAILELALDVGVLIRAPSAESLSNLLADKKNA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 222 KMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PMFHAFGVIISIMAALTKGATMV 300
Cdd:cd05926 141 KSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVmPLFHVHGLVASLLSTLAAGGSVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 LPAaGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQV-PLGRIKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYG 379
Cdd:cd05926 221 LPP-RFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPEsPPPKLRFIRSCSASLPPAVLEALEATFGA-PVLEAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETTAVIFqSLPGDSSDVVLNSVGhLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLR 459
Cdd:cd05926 299 MTEAAHQMT-SNPLPPGPRKPGSVG-KPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 460 TGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAE 539
Cdd:cd05926 377 TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG---ASVTEE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24581924 540 TLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd05926 454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
74-579 |
7.89e-91 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 286.97 E-value: 7.89e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAP 153
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 ETFKTQNYYEilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevakmqksiLPESAC 233
Cdd:cd05903 81 ERFRQFDPAA----------------------------------------------------------------MPDAVA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 NIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAgFSPKDSL 312
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLgPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDI-WDPDKAL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLnVEAVHSVYGLTETTAvIFQSLP 392
Cdd:cd05903 176 ALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPG-AVTSIT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYG 472
Cdd:cd05903 254 PAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEegvDPASFTAETLKAYAKGK-LAH 551
Cdd:cd05903 333 RITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTK---SGALLTFDELVAYLDRQgVAK 409
|
490 500
....*....|....*....|....*...
gi 24581924 552 FKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd05903 410 QYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
47-583 |
2.09e-88 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 283.58 E-value: 2.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVD--GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICpeisdadtgkirsEKFPHLRSVIIDsNDSlkgalrfD 206
Cdd:COG1021 103 VFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQ-------------AEVPSLRHVLVV-GDA-------G 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 DFLDLASkSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGihvgnrneLEGERIC---------VQV 277
Cdd:COG1021 162 EFTSLDA-LLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSV--------RASAEICgldadtvylAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 278 PMFHAFGVIIS-IMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAI 356
Cdd:COG1021 233 PAAHNFPLSSPgVLGVLYAGGTVVL-APDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 357 VSPQLIKDVRQVLNVeAVHSVYGLTEttAVIFQSLPGDSSDVVLNSVGH-LTDHIEAKVVDAEGRCVPFGQPGELCVRGY 435
Cdd:COG1021 312 LSPELARRVRPALGC-TLQQVFGMAE--GLVNYTRLDDPEEVILTTQGRpISPDDEVRIVDEDGNPVPPGEVGELLTRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 436 TTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDE 515
Cdd:COG1021 389 YTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 516 RLGEEVCAYVRLeegvDPASFTAETLKAYAKGK-LAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:COG1021 469 YLGERSCAFVVP----RGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
72-577 |
9.13e-88 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 278.41 E-value: 9.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYclnkvnvkaii 151
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAY----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 apetfktqnyyeILRDicpeiSDAdtgkirsekfphlRSVIIDSndslkgalrfddfldlasksereevakmqksilpes 231
Cdd:cd05934 70 ------------IIDH-----SGA-------------QLVVVDP------------------------------------ 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 232 aCNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATMVLpAAGFSPKD 310
Cdd:cd05934 84 -ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLgEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL-LPRFSASR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKkaVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIFQS 390
Cdd:cd05934 162 FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGV-RLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 391 LPGDssdVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR---GYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLE 467
Cdd:cd05934 239 RDEP---RRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNG-WFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 468 ANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKG 547
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG---ETLDPEELFAFCEG 391
|
490 500 510
....*....|....*....|....*....|
gi 24581924 548 KLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05934 392 QLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
234-574 |
1.77e-85 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 269.37 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 NIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATmVLPAAGFSPKDSL 312
Cdd:cd17638 4 DIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLtEDDRYLIINPFFHTFGYKAGIVACLLTGAT-VVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFqSLP 392
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATM-CRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDSSDVVLNSVGHLTDHIEAKVVDaegrcvpfgqPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYG 472
Cdd:cd17638 162 GDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVdpaSFTAETLKAYAKGKLAHF 552
Cdd:cd17638 232 RITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV---TLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 24581924 553 KVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
61-577 |
1.04e-84 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 275.07 E-value: 1.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 61 GDVEAIVSCHEG---KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPE 137
Cdd:COG0365 23 GDKVALIWEGEDgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 138 IAYCLNKVNVKAII-APETF---KTQNYYEILRDICpeisdadtgkirsEKFPHLRSVII----DSNDSLKGALRFDDFL 209
Cdd:COG0365 103 LADRIEDAEAKVLItADGGLrggKVIDLKEKVDEAL-------------EELPSLEHVIVvgrtGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 210 dlASKSEREEVAKMQksilPESACNIQFTSGTTGNPKAACLTHHNFVNN---------GIHvgnrnelEGERICVQVPMF 280
Cdd:COG0365 170 --AAASAEFEPEPTD----ADDPLFILYTSGTTGKPKGVVHTHGGYLVHaattakyvlDLK-------PGDVFWCTADIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 281 HAFGVIISIMAALTKGATMVL----PAAGfSPKDSLQAIVNEKCSVIHGTPTMY-------VDLVNtqkklQVPLGRIKK 349
Cdd:COG0365 237 WATGHSYIVYGPLLNGATVVLyegrPDFP-DPGRLWELIEKYGVTVFFTAPTAIralmkagDEPLK-----KYDLSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 350 AVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTAVIFQSLPGDssDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGE 429
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEAVGVP-IVDGWGQTETGGIFISNLPGL--PVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 430 LCVRGYTT--MLGYHDDEEKTKETIGNDR--WLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVI 505
Cdd:COG0365 388 LVIKGPWPgmFRGYWNDPERYRETYFGRFpgWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 506 EAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:COG0365 468 EAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
55-572 |
3.38e-84 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 271.80 E-value: 3.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 55 LSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQ 134
Cdd:cd05904 13 LFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 135 GPEIAYCLNKVNVKAIIApetfkTQNYYEILRDIcpeisdadtgkirsekfpHLRSVIIDSNDSlkGALRFDDFLDLASK 214
Cdd:cd05904 93 PAEIAKQVKDSGAKLAFT-----TAELAEKLASL------------------ALPVVLLDSAEF--DSLSFSDLLFEADE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 215 SEREEVAkmqksILPESACNIQFTSGTTGNPKAACLTHHNFVNN--GIHVGNRNELEGER--ICVqVPMFHAFGVIISIM 290
Cdd:cd05904 148 AEPPVVV-----IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMvaQFVAGEGSNSDSEDvfLCV-LPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 291 AALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVL- 369
Cdd:cd05904 222 GLLRLGATVVV-MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFp 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 370 NVEAVHSvYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYHDDEEKT 448
Cdd:cd05904 301 NVDLGQG-YGMTESTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEAT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 449 KETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLE 528
Cdd:cd05904 380 AATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRK 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24581924 529 EGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05904 460 PG---SSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI 500
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
47-579 |
8.24e-83 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 269.62 E-value: 8.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSCHEG----KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARA 122
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 123 GLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEIsdadtgkirsekfPHLRSVIIDSNDslkGA 202
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPEL-------------PALRHVVVVGGD---GA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 203 LRFDDFL-DLASKSEREEVAKMQKSIL-PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PM 279
Cdd:PRK13295 168 DSFEALLiTPAWEQEPDAPAILARLRPgPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMAsPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 280 FHAFGVIISIMAALTKGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSP 359
Cdd:PRK13295 248 AHQTGFMYGLMMPVMLGATAVLQDI-WDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 360 QLIKDVRQVLNVEAVhSVYGLTETTAVIFqSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTML 439
Cdd:PRK13295 327 ALVERARAALGAKIV-SAWGMTENGAVTL-TKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 440 GYHDDEEKTKETigNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:PRK13295 405 GYLKRPQLNGTD--ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGE 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 520 EVCAYVRLEEGvdpASFTAETLKAYAKG-KLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK13295 483 RACAFVVPRPG---QSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
48-587 |
2.11e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 257.17 E-value: 2.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 48 TIGQQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSV 127
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALV--FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 128 GLNPAYQGPEIAYCLNKVNVKAIIA-PEtfktqnyyeiLRDICPEISDADTgkirsekfphlrSVIIDSNDSLKGALRFD 206
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVdPA----------LAPTAEAALALLP------------VDTLILSLVLGGREAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 DFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTH----HNFVNnGIHVGnrnELEGERICVQ-VPMFH 281
Cdd:PRK08316 148 GWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHraliAEYVS-CIVAG---DMSADDIPLHaLPLYH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 AFGVIISIMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQL 361
Cdd:PRK08316 224 CAQLDVFLGPYLYVGATNVI-LDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 362 IKDVRQVLNVEAVHSVYGLTET--TAVIFQslPGDSsDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTML 439
Cdd:PRK08316 303 LKELRERLPGLRFYNCYGQTEIapLATVLG--PEEH-LRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLML 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 440 GYHDDEEKTKETIGnDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:PRK08316 380 GYWDDPEKTAEAFR-GGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIE 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 520 EVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKETE 587
Cdd:PRK08316 459 AVTAVVVPKAG---ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFTD 523
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
48-579 |
4.17e-78 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 256.98 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 48 TIGQQLELSASNFGDVEAIVSCHeGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSV 127
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 128 GLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDIcpeisdadtgkirSEKFPHLRSVIIdsNDSLKGALRFDD 207
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPL-------------QNQLPQLQQIVG--VDKLAPATSSLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 208 FLDLASKSEREEVAKMQKSilPESACnIQFTSGTTGNPKAACLTHHNFV-NNGIHVGNRNELEGERICVQVPMFHAFGVI 286
Cdd:PRK06087 168 LSQIIADYEPLTTAITTHG--DELAA-VLFTSGTEGLPKGVMLTHNNILaSERAYCARLNLTWQDVFMMPAPLGHATGFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 287 ISIMAALTKGATMVLPAAgFSPKDSLQAIVNEKCSVIHG-TPTMYvDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDV 365
Cdd:PRK06087 245 HGVTAPFLIGARSVLLDI-FTPDACLALLEQQRCTCMLGaTPFIY-DLLNLLEKQPADLSALRFFLCGGTTIPKKVAREC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVlNVEAVhSVYGLTETTAVIFQSlPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDE 445
Cdd:PRK06087 323 QQR-GIKLL-SVYGSTESSPHAVVN-LDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 446 EKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYV 525
Cdd:PRK06087 400 ELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 526 RLEEGVdpASFTAETLKAY-AKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK06087 480 VLKAPH--HSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
53-577 |
1.15e-75 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 249.85 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEaIVSC-HEGK--RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN---YLHWYLGMMGAARAGLTs 126
Cdd:cd12119 2 LEHAARLHGDRE-IVSRtHEGEvhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNthrHLELYYAVPGMGAVLHT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 vgLNPAYQGPEIAYCLNKVNVKAIIAPETFktQNYYEILRDICPEIsdadtgkirsEKFPHLRSVIIDSNDSLKGALRFD 206
Cdd:cd12119 80 --INPRLFPEQIAYIINHAEDRVVFVDRDF--LPLLEAIAPRLPTV----------EHVVVMTDDAAMPEPAGVGVLAYE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 DFLDLASKSEREEVakmqksiLPE-SACNIQFTSGTTGNPKAACLTH-----HNFVnnGIHVGNRNELEGERICVQVPMF 280
Cdd:cd12119 146 ELLAAESPEYDWPD-------FDEnTAAAICYTSGTTGNPKGVVYSHrslvlHAMA--ALLTDGLGLSESDVVLPVVPMF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 281 HAFGVIISIMAALTkGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQ 360
Cdd:cd12119 217 HVNAWGLPYAAAMV-GAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 361 LIKDVRQvLNVEAVHSvYGLTETTAVI--------FQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPF-GQP-GEL 430
Cdd:cd12119 296 LIEAFEE-RGVRVIHA-WGMTETSPLGtvarppseHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGEL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 431 CVRG------YttmlgYHDDEEKTKETigNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQV 504
Cdd:cd12119 374 QVRGpwvtksY-----YKNDEESEALT--EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581924 505 IEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd12119 447 AEAAVIGVPHPKWGERPLAVVVLKEGATV---TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
53-577 |
1.54e-73 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 243.36 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:cd12118 10 LERAAAVYPDRTSIV--YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFktqNYYEILrdicpeisdaDTGKirsekfphlrsviidsndslkgalrfDDFLDLA 212
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREF---EYEDLL----------AEGD--------------------------PDFEWIP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SKSEREEVAkmqksilpesacnIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGEriCV---QVPMFHAFG-VIIS 288
Cdd:cd12118 129 PADEWDPIA-------------LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQH--PVylwTLPMFHCNGwCFPW 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 289 IMAALtkGATMV-LPAagFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQ 367
Cdd:cd12118 194 TVAAV--GGTNVcLRK--VDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 368 vLNVEAVHsVYGLTETTAVI--------FQSLPgDSSDVVLNS---VGHLTDHiEAKVVDAEG-RCVPF-GQP-GELCVR 433
Cdd:cd12118 270 -LGFDVTH-VYGLTETYGPAtvcawkpeWDELP-TEERARLKArqgVRYVGLE-EVDVLDPETmKPVPRdGKTiGEIVFR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 434 GYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVP 513
Cdd:cd12118 346 GNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARP 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 514 DERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIpIDAFPKTTSGKIQKFKL 577
Cdd:cd12118 425 DEKWGEVPCAFVELKEGAKV---TEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVL 484
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
72-572 |
5.51e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 241.44 E-value: 5.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 APEtfKTQNYYEILRDICP-------EISDADTGKIR---SEKFPHLRsviiDSNDSL----KGALRFDDFLD-----LA 212
Cdd:PRK05605 135 VWD--KVAPTVERLRRTTPletivsvNMIAAMPLLQRlalRLPIPALR----KARAALtgpaPGTVPWETLVDaaiggDG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SKSEREEVAkmqksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIH-------VGNRNElegeRICVQVPMFHAFGV 285
Cdd:PRK05605 209 SDVSHPRPT-------PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawvpgLGDGPE----RVLAALPMFHAYGL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 IISIMAALTKGATMVL-PAagFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD 364
Cdd:PRK05605 278 TLCLTLAVSIGGELVLlPA--PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 365 VRQVLN---VEAvhsvYGLTETTAVIFQSLPGDSSDVvlNSVGHLTDHIEAKVVDAE--GRCVPFGQPGELCVRGYTTML 439
Cdd:PRK05605 356 WEKLTGgllVEG----YGLTETSPIIVGNPMSDDRRP--GYVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 440 GYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:PRK05605 430 GYWNRPEETAKSFLDG-WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSE 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 24581924 520 EVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK05605 509 EVVAAVVLEPG---AALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
42-577 |
1.31e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 237.74 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 42 DPLVYRTIGQQLELSASNFGDVEAIVSCheGKRYSFKSLLQEADALAAGFRKL-GLQPGDAVGLWAPNYLHWYLGMMGAA 120
Cdd:PRK05677 19 NPDEYPNIQAVLKQSCQRFADKPAFSNL--GKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 121 RAGLTSVGLNPAYQGPEIAYCLNKVNVKAII-----APETFKTQNYYEILRDICPEISDAdtgkirsekFPHLRSVIIDS 195
Cdd:PRK05677 97 RAGLIVVNTNPLYTAREMEHQFNDSGAKALVclanmAHLAEKVLPKTGVKHVIVTEVADM---------LPPLKRLLINA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 196 ----------NDSLKGALRFDDFLDLASKSEREEVakmqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHV--- 262
Cdd:PRK05677 168 vvkhvkkmvpAYHLPQAVKFNDALAKGAGQPVTEA-----NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCral 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 263 --GNRNElEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAagfSPKDsLQAIVNE----KCSVIHGTPTMYVDLVNT 336
Cdd:PRK05677 243 mgSNLNE-GCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS---NPRD-LPAMVKElgkwKFSGFVGLNTLFVALCNN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 337 QKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIFQSLPgdsSDVVLNSVGHLTDHIEAKVVD 416
Cdd:PRK05677 318 EAFRKLDFSALKLTLSGGMALQLATAERWKEVTGC-AICEGYGMTETSPVVSVNPS---QAIQVGTIGIPVPSTLCKVID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 417 AEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIED 496
Cdd:PRK05677 394 DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELED 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 497 FLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVdpaSFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFK 576
Cdd:PRK05677 474 VLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGE---TLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRE 550
|
.
gi 24581924 577 L 577
Cdd:PRK05677 551 L 551
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
53-574 |
5.14e-70 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 237.55 E-value: 5.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIV------SCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLtS 126
Cdd:PRK07529 31 LSRAAARHPDAPALSflldadPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI-A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIA--PEtFKTqnyyEILRDICPEISDAdtgkirsekfPHLRSVI-IDSNDSLKGAL 203
Cdd:PRK07529 110 NPINPLLEPEQIAELLRAAGAKVLVTlgPF-PGT----DIWQKVAEVLAAL----------PELRTVVeVDLARYLPGPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 204 RFDDFLDLASKSER-----EEVAKmQKSILPESACNIQ-------F-TSGTTGNPKAACLTHHNFVNNGiHVGNRNELEG 270
Cdd:PRK07529 175 RLAVPLIRRKAHARildfdAELAR-QPGDRLFSGRPIGpddvaayFhTGGTTGMPKLAQHTHGNEVANA-WLGALLLGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 271 E---RICvQVPMFHAFGVIISIMAALTKGATMVLPA-AGFSPK---DSLQAIVNE-KCSVIHGTPTMYVDLvntqkkLQV 342
Cdd:PRK07529 253 PgdtVFC-GLPLFHVNALLVTGLAPLARGAHVVLATpQGYRGPgviANFWKIVERyRINFLSGVPTVYAAL------LQV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 343 PLGR-----IKKAVTGGAIVSPQLIKDVRQVLNVEAVHsVYGLTETTAVIFQSLPGdsSDVVLNSVGHLTDHIEAKVV-- 415
Cdd:PRK07529 326 PVDGhdissLRYALCGAAPLPVEVFRRFEAATGVRIVE-GYGLTEATCVSSVNPPD--GERRIGSVGLRLPYQRVRVVil 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 416 DAEGR----CVPfGQPGELCVRGYTTMLGYHDdEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFP 491
Cdd:PRK07529 403 DDAGRylrdCAV-DEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 492 KEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAH-FKVPRYVIPIDAFPKTTSG 570
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG---ASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVG 557
|
....
gi 24581924 571 KIQK 574
Cdd:PRK07529 558 KIFK 561
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
74-572 |
7.67e-70 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 231.98 E-value: 7.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAp 153
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 etfktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasKSEREEVAkmqksILPesac 233
Cdd:cd05935 80 ------------------------------------------------------------GSELDDLA-----LIP---- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 niqFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQ-VPMFHAFGVIISIMAALTKGATMVLpAAGFSPKDSL 312
Cdd:cd05935 91 ---YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILAcLPLFHVTGFVGSLNTAVYVGGTYVL-MARWDRETAL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHsVYGLTETTAVIFQSLP 392
Cdd:cd05935 167 ELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVE-GYGLTETMSQTHTNPP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDSSdvvLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE---TIGNDRWLRTGDQFVLEA 468
Cdd:cd05935 246 LRPK---LQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 469 NGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDpASFTAETLKAYAKGK 548
Cdd:cd05935 323 EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYR-GKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....
gi 24581924 549 LAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKI 425
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
46-516 |
9.31e-70 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 236.15 E-value: 9.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 46 YRTIGQQLELSASNFGDVEAIVSCHEG--KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAG 123
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 124 LTSVGLNPAYQGPEIAYCLNKVNVKAIIApETfktQNYYEILRDICPEIsdadtgkirsekfPHLRSVIIDSNDSLKGAL 203
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFV-ED---QEQLDKLLEVRDEL-------------PSLRHIVVLDPRGLRDDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 204 R---FDDFLDL-ASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVP 278
Cdd:COG1022 153 RllsLDELLALgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLgPGDRTLSFLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 279 MFHAFGVIISImAALTKGATMVLPAagfSPK---DSLQAI------------------VNEKcsvIHGTPTM-------- 329
Cdd:COG1022 233 LAHVFERTVSY-YALAAGATVAFAE---SPDtlaEDLREVkptfmlavprvwekvyagIQAK---AEEAGGLkrklfrwa 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 330 ------YVDLVNTQK------KLQVPL--------------GRIKKAVTGGAIVSPQLIK-------DVRQVlnveavhs 376
Cdd:COG1022 306 lavgrrYARARLAGKspslllRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARffralgiPVLEG-------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 377 vYGLTETTAVIFQSLPGDssdVVLNSVGHLTDHIEAKVvdaegrcvpfGQPGELCVRGYTTMLGYHDDEEKTKETIGNDR 456
Cdd:COG1022 378 -YGLTETSPVITVNRPGD---NRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADG 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 457 WLRTGDQFVLEANGYGRIVGRLKEMLI-RGGENIFPKEIEDFLNAHPQVIEAHVIGvpDER 516
Cdd:COG1022 444 WLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG--DGR 502
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
43-580 |
5.14e-68 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 230.03 E-value: 5.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 43 PLVYRTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN---YLHWYLGmmgA 119
Cdd:PRK06155 17 PPSERTLPAMLARQAERYPDRPLLVF--GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNrieFLDVFLG---C 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 120 ARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFktqnyyeilrdiCPEISDADTGkirSEKFPHLrsVIIDSNDSL 199
Cdd:PRK06155 92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL------------LAALEAADPG---DLPLPAV--WLLDAPASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 200 KGALRFDdFLDLASKSEREEVAKMQksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVP 278
Cdd:PRK06155 155 SVPAGWS-TAPLPPLDAPAPAAAVQ----PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIgADDVLYTTLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 279 MFHAFGVIISIMAALTkGATMVL----PAAGFSPkdslqAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGG 354
Cdd:PRK06155 230 LFHTNALNAFFQALLA-GATYVLeprfSASGFWP-----AVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 355 aiVSPQLIKDVRQVLNVEAVhSVYGLTETTAVIFQSLPGDSSdvvlNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRG 434
Cdd:PRK06155 304 --VPAALHAAFRERFGVDLL-DGYGSTETNFVIAVTHGSQRP----GSMGRLAPGFEARVVDEHDQELPDGEPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 435 ---YTTMLGYHDDEEKTKETiGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIG 511
Cdd:PRK06155 377 depFAFATGYFGMPEKTVEA-WRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 512 VPDERLGEEVCAYVRLEEGV--DPASftaetLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDGTalEPVA-----LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
42-572 |
4.37e-67 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 227.98 E-value: 4.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 42 DPLVYRTIGQQLELSASNFGDVEAIVSCheGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAAR 121
Cdd:PRK07059 18 DASQYPSLADLLEESFRQYADRPAFICM--GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 122 AGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEISDADTGKIRSEKfPHLRSVIIDSND---- 197
Cdd:PRK07059 96 AGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLGFK-GHIVNFVVRRVKkmvp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 198 --SLKGALRFDDFLdlaSKSEREEVAKMqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVG--------NRNE 267
Cdd:PRK07059 175 awSLPGHVRFNDAL---AEGARQTFKPV--KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqpafeKKPR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 268 LEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAagfSPKDsLQAIVNE----KCSVIHGTPTMYVDLVNTQKKLQVP 343
Cdd:PRK07059 250 PDQLNFVCALPLYHIFALTVCGLLGMRTGGRNILIP---NPRD-IPGFIKElkkyQVHIFPAVNTLYNALLNNPDFDKLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 344 LGRIKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIFQSlPGDSSDVVlNSVGHLTDHIEAKVVDAEGRCVP 423
Cdd:PRK07059 326 FSKLIVANGGGMAVQRPVAERWLEMTGC-PITEGYGLSETSPVATCN-PVDATEFS-GTIGLPLPSTEVSIRDDDGNDLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 424 FGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQ 503
Cdd:PRK07059 403 LGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 504 VIEAHVIGVPDERLGEEVCAYVRLEegvDPAsFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK07059 483 VLEVAAVGVPDEHSGEAVKLFVVKK---DPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKI 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
65-574 |
3.74e-66 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 222.55 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVscHEGKRYSFKSLLQEADALAAGF-RKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYcln 143
Cdd:cd05941 4 AIV--DDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 kvnvkaiiapetfktqnyyeilrdicpeisdadtgkirsekfphlrsVIIDSNDSLkgalrfddFLDLASksereevakm 223
Cdd:cd05941 79 -----------------------------------------------VITDSEPSL--------VLDPAL---------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksilpesacnIQFTSGTTGNPKAACLTHHNFVNNgihvgnRNEL-------EGERICVQVPMFHAFGVIISIMAALTKG 296
Cdd:cd05941 94 -----------ILYTSGTTGRPKGVVLTHANLAAN------VRALvdawrwtEDDVLLHVLPLHHVHGLVNALLCPLFAG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 ATMV-LPaaGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNT--------QKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQ 367
Cdd:cd05941 157 ASVEfLP--KFDPKEVAISRLMPSITVFMGVPTIYTRLLQYyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 368 VLNveavHSV---YGLTETTAVIFQSLPGDSSDvvlNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYHD 443
Cdd:cd05941 235 ITG----HTLlerYGMTEIGMALSNPLDGERRP---GTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 444 DEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLI-RGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVC 522
Cdd:cd05941 308 KPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVV 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24581924 523 AYVRLEEGVDPASftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd05941 388 AVVVLRAGAAALS--LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
72-583 |
3.74e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 223.92 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAyclnkvnvkAII 151
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELD---------ALL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 ApetfktqnyyeilrdicpeisDADtgkirsekfPHLrsvIIDSNDSLKGALRFDDFLDLASKSEREEVAkMQKSILPES 231
Cdd:PRK09088 91 Q---------------------DAE---------PRL---LLGDDAVAAGRTDVEDLAAFIASADALEPA-DTPSIPPER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 232 ACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGE-RICVQVPMFHAFGVIISIMAALTKGATMvLPAAGFSPKD 310
Cdd:PRK09088 137 VSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHsSFLCDAPMFHIIGLITSVRPVLAVGGSI-LVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNEKCSVIH--GTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAivsPQLIKDVRQVLNvEAVHSV--YGLTETTAV 386
Cdd:PRK09088 216 TLGRLGDPALGITHyfCVPQMAQAFRAQPGFDAAALRHLTALFTGGA---PHAAEDILGWLD-DGIPMVdgFGMSEAGTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 387 IFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVL 466
Cdd:PRK09088 292 FGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 467 EANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE-EVCAYVRLEEgvdpASFTAETLKAYA 545
Cdd:PRK09088 372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEvGYLAIVPADG----APLDLERIRSHL 447
|
490 500 510
....*....|....*....|....*....|....*...
gi 24581924 546 KGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:PRK09088 448 STRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
46-579 |
6.16e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 224.81 E-value: 6.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 46 YRTIGQQLELSASNFGDVEAIVScHEGKRySFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLT 125
Cdd:PRK07788 48 YGPFAGLVAHAARRAPDRAALID-ERGTL-TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 126 SVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKtqnyyEILRDICPEIsdadtGKIRsekfphlrsVIIDSNDSLKGALRF 205
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFT-----DLLSALPPDL-----GRLR---------AWGGNPDDDEPSGST 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 206 DDFLDlaskserEEVAKMQKSILPESACN---IQFTSGTTGNPKAAclthhnfvnngihvgNRNELE------------- 269
Cdd:PRK07788 187 DETLD-------DLIAGSSTAPLPKPPKPggiVILTSGTTGTPKGA---------------PRPEPSplaplagllsrvp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 270 ---GERICVQVPMFHAFGV-IISIMAALtkGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNT-QKKLQVP- 343
Cdd:PRK07788 245 fraGETTLLPAPMFHATGWaHLTLAMAL--GSTVVLRRR-FDPEATLEDIAKHKATALVVVPVMLSRILDLgPEVLAKYd 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 344 LGRIKKAVTGGAIVSPQLIKDVRQVLNvEAVHSVYGLTE-TTAVIfqslpGDSSDVVLN--SVGHLTDHIEAKVVDAEGR 420
Cdd:PRK07788 322 TSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEvAFATI-----ATPEDLAEApgTVGRPPKGVTVKILDENGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 421 CVPFGQPGELCVRGYTTMLGYHDDeeKTKETIgnDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNA 500
Cdd:PRK07788 396 EVPRGVVGRIFVGNGFPFEGYTDG--RDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAG 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 501 HPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK07788 472 HPDVVEAAVIGVDDEEFGQRLRAFVVKAPG---AALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
65-579 |
1.85e-65 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 222.04 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVSCHEgkRYSFKSLLQEADALAAGFR-KLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:PRK06839 20 AIITEEE--EMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIAPETFktQNYYEILrdicpeisdadTGKIRSEkfphlRSVIIDsndslkgalrfddflDLASKSEREEVAKM 223
Cdd:PRK06839 98 DSGTTVLFVEKTF--QNMALSM-----------QKVSYVQ-----RVISIT---------------SLKEIEDRKIDNFV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERIC-VQVPMFHAFGVIISIMAALTKGATMVLP 302
Cdd:PRK06839 145 EKN--ESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSiVLLPLFHIGGIGLFAFPTLFAGGVIIVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDV--RQVLNVEAvhsvYGL 380
Cdd:PRK06839 223 RK-FEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFidRGFLFGQG----FGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 381 TETTAVIFQSLPGDSSDVVlNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRT 460
Cdd:PRK06839 298 TETSPTVFMLSEEDARRKV-GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 461 GDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAET 540
Cdd:PRK06839 376 GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS---SVLIEKD 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 24581924 541 LKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
46-577 |
5.37e-65 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 222.77 E-value: 5.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 46 YRTIGQQLELSASNFGDVEAIVSCheGKRYSFKSLLQEADALAAGFRK-LGLQPGDAVGLWAPNYLHWYLGMMGAARAGL 124
Cdd:PRK12492 23 YKSVVEVFERSCKKFADRPAFSNL--GVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 125 TSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKtQNYYEILRDICPE-ISDADTGKIRSEKFPHLRSVIIDS------ND 197
Cdd:PRK12492 101 IVVNTNPLYTAREMRHQFKDSGARALVYLNMFG-KLVQEVLPDTGIEyLIEAKMGDLLPAAKGWLVNTVVDKvkkmvpAY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 198 SLKGALRFDDFLDLASKSEREEVAKMQKSIlpesaCNIQFTSGTTGNPKAACLTHHNFVNNGIHV----------GNRNE 267
Cdd:PRK12492 180 HLPQAVPFKQALRQGRGLSLKPVPVGLDDI-----AVLQYTGGTTGLAKGAMLTHGNLVANMLQVraclsqlgpdGQPLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 268 LEGERICVQ-VPMFHAFGVIISIMAALTKGATMVLPAagfSPKDsLQAIVNE----KCSVIHGTPTMYVDLVNTQKKLQV 342
Cdd:PRK12492 255 KEGQEVMIApLPLYHIYAFTANCMCMMVSGNHNVLIT---NPRD-IPGFIKElgkwRFSALLGLNTLFVALMDHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 343 PLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSvYGLTETTAVIFQSLPGDSSDvvLNSVGHLTDHIEAKVVDAEGRCV 422
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATAERWEQLTGCTIVEG-YGLTETSPVASTNPYGELAR--LGTVGIPVPGTALKVIDDDGNEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 423 PFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHP 502
Cdd:PRK12492 408 PLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 503 QVIEAHVIGVPDERLGEEVCAYVRLEEGvdpaSFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVVARDP----GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
75-511 |
1.07e-64 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 219.00 E-value: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIApe 154
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 155 tfktqnyyeilrdicpeiSDADtgkirsekfphlrsviidsndslkgalrfddflDLASksereevakmqksilpesacn 234
Cdd:cd05907 84 ------------------EDPD---------------------------------DLAT--------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHVGNR-NELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPaagFSPKDSLQ 313
Cdd:cd05907 92 IIYTSGTTGRPKGVMLSHRNILSNALALAERlPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFA---SSAETLLD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 314 AIVNEKCSVIHGTPTMYVDLVNTQKKLQVP-----------LGRIKKAVTGGAIVSPQLIKDVRQvLNVEaVHSVYGLTE 382
Cdd:cd05907 169 DLSEVRPTVFLAVPRVWEKVYAAIKVKAVPglkrklfdlavGGRLRFAASGGAPLPAELLHFFRA-LGIP-VYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 383 TTAVIFQSLPGDssdVVLNSVGHLTDHIEAKVVDAegrcvpfgqpGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGD 462
Cdd:cd05907 247 TSAVVTLNPPGD---NRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGD 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24581924 463 QFVLEANGYGRIVGRLKEMLI-RGGENIFPKEIEDFLNAHPQVIEAHVIG 511
Cdd:cd05907 314 LGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-577 |
1.28e-64 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 220.32 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 56 SASNFGDVEAIVSCHegKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQG 135
Cdd:cd05959 13 LNEGRGDKTAFIDDA--GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 136 PEIAYCLNKVNVKAIIAPETFktqnyyeilrdiCPEISDADTGKIrsekfPHLRSVII-DSNDSLKGALRFDDFLdlASK 214
Cdd:cd05959 91 DDYAYYLEDSRARVVVVSGEL------------APVLAAALTKSE-----HTLVVLIVsGGAGPEAGALLLAELV--AAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 215 SEREEVAKMQksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGnRNEL---EGErICVQVP-MFHAFGVIISIM 290
Cdd:cd05959 152 AEQLKPAATH----ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYA-RNVLgirEDD-VCFSAAkLFFAYGLGNSLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 291 AALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLN 370
Cdd:cd05959 226 FPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 371 VEAVHSVyGLTETTAVIFQSLPGDssdVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE 450
Cdd:cd05959 306 LDILDGI-GSTEMLHIFLSNRPGR---VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 TIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEG 530
Cdd:cd05959 382 TFQGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24581924 531 VDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05959 461 YEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
47-574 |
1.27e-63 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 216.81 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVD--GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIAPETFktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalRFD 206
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYIVPDRH-----------------------------------------------AGF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 DFLDLAskseREEVAKmqksiLPESACnIQFTSGTTGNPKAACLTHHNFVNNgihVGNRNELEG----ERICVQVPMFHA 282
Cdd:cd05920 126 DHRALA----RELAES-----IPEVAL-FLLSGGTTGTPKLIPRTHNDYAYN---VRASAEVCGldqdTVYLAVLPAAHN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 283 F-----GVIISIMAaltkGATMVLPAAGfSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIV 357
Cdd:cd05920 193 FplacpGVLGTLLA----GGRVVLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 358 SPQLIKDVRQVLNVEaVHSVYGLTEttAVIFQSLPGDSSDVVLNSVGH-LTDHIEAKVVDAEGRCVPFGQPGELCVRGYT 436
Cdd:cd05920 268 SPALARRVPPVLGCT-LQQVFGMAE--GLLNYTRLDDPDEVIIHTQGRpMSPDDEIRVVDEEGNPVPPGEEGELLTRGPY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDER 516
Cdd:cd05920 345 TIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 517 LGEEVCAYVRLEegvdPASFTAETLKAYAKGK-LAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd05920 425 LGERSCAFVVLR----DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
65-572 |
1.76e-63 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 215.47 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYqgPE--IAYcl 142
Cdd:cd05930 5 AVV--DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY--PAerLAY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 143 nkvnvkaiiapetfktqnyyeILRDICPEIsdadtgkirsekfphlrsVIIDSNDslkgalrfddfldLASksereevak 222
Cdd:cd05930 79 ---------------------ILEDSGAKL------------------VLTDPDD-------------LAY--------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 223 mqksilpesacnIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVpMFHAFGVII-SIMAALTKGATMVL 301
Cdd:cd05930 98 ------------VIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQF-TSFSFDVSVwEIFGALLAGATLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 --PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIkkAVTGGAIVSPQLIKDVRQVLNVEAVHSVYG 379
Cdd:cd05930 165 lpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL--VLVGGEALPPDLVRRWRELLPGARLVNLYG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETTAVI-FQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETI------ 452
Cdd:cd05930 243 PTEATVDAtYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfg 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 GNDRWLRTGDQFVLEANG---Y-GRIVGRLKemlIRGgeniF---PKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYV 525
Cdd:cd05930 323 PGERMYRTGDLVRWLPDGnleFlGRIDDQVK---IRG----YrieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYV 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24581924 526 RLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05930 396 VPDEGGEL---DEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
53-584 |
4.77e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 217.14 E-value: 4.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAaGF--RKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLN 130
Cdd:PRK08314 16 LEVSARRYPDKTAIV--FYGRAISYRELLEEAERLA-GYlqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 131 PAYQGPEIAYCLNKVNVKAIIApetfkTQNYYEILRD----------ICPEISDADTGKIRSEKFPHLRSVIIDSNDSLK 200
Cdd:PRK08314 93 PMNREEELAHYVTDSGARVAIV-----GSELAPKVAPavgnlrlrhvIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 201 GALRFDDFLDLASKSEREEVAkmqksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PM 279
Cdd:PRK08314 168 GVVAWKEALAAGLAPPPHTAG-------PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVlPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 280 FHAFGVIISIMAALTKGATMVL------PAAGfspkdslQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKkAVTG 353
Cdd:PRK08314 241 FHVTGMVHSMNAPIYAGATVVLmprwdrEAAA-------RLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLR-YIGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 354 GAIVSP----QLIKDVRQVLNVEAvhsvYGLTETTAVIfQSLPGDSSDvvLNSVGHLTDHIEAKVVDAE-GRCVPFGQPG 428
Cdd:PRK08314 313 GGAAMPeavaERLKELTGLDYVEG----YGLTETMAQT-HSNPPDRPK--LQCLGIPTFGVDARVIDPEtLEELPPGEVG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 429 ELCVRGYTTMLGYHDDEEKTKE---TIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVI 505
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEafiEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 506 EAHVIGVPDERLGEEVCAYVRLEEGVdPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAK 584
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEA-RGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
46-583 |
7.69e-62 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 213.97 E-value: 7.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 46 YRTIGQQLELSASNFGDVEAIVSCheGKRYSFKsllqEADALAAGFR-----KLGLQPGDAVGLWAPNYLHWYLGMMGAA 120
Cdd:PRK08751 24 FRTVAEVFATSVAKFADRPAYHSF--GKTITYR----EADQLVEQFAayllgELQLKKGDRVALMMPNCLQYPIATFGVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 121 RAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTqNYYEILRD------ICPEISDA---DTGKIRSEKFPHLRSV 191
Cdd:PRK08751 98 RAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGT-TVQQVIADtpvkqvITTGLGDMlgfPKAALVNFVVKYVKKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 192 IIDSNdsLKGALRFDDFLDLASKserEEVAKMQksILPESACNIQFTSGTTGNPKAACLTHHNFVNN----GIHVGNRNE 267
Cdd:PRK08751 177 VPEYR--INGAIRFREALALGRK---HSMPTLQ--IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqaHQWLAGTGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 268 LE--GERICVQVPMFHAFgviisimaALTKGATMVLPAAGFS-----PKDsLQAIVNE----KCSVIHGTPTMYVDLVNT 336
Cdd:PRK08751 250 LEegCEVVITALPLYHIF--------ALTANGLVFMKIGGCNhlisnPRD-MPGFVKElkktRFTAFTGVNTLFNGLLNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 337 QKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSvYGLTETT-AVIFQSLPGDSSDvvlNSVGHLTDHIEAKVV 415
Cdd:PRK08751 321 PGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEA-YGLTETSpAACINPLTLKEYN---GSIGLPIPSTDACIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 416 DAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIE 495
Cdd:PRK08751 397 DDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 496 DFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEegvDPAsFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKF 575
Cdd:PRK08751 477 DVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK---DPA-LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRR 552
|
....*...
gi 24581924 576 KLVEAFKA 583
Cdd:PRK08751 553 ELRDAAKA 560
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
51-583 |
2.78e-61 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 212.15 E-value: 2.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 51 QQLELSASNFGDVEAIVscheGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLN 130
Cdd:PLN02330 36 QDAELYADKVAFVEAVT----GKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGAN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 131 PAYQGPEIAYCLNKVNVKAIIApetfktqnyyeilrdicpeiSDADTGKIRSEKFPhlrsVIIDSNDSLKGALRFDDFLD 210
Cdd:PLN02330 112 PTALESEIKKQAEAAGAKLIVT--------------------NDTNYGKVKGLGLP----VIVLGEEKIEGAVNWKELLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASKSEREEVakmQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNN--GIHVGNRNELEGERICVQ-VPMFHAFGvII 287
Cdd:PLN02330 168 AADRAGDTSD---NEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANlcSSLFSVGPEMIGQVVTLGlIPFFHIYG-IT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 288 SIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIK-KAV-TGGAIVSPQLIKDV 365
Cdd:PLN02330 244 GICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlQAImTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNVEAVHSVYGLTETTAVIFQSlpGDSSD----VVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLG 440
Cdd:PLN02330 324 EAKFPGVQVQEAYGLTEHSCITLTH--GDPEKghgiAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 441 YHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEE 520
Cdd:PLN02330 402 YYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEI 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 521 VCAYVRLEEgvdPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQ----KFKLVEAFKA 583
Cdd:PLN02330 482 PAACVVINP---KAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMrrllKEKMLSINKA 545
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
72-577 |
1.24e-60 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 207.72 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFR-KLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVnvkai 150
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 iapetfktqnyyEILRDICPEisdadtgkirsekfphlrsviidsndslkgalrfddfldlaSKSEREEVakmqksilpe 230
Cdd:cd05958 83 ------------RITVALCAH-----------------------------------------ALTASDDI---------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 saCNIQFTSGTTGNPKAACLTHHNFVNN----GIHV-GNRnelEGERICVQVPMFHAFGVIISIMAALTKGA-TMVLPAA 304
Cdd:cd05958 100 --CILAFTSGTTGAPKATMHFHRDPLASadryAVNVlRLR---EDDRFVGSPPLAFTFGLGGVLLFPFGVGAsGVLLEEA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 305 gfSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVyGLTETT 384
Cdd:cd05958 175 --TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGI-GSTEMF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 385 AVIFQSLPGDSSdvvLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTtmlGYHDDEEKTKETIGNDRWLRTGDQF 464
Cdd:cd05958 252 HIFISARPGDAR---PGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 465 VLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAY 544
Cdd:cd05958 326 SRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDH 405
|
490 500 510
....*....|....*....|....*....|...
gi 24581924 545 AKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05958 406 AKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
71-580 |
6.83e-60 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 206.74 E-value: 6.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAI 150
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 IAPETFKtqnyyeilrdicpeisDADTGKIRSekfphlrsviidsndslkgalrfdDFLDLASksEREEVAKMQKSILPE 230
Cdd:PRK03640 104 ITDDDFE----------------AKLIPGISV------------------------KFAELMN--GPKEEAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SACNIQFTSGTTGNPKAACLTHHNF--------VNNGIHvgnrnelEGERICVQVPMFHAFGVIIsIMAALTKGATMVLP 302
Cdd:PRK03640 142 EVATIMYTSGTTGKPKGVIQTYGNHwwsavgsaLNLGLT-------EDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPlGRIKKAVTGGAIVSPQLIKDVRQvLNVEAVHSvYGLTE 382
Cdd:PRK03640 214 EK-FDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKE-KGIPVYQS-YGMTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 383 TTAVIFqSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFgQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGD 462
Cdd:PRK03640 290 TASQIV-TLSPEDALTKLGSAGKPLFPCELKIEKDGVVVPPF-EEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 463 QFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpasFTAETLK 542
Cdd:PRK03640 367 IGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE-----VTEEELR 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 24581924 543 AYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:PRK03640 442 HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
42-584 |
8.03e-60 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 208.75 E-value: 8.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 42 DPLVYRTIGQQLELSASNFGDVEAIVSCheGKRYSFKSLLQEADALAAGFR-KLGLQPGDAVGLWAPNYLHWYLGMMGAA 120
Cdd:PRK08974 18 NPDRYQSLVDMFEQAVARYADQPAFINM--GEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 121 RAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETF---------KTQNYYEILRDICPEISdadTGKIRSEKF--PHLR 189
Cdd:PRK08974 96 RAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFahtlekvvfKTPVKHVILTRMGDQLS---TAKGTLVNFvvKYIK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 190 SVIIDSNdsLKGALRFDDFLdlaSKSEREEVAKMQksILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHV-GNRNEL 268
Cdd:PRK08974 173 RLVPKYH--LPDAISFRSAL---HKGRRMQYVKPE--LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAkAAYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 269 --EGERICV-QVPMFHAFGVIISIMAALTKGATMVLPAagfSPKDsLQAIVNE----KCSVIHGTPTMYVDLVNTQKKLQ 341
Cdd:PRK08974 246 lhPGKELVVtALPLYHIFALTVNCLLFIELGGQNLLIT---NPRD-IPGFVKElkkyPFTAITGVNTLFNALLNNEEFQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 342 VPLGRIKKAVTGGAIVSpQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSlPGDSSDVVlNSVGHLTDHIEAKVVDAEGRC 421
Cdd:PRK08974 322 LDFSSLKLSVGGGMAVQ-QAVAERWVKLTGQYLLEGYGLTECSPLVSVN-PYDLDYYS-GSIGLPVPSTEIKLVDDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 422 VPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAH 501
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 502 PQVIEAHVIGVPDERLGEEVCAYVRLEEgvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAF 581
Cdd:PRK08974 478 PKVLEVAAVGVPSEVSGEAVKIFVVKKD----PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
...
gi 24581924 582 KAK 584
Cdd:PRK08974 554 RAK 556
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
72-587 |
1.58e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.96 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 A-----PETFKTQNYYEILRDICPEISDAdtgkirsEKFPH--LRSVIIDSNDSLKGALRFDDFLDLASKSEREEVAKMQ 224
Cdd:PRK06710 127 CldlvfPRVTNVQSATKIEHVIVTRIADF-------LPFPKnlLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 KSILPESACNI-QFTSGTTGNPKAACLTHHNFVNN---GIHvGNRNELEGERICVQV-PMFHAFGVIISIMAALTKGATM 299
Cdd:PRK06710 200 VPCDPENDLALlQYTGGTTGFPKGVMLTHKNLVSNtlmGVQ-WLYNCKEGEEVVLGVlPFFHVYGMTAVMNLSIMQGYKM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 300 VLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSvYG 379
Cdd:PRK06710 279 VL-IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEG-YG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETTAVIFQSLPGDSSdvVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWL 458
Cdd:PRK06710 357 LTESSPVTHSNFLWEKR--VPGSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 459 RTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASfta 538
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE--- 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24581924 539 ETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKETE 587
Cdd:PRK06710 511 EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
75-577 |
5.95e-59 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 202.95 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIApe 154
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 155 tfktqnyyeilrdicpeisdadtgkirsekfphlrsviiDSNDslkgalrfddfldlasksereevakmqksilpesACN 234
Cdd:cd05972 79 ---------------------------------------DAED----------------------------------PAL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERI--CVQVPMFhAFGVIISIMAALTKGATMVL-PAAGFSPKDS 311
Cdd:cd05972 86 IYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIhwNIADPGW-AKGAWSSFFGPWLLGATVFVyEGPRFDAERI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEKCSVIHGTPTMYVDLVnTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNvEAVHSVYGLTETTAVIfqsl 391
Cdd:cd05972 165 LELLERYGVTSFCGPPTAYRMLI-KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG-LPIRDGYGQTETGLTV---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 392 pGDSSDVVLN--SVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTT--MLGYHDDEEKTKETIGNDrWLRTGDQFVLE 467
Cdd:cd05972 239 -GNFPDMPVKpgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGD-YYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 468 ANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKG 547
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKK 396
|
490 500 510
....*....|....*....|....*....|
gi 24581924 548 KLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
71-586 |
8.96e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 204.37 E-value: 8.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAI 150
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 IAPETfktqnyyeiLRDICPEISDAdtgkiRSEKFPHLRSVIIDsndsLKGALRFDDFLDLASKSereevakmqkSILPE 230
Cdd:PRK08276 88 IVSAA---------LADTAAELAAE-----LPAGVPLLLVVAGP----VPGFRSYEEALAAQPDT----------PIADE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SA-CNIQFTSGTTGNPKaaclthhnfvnnGIhvgnRNELEGERI--------------------CVQV---PMFHAfGVI 286
Cdd:PRK08276 140 TAgADMLYSSGTTGRPK------------GI----KRPLPGLDPdeapgmmlallgfgmyggpdSVYLspaPLYHT-APL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 287 ISIMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLvntqkkLQVP--------LGRIKKAVTGGAiVS 358
Cdd:PRK08276 203 RFGMSALALGGTVVV-MEKFDAEEALALIERYRVTHSQLVPTMFVRM------LKLPeevrarydVSSLRVAIHAAA-PC 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 359 PQLIKdvRQVLNV--EAVHSVYGLTETTAVIF----QSL--PGdssdvvlnSVGHLTDHiEAKVVDAEGRCVPFGQPGEL 430
Cdd:PRK08276 275 PVEVK--RAMIDWwgPIIHEYYASSEGGGVTVitseDWLahPG--------SVGKAVLG-EVRILDEDGNELPPGEIGTV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 431 CVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVI 510
Cdd:PRK08276 344 YFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVF 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 511 GVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKET 586
Cdd:PRK08276 424 GVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQ 499
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
53-583 |
9.01e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 205.57 E-value: 9.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNY-----LHWYLGMMGAAragLTSv 127
Cdd:PRK08162 24 LERAAEVYPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIpamveAHFGVPMAGAV---LNT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 128 gLNPAYQGPEIAYCLNKVNVKAIIA-PEtfktqnYYEILRDICPEIsdadtgkirsekfPHLRSVIIDSND------SLK 200
Cdd:PRK08162 98 -LNTRLDAASIAFMLRHGEAKVLIVdTE------FAEVAREALALL-------------PGPKPLVIDVDDpeypggRFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 201 GALRFDDFLdlASKSEREEvakmqkSILPES---ACNIQFTSGTTGNPKAAcLTHH-----NFVNNGIHVGNRNEleger 272
Cdd:PRK08162 158 GALDYEAFL--ASGDPDFA------WTLPADewdAIALNYTSGTTGNPKGV-VYHHrgaylNALSNILAWGMPKH----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 273 iCV---QVPMFHAFGVIIS-IMAALtkGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIK 348
Cdd:PRK08162 224 -PVylwTLPMFHCNGWCFPwTVAAR--AGTNVCLRK-VDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 349 KAVTGGAIVSPQLIKDVRQvLNVEAVHsVYGLTET--TAVI------FQSLPGDSSdVVLNS---VGHLTDHiEAKVVDA 417
Cdd:PRK08162 300 HAMVAGAAPPAAVIAKMEE-IGFDLTH-VYGLTETygPATVcawqpeWDALPLDER-AQLKArqgVRYPLQE-GVTVLDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 418 E-GRCVPF-GQP-GELCVRGYTTMLGYHDDEEKTKETIGnDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEI 494
Cdd:PRK08162 376 DtMQPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 495 EDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIpIDAFPKTTSGKIQK 574
Cdd:PRK08162 455 EDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDG---ASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQK 530
|
....*....
gi 24581924 575 FKLVEAFKA 583
Cdd:PRK08162 531 FVLREQAKS 539
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
72-585 |
1.17e-58 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 204.16 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 ApetfkTQNYYEILRDICPeisdADTGKIRSEKFPHLRSVIIDSNDSLK---GALRFDDFLDLASKSEREEVAKMQKSIl 228
Cdd:PRK12406 89 A-----HADLLHGLASALP----AGVTVLSVPTPPEIAAAYRISPALLTppaGAIDWEGWLAQQEPYDGPPVPQPQSMI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 pesacniqFTSGTTGNPK----AACLTHHNFVNNGIHVGNRNELEGERICVQVPMFH----AFGviisiMAALTKGATMV 300
Cdd:PRK12406 159 --------YTSGTTGHPKgvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYG-----LRAGRLGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 LPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLvntqkkLQVPLGRIKK-------AVTGGAIVSPqliKDVRQVLnVE- 372
Cdd:PRK12406 226 LQPR-FDPEELLQLIERHRITHMHMVPTMFIRL------LKLPEEVRAKydvsslrHVIHAAAPCP---ADVKRAM-IEw 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 373 ---AVHSVYGLTETTAVIFQSlpgdsSDVVLN---SVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR--GYTTMLgYHDD 444
Cdd:PRK12406 295 wgpVIYEYYGSTESGAVTFAT-----SEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiaGNPDFT-YHNK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 445 EEKTKEtIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAY 524
Cdd:PRK12406 369 PEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAV 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 525 VRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKE 585
Cdd:PRK12406 448 VEPQPGATL---DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANA 505
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
72-583 |
5.06e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 203.47 E-value: 5.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 APEtfktqnyyeILRDICPEISDADtgkirsekfPHLRSVIIDSNDSLKGALRFDDFLdlaskseREEVAKMQKSILPE- 230
Cdd:PRK07786 120 TEA---------ALAPVATAVRDIV---------PLLSTVVVAGGSSDDSVLGYEDLL-------AEAGPAHAPVDIPNd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SACNIQFTSGTTGNPKAACLTHHNFVNNGIHV--GNRNELEGERICVQVPMFHAFGvIISIMAALTKGATMVL-PAAGFS 307
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLTGQAMTClrTNGADINSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIyPLGAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 PKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLgRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVI 387
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 388 FQsLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLE 467
Cdd:PRK07786 333 CM-LLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG-WFHSGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 468 ANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDpaSFTAETLKAYAKG 547
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDA--ALTLEDLAEFLTD 488
|
490 500 510
....*....|....*....|....*....|....*.
gi 24581924 548 KLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:PRK07786 489 RLARYKHPKALEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
230-577 |
1.78e-57 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 198.34 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 ESACNIQFTSGTTGNPKAACLTHHNFVNNGIhvGNRNEL---EGERICVQVPMFHAFGVIIsIMAALTKGATMVLPAAgF 306
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAI--GSALNLgltEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDK-F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPKDSLQAIVNEKCSVIHGTPTMYVDLVntQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQvLNVEAVHSvYGLTETTAV 386
Cdd:cd05912 153 DAEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQS-YGMTETCSQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 387 IFQSLPGDSSDVvLNSVGHLTDHIEAKVVDAEGrcvPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVL 466
Cdd:cd05912 229 IVTLSPEDALNK-IGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENG-WFKTGDIGYL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 467 EANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEgvdpaSFTAETLKAYAK 546
Cdd:cd05912 304 DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER-----PISEEELIAYCS 378
|
330 340 350
....*....|....*....|....*....|.
gi 24581924 547 GKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05912 379 EKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
91-581 |
5.29e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 200.21 E-value: 5.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 91 FRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKA-IIAPETFktqnyyeilrdic 169
Cdd:PRK06188 54 FEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTlIVDPAPF------------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 170 peisdADTGKIRSEKFPHLRSVIidsndslkGALRFDDFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAAC 249
Cdd:PRK06188 121 -----VERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 250 LTHHNFVN-NGIHVGNRNELEGERICVQVPMFHAFGVIIsiMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPT 328
Cdd:PRK06188 188 GTHRSIATmAQIQLAEWEWPADPRFLMCTPLSHAGGAFF--LPTLLRGGTVIV-LAKFDPAEVLRAIEEQRITATFLVPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 329 MYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPqlikdVRQVLNVEAVHSV----YGLTETTAVIFQSLPGD---SSDVVLN 401
Cdd:PRK06188 265 MIYALLDHPDLRTRDLSSLETVYYGASPMSP-----VRLAEAIERFGPIfaqyYGQTEAPMVITYLRKRDhdpDDPKRLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 402 SVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEM 481
Cdd:PRK06188 340 SCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-WLHTGDVAREDEDGFYYIVDRKKDM 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 482 LIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPI 561
Cdd:PRK06188 419 IVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAV---DAAELQAHVKERKGSVHAPKQVDFV 495
|
490 500
....*....|....*....|
gi 24581924 562 DAFPKTTSGKIQKFKLVEAF 581
Cdd:PRK06188 496 DSLPLTALGKPDKKALRARY 515
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
47-574 |
8.42e-57 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 199.52 E-value: 8.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIV---SCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAG 123
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIfesSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 124 LTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFktqnyYEILRdicpeisdadtgKIRSEKFPHLRSV-IIDSNDS-LKG 201
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQF-----YPMYR------------QIQQEDATPLRHIcLTRVALPaDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 202 ALRFDDFLDLASKSEREEVAkmqksILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMF 280
Cdd:PRK08008 150 VSSFTQLKAQQPATLCYAPP-----LSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALrDDDVYLTVMPAF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 281 HAFGVIISIMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVntqkkLQVPLGRIK----KAVTGGAI 356
Cdd:PRK08008 225 HIDCQCTAAMAAFSAGATFVL-LEKYSARAFWGQVCKYRATITECIPMMIRTLM-----VQPPSANDRqhclREVMFYLN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 357 VSPQLIKDVRQVLNVEAVHSvYGLTETTAVIFQSLPGDSSDvvLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGY- 435
Cdd:PRK08008 299 LSDQEKDAFEERFGVRLLTS-YGMTETIVGIIGDRPGDKRR--WPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 436 --TTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVP 513
Cdd:PRK08008 376 gkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 514 DERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK08008 456 DSIRDEAIKAFVVLNEG---ETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIK 513
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
43-579 |
1.07e-56 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 199.68 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 43 PLVYRTIGQQLELSAS---NFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGA 119
Cdd:cd17642 10 PLEDGTAGEQLHKAMKryaSVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 120 ARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIapetfktqnyyeilrdiCPEISDADTGKIRSeKFPHLRSVII-DSNDS 198
Cdd:cd17642 90 LFIGVGVAPTNDIYNERELDHSLNISKPTIVF-----------------CSKKGLQKVLNVQK-KLKIIKTIIIlDSKED 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 199 LKGALRFDDFldlasKSEREEVAKMQKSILPESACN------IQFTSGTTGNPKAACLTHHNFVNNGIH-----VGNRnE 267
Cdd:cd17642 152 YKGYQCLYTF-----ITQNLPPGFNEYDFKPPSFDRdeqvalIMNSSGSTGLPKGVQLTHKNIVARFSHardpiFGNQ-I 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 268 LEGERICVQVPMFHAFGVIISImAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRI 347
Cdd:cd17642 226 IPDTAILTVIPFHHGFGMFTTL-GYLICGFRVVL-MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 KKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDvvlNSVGHLTDHIEAKVVDAE-GRCVPFGQ 426
Cdd:cd17642 304 HEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDDKP---GAVGKVVPFFYAKVVDLDtGKTLGPNE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 427 PGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIE 506
Cdd:cd17642 381 RGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFD 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 507 AHVIGVPDERLGEEVCAYVRLEEGVdpaSFTAETLKAYAKGKLAHFKVPR-YVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd17642 461 AGVAGIPDEDAGELPAAVVVLEAGK---TMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
47-572 |
2.23e-56 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 197.73 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIapetfktqnyYEILRDICPEISDADTGKIRSEKFPHLRSVIIDSndslkgalrfd 206
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAV----------IAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAG----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 dflDLASKSEREevakmqksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGI----HVGNRNElEGERICVQVPMFHA 282
Cdd:cd05923 140 ---PLIEDPPRE----------PEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLfmstQAGLRHG-RHNVVLGLMPLYHV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 283 FGVIISIMAALTKGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLI 362
Cdd:cd05923 206 IGFFAVLVAALALDGTYVVVEE-FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQVLNVEAVhSVYGLTETTAVIFQS--------LPGDSSDVVLNSVGHLTDHIeakvvdaegrcVPFGQPGELCVR- 433
Cdd:cd05923 285 ERVNQHLPGEKV-NIYGTTEAMNSLYMRdartgtemRPGFFSEVRIVRIGGSPDEA-----------LANGEEGELIVAa 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 434 -GYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV 512
Cdd:cd05923 353 aADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 513 PDERLGEEVCAYVRLEEGvdpaSFTAETLKAYAK-GKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05923 432 ADERWGQSVTACVVPREG----TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKV 488
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
70-583 |
2.64e-56 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 197.79 E-value: 2.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWA---PNYLHWYLGmmgAARAGLTSVGLNPAYQGPEIAYCLNKVN 146
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVeksPEALALYLA---TLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 147 VKAII-APETFktqnyyEILRDICP-------EISDAD-TGKI--RSEKFPhlrsviidsnDSLKGALRFDDflDLASks 215
Cdd:PRK07514 101 PALVVcDPANF------AWLSKIAAaagaphvETLDADgTGSLleAAAAAP----------DDFETVPRGAD--DLAA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 216 ereevakmqksilpesacnIQFTSGTTGNPKAACLTHHNFVNNGI------HVGnrnelEGERICVQVPMFHAFGVIISI 289
Cdd:PRK07514 161 -------------------ILYTSGTTGRSKGAMLSHGNLLSNALtlvdywRFT-----PDDVLIHALPIFHTHGLFVAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 290 MAALTKGATMVlpaagFSPKDSLQAIVNE--KCSVIHGTPTMYVDLvntqkkLQVPlgRIKKAVTGGA--IVS---PQLI 362
Cdd:PRK07514 217 NVALLAGASMI-----FLPKFDPDAVLALmpRATVMMGVPTFYTRL------LQEP--RLTREAAAHMrlFISgsaPLLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQVlnvEAV--HSV---YGLTETtaVIFQSLPGDSsDVVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYT 436
Cdd:PRK07514 284 ETHREF---QERtgHAIlerYGMTET--NMNTSNPYDG-ERRAGTVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGPN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDER 516
Cdd:PRK07514 358 VFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 517 LGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:PRK07514 438 FGEGVTAVVVPKPG---AALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
238-577 |
5.84e-56 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 192.70 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 238 TSGTTGNPKAACLTHHNFVNNGiHVGNRNELEGER--ICVQVPMFHAFGVIISIMAALTKGATMVLPA-AGFSPK---DS 311
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNA-WMLALNSLFDPDdvLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpAGYRNPglfDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNE-KCSVIHGTPTMYVDLvntqkkLQVPLGR----IKKAVTGGAIVSPQLIKDVRQVLNVEAVHsVYGLTETTAV 386
Cdd:cd05944 89 FWKLVERyRITSLSTVPTVYAAL------LQVPVNAdissLRFAMSGAAPLPVELRARFEDATGLPVVE-GYGLTEATCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 387 IFQSLPGdsSDVVLNSVGHLTDHIEAKVV--DAEGR----CVPfGQPGELCVRGYTTMLGYHDDEEKtKETIGNDRWLRT 460
Cdd:cd05944 162 VAVNPPD--GPKRPGSVGLRLPYARVRIKvlDGVGRllrdCAP-DEVGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 461 GDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAET 540
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG---AVVEEEE 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 24581924 541 LKAYAKGKLAH-FKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05944 315 LLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
55-579 |
1.41e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 196.50 E-value: 1.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 55 LSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQ 134
Cdd:PRK06164 16 LDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 135 GPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPeisDADtgkirsekfPHLRSVII--DSNDSLKGALRFDDFlDLA 212
Cdd:PRK06164 96 SHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPP---DAL---------PPLRAIAVvdDAADATPAPAPGARV-QLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SKSEREEVAKMQKSILPESACNIQFT-SGTTGNPK------AACLTHHNFVNNGIHVGNrneleGERICVQVPMFHAFGv 285
Cdd:PRK06164 163 ALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGYDP-----GAVLLAALPFCGVFG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 IISIMAALTKGATMVLPAAgFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQvPLGRIKkaVTGGAIVSPQLiKDV 365
Cdd:PRK06164 237 FSTLLGALAGGAPLVCEPV-FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSAR--LFGFASFAPAL-GEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNVEAV--HSVYGLTETTA-VIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGY 441
Cdd:PRK06164 312 AALARARGVplTGLYGSSEVQAlVALQPATDPVSVRIEGGGRPASPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 442 HDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVpdERLGEEV 521
Cdd:PRK06164 392 LDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTV 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 522 C-AYVRLEEGVDPAsftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSG---KIQKFKLVE 579
Cdd:PRK06164 470 PvAFVIPTDGASPD---EAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
61-577 |
4.57e-55 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 193.96 E-value: 4.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 61 GDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAY 140
Cdd:cd12117 11 PDAVAVV--YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 141 clnkvnvkaiiapetfktqnyyeILRDicpeiSDAdtgkirsekfphlrSVIIDSNdSLKGALRFDDFLDLASKSEREEV 220
Cdd:cd12117 89 -----------------------MLAD-----AGA--------------KVLLTDR-SLAGRAGGLEVAVVIDEALDAGP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 221 AKMQKSIL-PESACNIQFTSGTTGNPKAACLTHHN---FVNNGIHVGnrnELEGERICVQVPM-FHAFGviISIMAALTK 295
Cdd:cd12117 126 AGNPAVPVsPDDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTNYVT---LGPDDRVLQTSPLaFDAST--FEIWGALLN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 296 GATMVL--PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNtqkklQVP--LGRIKKAVTGGAIVSPQLikdVRQVLNV 371
Cdd:cd12117 201 GARLVLapKGTLLDPDALGALIAEEGVTVLWLTAALFNQLAD-----EDPecFAGLRELLTGGEVVSPPH---VRRVLAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 372 EA---VHSVYGLTETT--AVIFQSLPGDSSDVVLnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEE 446
Cdd:cd12117 273 CPglrLVNGYGPTENTtfTTSHVVTELDEVAGSI-PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 447 KTKET------IGNDRWLRTGDQFVLEANGYGRIVGRL-KEMLIRGgENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:cd12117 352 LTAERfvadpfGPGERLYRTGDLARWLPDGRLEFLGRIdDQVKIRG-FRIELGEIEAALRAHPGVREAVVVVREDAGGDK 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 520 EVCAYVRLEEGVDPASftaetLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd12117 431 RLVAYVVAEGALDAAE-----LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
53-580 |
8.97e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 194.10 E-value: 8.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:PRK07470 13 LRQAARRFPDRIALV--WGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFktQNYYEILRDICPEISdadtgkirsekfphlRSVIIDSNDslkGALRFDDFL--D 210
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADF--PEHAAAVRAASPDLT---------------HVVAIGGAR---AGLDYEALVarH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASKSEREEVAKmqksilpESACNIQFTSGTTGNPKAACLTHHN--FV-NNgiHVGNRNELEGERIC--VQVPMFHAFGv 285
Cdd:PRK07470 151 LGARVANAAVDH-------DDPCWFFFTSGTTGRPKAAVLTHGQmaFViTN--HLADLMPGTTEQDAslVVAPLSHGAG- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 iISIMAALTKGATMVLPAA-GFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD 364
Cdd:PRK07470 221 -IHQLCQVARGAATVLLPSeRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 365 VRQVLNVEAVHsVYGLTETTAVI------FQSlPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTM 438
Cdd:PRK07470 300 ALAKLGKVLVQ-YFGLGEVTGNItvlppaLHD-AEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 439 LGYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLG 518
Cdd:PRK07470 378 AGYYNNPEANAKAFRDG-WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWG 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 519 EEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKfKLVEA 580
Cdd:PRK07470 457 EVGVAVCVARDGAPV---DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK-KMVRE 514
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
76-577 |
1.36e-54 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 191.51 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPET 155
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 FKTQNyyeILRDICPEISdadtgkirsekFPHLRSVIIDSNDSLKgalrfddflDLASksereevakmqksilpesacnI 235
Cdd:TIGR01923 81 LEEKD---FQADSLDRIE-----------AAGRYETSLSASFNMD---------QIAT---------------------L 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFVNNGihVGNRNEL---EGERICVQVPMFHAFGVIIsIMAALTKGATMVLPAaGFSpkDSL 312
Cdd:TIGR01923 117 MFTSGTTGKPKAVPHTFRNHYASA--VGSKENLgftEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVD-KFN--QLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMyvdLVNTQKKLQVPLgRIKKAVTGGAIVSPQLIKDVRQvLNVEaVHSVYGLTETTAVIFQSLP 392
Cdd:TIGR01923 191 EMIANERVTHISLVPTQ---LNRLLDEGGHNE-NLRKILLGGSAIPAPLIEEAQQ-YGLP-IYLSYGMTETCSQVTTATP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDSSDVVlnSVGHLTDHIEAKVVDAEGRCVpfgqpGELCVRGYTTMLGYHDDEEKTkETIGNDRWLRTGDQFVLEANGYG 472
Cdd:TIGR01923 265 EMLHARP--DVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDpasftAETLKAYAKGKLAHF 552
Cdd:TIGR01923 337 YVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDIS-----QAKLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 24581924 553 KVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
49-574 |
1.54e-54 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 194.25 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 49 IGQQLELSASNFGDveAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN---YLHWYLGMmgaARAGLT 125
Cdd:PLN02860 9 ICQCLTRLATLRGN--AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNsdlYLEWLLAV---ACAGGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 126 SVGLNPAYQGPEIAYCLNKVNVKAIIAPETfkTQNYYEilrdicpeisdadtgKIRSEKFPHLRSVIIDSNDSLKGALRF 205
Cdd:PLN02860 84 VAPLNYRWSFEEAKSAMLLVRPVMLVTDET--CSSWYE---------------ELQNDRLPSLMWQVFLESPSSSVFIFL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 206 DDFLDLASKSEREEVAK-MQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNG---IHVGNRNELEgericVQV---P 278
Cdd:PLN02860 147 NSFLTTEMLKQRALGTTeLDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSlakIAIVGYGEDD-----VYLhtaP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 279 MFHaFGVIISIMAALTKGATMV-LPAagFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGR--IKKAVTGGA 355
Cdd:PLN02860 222 LCH-IGGLSSALAMLMVGACHVlLPK--FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFpsVRKILNGGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 356 IVSPQLIKDVRQVLNVEAVHSVYGLTET-TAVIFQSL---PGDSSDVVLNSVGHLTDhieAKVVDAEGRCVpfGQP---- 427
Cdd:PLN02860 299 SLSSRLLPDAKKLFPNAKLFSAYGMTEAcSSLTFMTLhdpTLESPKQTLQTVNQTKS---SSVHQPQGVCV--GKPaphv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 428 ------------GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDqfVLEANGYGRI--VGRLKEMLIRGGENIFPKE 493
Cdd:PLN02860 374 elkigldessrvGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGD--IGWIDKAGNLwlIGRSNDRIKTGGENVYPEE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 494 IEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEG-----------VDPASFTAETLKAYAKGK-LAHFKVPR-YVIP 560
Cdd:PLN02860 452 VEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenaKKNLTLSSETLRHHCREKnLSRFKIPKlFVQW 531
|
570
....*....|....
gi 24581924 561 IDAFPKTTSGKIQK 574
Cdd:PLN02860 532 RKPFPLTTTGKIRR 545
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
48-571 |
5.77e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 192.02 E-value: 5.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 48 TIGQQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSV 127
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALV--CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 128 GLNPAYQGPEIAYCLNKVNVKAIIapetfktqnyYEilRDICPEISDAdtgkirSEKFPHLRSVII----DSNDSLKGAL 203
Cdd:PRK07798 82 NVNYRYVEDELRYLLDDSDAVALV----------YE--REFAPRVAEV------LPRLPKLRTLVVvedgSGNDLLPGAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 204 RFDDFLDlASKSEREevakmqksILPESACNIQF--TSGTTGNPKAACLTHHNFVN---NGI-------------HVGNR 265
Cdd:PRK07798 144 DYEDALA-AGSPERD--------FGERSPDDLYLlyTGGTTGMPKGVMWRQEDIFRvllGGRdfatgepiedeeeLAKRA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 266 NELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIhgtpTMYVD-----LVNT-QKK 339
Cdd:PRK07798 215 AAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVI----TIVGDamarpLLDAlEAR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 340 LQVPLGRIKKAVTGGAIVSPQlIKD--VRQVLNVEAVHSvYGLTET----TAVIFQSLPGDSSDVVlnSVGHLTdhieaK 413
Cdd:PRK07798 291 GPYDLSSLFAIASGGALFSPS-VKEalLELLPNVVLTDS-IGSSETgfggSGTVAKGAVHTGGPRF--TIGPRT-----V 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 414 VVDAEGRCVPFG--QPGELCVRGYTTmLGYHDDEEKTKET---IGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGEN 488
Cdd:PRK07798 362 VLDEDGNPVEPGsgEIGWIARRGHIP-LGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 489 IFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTT 568
Cdd:PRK07798 441 VFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG---ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSP 517
|
...
gi 24581924 569 SGK 571
Cdd:PRK07798 518 AGK 520
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
76-577 |
4.47e-53 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 187.28 E-value: 4.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYclnkvnvkaiiapet 155
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAY--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 fktqnyyeILRDIcpeisdadtgkirsekfpHLRSVIIDSNDslkgalrfddfldlasksereevakmqksilpesACNI 235
Cdd:cd05919 77 --------IARDC------------------EARLVVTSADD----------------------------------IAYL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFVNNGIHVGnRNEL---EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSL 312
Cdd:cd05919 97 LYSSGTTGPPKGVMHAHRDPLLFADAMA-REALgltPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVyGLTETTAVIFQSLP 392
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI-GATEVGHIFLSNRP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDssdVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYG 472
Cdd:cd05919 255 GA---WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWY 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHF 552
Cdd:cd05919 331 THAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAH 410
|
490 500
....*....|....*....|....*
gi 24581924 553 KVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05919 411 KVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
72-579 |
5.02e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 190.25 E-value: 5.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 APETFktqnyYEILRDICPEISdadtgkirsekfphLRSVIIDS-------------NDSLKGA-LRFDDFLDLASKSER 217
Cdd:PRK06178 136 ALDQL-----APVVEQVRAETS--------------LRHVIVTSladvlpaeptlplPDSLRAPrLAAAGAIDLLPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 218 EEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFV-----NNGIHVGNRnelEGERICVQVPMF----HAFGVIIS 288
Cdd:PRK06178 197 CTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAVVGG---EDSVFLSFLPEFwiagENFGLLFP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 289 IMAaltkGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQ-------------------KKLQVPLGRIKK 349
Cdd:PRK06178 274 LFS----GATLVL-LARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPrfaeydlsslrqvrvvsfvKKLNPDYRQRWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 350 AVTGGAIVspqlikdvrqvlnvEAVhsvYGLTET-TAVIFQS-LPGDSSDvvLNS----VGHLTDHIEAKVVDAE-GRCV 422
Cdd:PRK06178 349 ALTGSVLA--------------EAA---WGMTEThTCDTFTAgFQDDDFD--LLSqpvfVGLPVPGTEFKICDFEtGELL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 423 PFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHP 502
Cdd:PRK06178 410 PLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 503 QVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIpIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK06178 489 AVLGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQA 561
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
62-579 |
6.16e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 188.75 E-value: 6.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 62 DVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYC 141
Cdd:PRK13391 12 DKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 142 LNKVNVKAIIapeTFKTQnyyeilRDICPEISdadtgkirsEKFPHLR-SVIIDSNDSLKGALRFDDFLDLASK----SE 216
Cdd:PRK13391 92 VDDSGARALI---TSAAK------LDVARALL---------KQCPGVRhRLVLDGDGELEGFVGYAEAVAGLPAtpiaDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 217 REEVAkmqksilpesacnIQFTSGTTGNPKA-----------ACLTHHNFVNNGIHVGnrnelEGERICVQVPMFHAfGV 285
Cdd:PRK13391 154 SLGTD-------------MLYSSGTTGRPKGikrplpeqppdTPLPLTAFLQRLWGFR-----SDMVYLSPAPLYHS-AP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 IISIMAALTKGATMVLPAAgFSPKDSLQAIvnEKCSVIHG--TPTMYVdlvntqKKLQVP--------LGRIKKAVTGGA 355
Cdd:PRK13391 215 QRAVMLVIRLGGTVIVMEH-FDAEQYLALI--EEYGVTHTqlVPTMFS------RMLKLPeevrdkydLSSLEVAIHAAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 356 IVSPQlIKdvRQVLNV--EAVHSVYGLTE---TTAVifqslpgDSSDVVLN--SVGHL---TDHIeakvVDAEGRCVPFG 425
Cdd:PRK13391 286 PCPPQ-VK--EQMIDWwgPIIHEYYAATEglgFTAC-------DSEEWLAHpgTVGRAmfgDLHI----LDDDGAELPPG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 426 QPGELCVRGyTTMLGYHDDEEKTKETIGNDR-WLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQV 504
Cdd:PRK13391 352 EPGTIWFEG-GRPFEYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 505 IEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK13391 431 ADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
43-582 |
7.51e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 189.15 E-value: 7.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 43 PLvyrTIGQQLELSASNFGDVEaIVSCH-EGK--RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN-YLHW--YLGM 116
Cdd:PRK07008 9 PL---LISSLIAHAARHAGDTE-IVSRRvEGDihRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNgYRHLeaYYGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 117 MGAARAGLTsvgLNPAYQGPEIAYCLNKVNVKAIIAPETFKTqnYYEILRDICPE----ISDADTGKIRSEKFPHL-RSV 191
Cdd:PRK07008 85 SGSGAVCHT---INPRLFPEQIAYIVNHAEDRYVLFDLTFLP--LVDALAPQCPNvkgwVAMTDAAHLPAGSTPLLcYET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 192 IIDSNDSLKGALRFDDfldlasksereevakmqksilpESACNIQFTSGTTGNPKAACLTH-----HNF---VNNGIHVG 263
Cdd:PRK07008 160 LVGAQDGDYDWPRFDE----------------------NQASSLCYTSGTTGNPKGALYSHrstvlHAYgaaLPDAMGLS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 264 NRNElegerICVQVPMFH--AFGVIISimAALTkGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQ 341
Cdd:PRK07008 218 ARDA-----VLPVVPMFHvnAWGLPYS--APLT-GAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 342 VPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSvYGLTE-----TTAVI---FQSLPGDSSDVVLNSVGHLTDHIEAK 413
Cdd:PRK07008 290 LRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHA-WGMTEmsplgTLCKLkwkHSQLPLDEQRKLLEKQGRVIYGVDMK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 414 VVDAEGRCVPF-GQP-GELCVRGYTTMLGYHDDEEKTKEtignDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFP 491
Cdd:PRK07008 369 IVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDASPLV----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 492 KEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDpasFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:PRK07008 445 IDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE---VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGK 521
|
570
....*....|.
gi 24581924 572 IQKFKLVEAFK 582
Cdd:PRK07008 522 LQKLKLREQFR 532
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
74-580 |
1.38e-52 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 187.74 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAP 153
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 ETFKtqnyyeilrdicPEISDADTgkirseKFPHLRSVIIdSNDSLKGALRFDDFLdlASKSEREEVAKMQksilPESAC 233
Cdd:TIGR02262 110 GALL------------PVIKAALG------KSPHLEHRVV-VGRPEAGEVQLAELL--ATESEQFKPAATQ----ADDPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 NIQFTSGTTGNPKAACLTHHN-FVNNGIHVGNRNELEGERICVQVP-MFHAFGVIISIMAALTKGATMVLPAAGFSPKDS 311
Cdd:TIGR02262 165 FWLYSSGSTGMPKGVVHTHSNpYWTAELYARNTLGIREDDVCFSAAkLFFAYGLGNALTFPMSVGATTVLMGERPTPDAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVyGLTETTAVIFQSL 391
Cdd:TIGR02262 245 FDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGI-GSTEMLHIFLSNL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 392 PGDssdVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEANGY 471
Cdd:TIGR02262 324 PGD---VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE-WTRSGDKYVRNDDGS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 472 GRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGKLAH 551
Cdd:TIGR02262 400 YTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG---QTALETELKEHVKDRLAP 476
|
490 500
....*....|....*....|....*....
gi 24581924 552 FKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:TIGR02262 477 YKYPRWIVFVDDLPKTATGKIQRFKLREG 505
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
76-572 |
2.15e-52 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 188.04 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPET 155
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 FKtqnyyeilrDICPEISDADTGKIRSEKFPhlrsviidsndslkgalrfDDFLDLASKSEREEVAKMQKSILPESACNI 235
Cdd:PRK13382 150 FS---------ATVDRALADCPQATRIVAWT-------------------DEDHDLTVEVLIAAHAGQRPEPTGRKGRVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PMFHAFGvIISIMAALTKGATMVLPAAgFSPKDSLQA 314
Cdd:PRK13382 202 LLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVaPMFHAWG-FSQLVLAASLACTIVTRRR-FDPEATLDL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 315 IVNEKCSVIHGTPTMY---VDLVntQKKLQVPLGR-IKKAVTGGAIVSPQLikdVRQVLNV--EAVHSVYGLTETtAVIF 388
Cdd:PRK13382 280 IDRHRATGLAVVPVMFdriMDLP--AEVRNRYSGRsLRFAAASGSRMRPDV---VIAFMDQfgDVIYNNYNATEA-GMIA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 389 QSLPGDSSdVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYhdDEEKTKETIgnDRWLRTGDQFVLEA 468
Cdd:PRK13382 354 TATPADLR-AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH--DGFMASGDVGYLDE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 469 NGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGK 548
Cdd:PRK13382 429 NGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDN 505
|
490 500
....*....|....*....|....
gi 24581924 549 LAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK13382 506 LANYKVPRDIVVLDELPRGATGKI 529
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
43-582 |
1.18e-51 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 186.11 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 43 PLVYRTIgqqLELSASNFGDVEAIVSCHEGK--RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPN-YLH---WYlGM 116
Cdd:PRK06018 9 PLLCHRI---IDHAARIHGNREVVTRSVEGPivRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNtWRHleaWY-GI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 117 MGAaraGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFktqnyYEILRDICPeisdadtgkirseKFPHLRSVIIDSN 196
Cdd:PRK06018 85 MGI---GAICHTVNPRLFPEQIAWIINHAEDRVVITDLTF-----VPILEKIAD-------------KLPSVERYVVLTD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 197 DS------LKGALRFDDFLDLASKSEReevakmQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-- 268
Cdd:PRK06018 144 AAhmpqttLKNAVAYEEWIAEADGDFA------WKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALgt 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 269 -EGERICVQVPMFHA--FGVIISimaALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLG 345
Cdd:PRK06018 218 sAADTMLPVVPLFHAnsWGIAFS---APSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 346 RIKKAVTGGAIVSPQLIKdVRQVLNVEAVHSvYGLTETTAV--------IFQSLPGDSSDVVLNSVGHLTDHIEAKVVDA 417
Cdd:PRK06018 295 HLKMVVCGGSAMPRSMIK-AFEDMGVEVRHA-WGMTEMSPLgtlaalkpPFSKLPGDARLDVLQKQGYPPFGVEMKITDD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 418 EGRCVPF-GQ-PGELCVRGYTTMLGYHDDEektKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIE 495
Cdd:PRK06018 373 AGKELPWdGKtFGRLKVRGPAVAAAYYRVD---GEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 496 DFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKF 575
Cdd:PRK06018 450 NLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETA---TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKT 526
|
....*..
gi 24581924 576 KLVEAFK 582
Cdd:PRK06018 527 ALREQFK 533
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
56-583 |
1.78e-51 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 185.82 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 56 SASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRK-LGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQ 134
Cdd:PLN02574 48 SHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 135 GPEIAYCLNKVNVK-AIIAPETfktqnyyeilrdicpeisdadtgkirSEKFPHLRSVII---DSNDSLKGALRFDDFLD 210
Cdd:PLN02574 128 LGEIKKRVVDCSVGlAFTSPEN--------------------------VEKLSPLGVPVIgvpENYDFDSKRIEFPKFYE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASksEREEVAkMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNN-GIHVGNRNELEGERICVQV-----PMFHAFG 284
Cdd:PLN02574 182 LIK--EDFDFV-PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvELFVRFEASQYEYPGSDNVylaalPMFHIYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 285 VIISIMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKL-QVPLGRIKKAVTGGAIVSPQLIK 363
Cdd:PLN02574 259 LSLFVVGLLSLGSTIVV-MRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVcGEVLKSLKQVSCGAAPLSGKFIQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 364 DVRQVL-NVEAVHSvYGLTETTAVifqSLPGDSSDVVLN--SVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTML 439
Cdd:PLN02574 338 DFVQTLpHVDFIQG-YGMTESTAV---GTRGFNTEKLSKysSVGLLAPNMQAKVVDWStGCLLPPGNCGELWIQGPGVMK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 440 GYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:PLN02574 414 GYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 520 EVCAYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:PLN02574 494 IPVAFVVRRQG---STLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
53-581 |
3.58e-51 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 184.32 E-value: 3.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEIS-DADTGKIRSEKFPHLRSVIIDSND-SLKGALRFDDFLd 210
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNvGGDSGPSGGTLSVHLDAATEPTPAtSTPEGLRPDDAM- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 lasksereevakmqksilpesacnIQFTSGTTGNPKAACLTHHNFVNN--GIHVGNRNELEGERICVqVPMFHAFGVIIS 288
Cdd:PRK05852 181 ------------------------IMFTGGTTGLPKMVPWTHANIASSvrAIITGYRLSPRDATVAV-MPLYHGHGLIAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 289 IMAALTKGATMVLPAAG-FSPKDSLQAIVNEKCSVIHGTPTMYVDLVntQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQ 367
Cdd:PRK05852 236 LLATLASGGAVLLPARGrFSAHTFWDDIKAVGATWYTAVPTIHQILL--ERAATEPSGRKPAALRFIRSCSAPLTAETAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 368 VLNVE---AVHSVYGLTETTAVIFQSL---------PGDSSDVVLNSVGhltdhIEAKVVDAEGRCVPFGQPGELCVRGY 435
Cdd:PRK05852 314 ALQTEfaaPVVCAFGMTEATHQVTTTQiegigqtenPVVSTGLVGRSTG-----AQIRIVGSDGLPLPAGAVGEVWLRGT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 436 TTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDE 515
Cdd:PRK05852 389 TVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQ 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 516 RLGEEVCAYVRLEEgvdPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAF 581
Cdd:PRK05852 468 LYGEAVAAVIVPRE---SAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
233-574 |
3.62e-51 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 179.06 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 CNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERIC-VQVPMFHAFGVIISIMAALTkGATMVLPaagfspkDS 311
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWlLSLPLYHVGGLAILVRSLLA-GAELVLL-------ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEkcsvIHGTPTMYVDLVNTQkkLQ---------VPLGRIKKAVTGGAIVSPQLIKDVRQvLNVEaVHSVYGLTE 382
Cdd:cd17630 75 NQALAED----LAPPGVTHVSLVPTQ--LQrlldsgqgpAALKSLRAVLLGGAPIPPELLERAAD-RGIP-LYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 383 TTAVIFQSLPGDSSDvvlNSVGHLTDHIEAKVVDaegrcvpfgqPGELCVRGYTTMLGYHDDEEKTKETigNDRWLRTGD 462
Cdd:cd17630 147 TASQVATKRPDGFGR---GGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPEFN--EDGWFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 463 QFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPAsftaeTLK 542
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA-----ELR 286
|
330 340 350
....*....|....*....|....*....|..
gi 24581924 543 AYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDR 318
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
70-574 |
1.45e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 179.31 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKA 149
Cdd:PRK06145 23 YRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 IIAPETFKTQNYYEILRDICPEISDADTGKIRSekfPHlrsviidsndslkgalrfddfldlaskserEEVAKMQKSiLP 229
Cdd:PRK06145 103 LLVDEEFDAIVALETPKIVIDAAAQADSRRLAQ---GG------------------------------LEIPPQAAV-AP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 ESACNIQFTSGTTGNPKAACLTHHNFVNNGI-HVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLpAAGFSP 308
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIdHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRI-HREFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 309 KDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIF 388
Cdd:PRK06145 228 EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 389 QSLPGDSSDVVlNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEA 468
Cdd:PRK06145 308 LMEAGREIEKI-GSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 469 NGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKGK 548
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG---ATLTLEALDRHCRQR 462
|
490 500
....*....|....*....|....*.
gi 24581924 549 LAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLK 488
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
57-572 |
3.98e-49 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 179.02 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 57 ASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGP 136
Cdd:PLN02246 33 LSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 137 EIAYCLNKVNVKAIIapetfkTQN-YYEILRDICPEisdadtgkirsekfPHLRSVIIDSNdsLKGALRFDDFLDlASKS 215
Cdd:PLN02246 113 EIAKQAKASGAKLII------TQScYVDKLKGLAED--------------DGVTVVTIDDP--PEGCLHFSELTQ-ADEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 216 EREEVakmqkSILPESACNIQFTSGTTGNPKAACLTHHNFV------------NNGIHVGNRnelegeRICVqVPMFHAF 283
Cdd:PLN02246 170 ELPEV-----EISPDDVVALPYSSGTTGLPKGVMLTHKGLVtsvaqqvdgenpNLYFHSDDV------ILCV-LPMFHIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 284 GVIISIMAALTKGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIK 363
Cdd:PLN02246 238 SLNSVLLCGLRVGAAILI-MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 364 DVRQVLNVEAVHSVYGLTETTAVIFQSL----------PGDSSDVVLNSvghltdhiEAKVVDAE-GRCVPFGQPGELCV 432
Cdd:PLN02246 317 AFRAKLPNAVLGQGYGMTEAGPVLAMCLafakepfpvkSGSCGTVVRNA--------ELKIVDPEtGASLPRNQPGEICI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 433 RGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV 512
Cdd:PLN02246 389 RGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPM 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 513 PDERLGEEVCAYVRLEEGVDpasFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PLN02246 469 KDEVAGEVPVAFVVRSNGSE---ITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKI 525
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
233-572 |
7.89e-49 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 172.59 E-value: 7.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 CNIQFTSGTTGNPKAACLTHHNFV------NNGIHVGNRNelegeRICVQVPMFHAfGVIISIMAALTKGATMVLpAAGF 306
Cdd:cd17633 3 FYIGFTSGTTGLPKAYYRSERSWIesfvcnEDLFNISGED-----AILAPGPLSHS-LFLYGAISALYLGGTFIG-QRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQkklqVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAV 386
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTMLQALARTL----EPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 387 IFqSLPGDSSDVvlNSVGHLTDHIEAKVVDAEGRCVpfgqpGELCVRGYTTMLGYHDDEEktketIGNDRWLRTGDQFVL 466
Cdd:cd17633 152 TY-NFNQESRPP--NSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 467 EANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasftaeTLKAYAK 546
Cdd:cd17633 219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYK------QLKRFLK 292
|
330 340
....*....|....*....|....*.
gi 24581924 547 GKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
235-572 |
8.94e-48 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 170.14 E-value: 8.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PMFHAFGVIISiMAALTKGATMVLpAAGFSPKDSLQ 313
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMlPLFHIAGLNLA-LATFHAGGANVV-MEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 314 AIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKkAVTGgaIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVI----FQ 389
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR-HVLG--LDAPETIQRFEETTGA-TFWSLYGQTETSGLVtlspYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 390 SLPGdssdvvlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEAN 469
Cdd:cd17637 159 ERPG--------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-WHHTGDLGRFDED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 470 GYGRIVGRL--KEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAYAKG 547
Cdd:cd17637 230 GYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG---ATLTADELIEFVGS 306
|
330 340
....*....|....*....|....*
gi 24581924 548 KLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17637 307 RIARYKKPRYVVFVEALPKTADGSI 331
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
75-585 |
9.64e-48 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 173.07 E-value: 9.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYqGPE-IAYCLNKVNVKAIIAp 153
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAF-GPEaIRDRLENSEAKVLIT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 etfkTQNYYEilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevaKMQksilPESAC 233
Cdd:cd05969 79 ----TEELYE----------------------------------------------------------RTD----PEDPT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 NIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERI--CVQVPMFHAfGVIISIMAALTKGATMVLPAAGFSPKDS 311
Cdd:cd05969 93 LLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIywCTADPGWVT-GTVYGIWAPWLNGVTNVVYEGRFDAESW 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEKCSVIHGTPTMYVDLVNTQKKL--QVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTAVIFQ 389
Cdd:cd05969 172 YGIIERVKVTVWYTAPTAIRMLMKEGDELarKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTETGSIMIA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 390 SLPGdsSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR-GYTTML-GYHDDEEKTKETIgNDRWLRTGDQFVLE 467
Cdd:cd05969 251 NYPC--MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKpGWPSMFrGIWNDEERYKNSF-IDGWYLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 468 ANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKG 547
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQ 407
|
490 500 510
....*....|....*....|....*....|....*...
gi 24581924 548 KLAHFKVPRYVIPIDAFPKTTSGKIQKfklvEAFKAKE 585
Cdd:cd05969 408 KLGAHVAPREIEFVDNLPKTRSGKIMR----RVLKAKE 441
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
76-572 |
3.09e-46 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 169.82 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKlGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII---- 151
Cdd:cd05909 9 TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLtskq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 ----APETFKTQNYYEI----LRDICPEISDADtgKIRSekfphlrsviidsndSLKGALRFDDFLDLASKSEREevakm 223
Cdd:cd05909 88 fiekLKLHHLFDVEYDArivyLEDLRAKISKAD--KCKA---------------FLAGKFPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATMVLP 302
Cdd:cd05909 146 -----PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPnPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPlgRIKKAVTGGAIVSP---QLIKDVRQVLNVEAvhsvYG 379
Cdd:cd05909 221 PNPLDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFS--SLRLVVAGAEKLKDtlrQEFQEKFGIRILEG----YG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETTAVIFQSLPgdSSDVVLNSVGHLTDHIEAKVVDAEGRC-VPFGQPGELCVRGYTTMLGYHDDEEKTKETIGnDRWL 458
Cdd:cd05909 295 TTECSPVISVNTP--QSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFG-DGWY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 459 RTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAH-PQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpasfT 537
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDT------D 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 24581924 538 AETLKAYAK-GKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05909 446 PSSLNDILKnAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
57-581 |
5.40e-46 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 170.50 E-value: 5.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 57 ASNFGDVEAIV----SCHEGKRYSFKSLLQEADALAAGFRKLGlQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVglnPA 132
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQgPEIAyclnkvnvkaiiaPETFKTQNyyeILRDICPEISDADTGKIrsekfPHLRSVIIDSNDSLKGALRFDDFLDLA 212
Cdd:cd05931 79 PP-PTPG-------------RHAERLAA---ILADAGPRVVLTTAAAL-----AAVRAFAASRPAAGTPRLLVVDLLPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SkSEREEVAkmqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNN--GIHVGNRNElEGERICVQVPMFHAFGVIISIM 290
Cdd:cd05931 137 S-AADWPPP----SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANvrQIRRAYGLD-PGDVVVSWLPLYHDMGLIGGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 291 AALTKGATMVL--PAAgF--SPKDSLQAIvNEKCSVIHGTPTMYVDL----VNTQKKLQVPLGRIKKAVTGGAIVSPQLI 362
Cdd:cd05931 211 TPLYSGGPSVLmsPAA-FlrRPLRWLRLI-SRYRATISAAPNFAYDLcvrrVRDEDLEGLDLSSWRVALNGAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQV-----LNVEAVHSVYGLTETT----------------------AVIFQSLPGDSSDVV-LNSVGHLTDHIEAKV 414
Cdd:cd05931 289 RRFAEAfapfgFRPEAFRPSYGLAEATlfvsggppgtgpvvlrvdrdalAGRAVAVAADDPAAReLVSCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 415 VDAEG-RCVPFGQPGELCVRGYTTMLGYHDDEEKTKET------IGNDRWLRTGD-QFVLEANGYgrIVGRLKEMLIRGG 486
Cdd:cd05931 369 VDPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDlGFLHDGELY--ITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 487 ENIFPKEIEDFLNAHPQVIEAH---VIGVPDERLGEE--VCAYVRLEEGVDPASFTAETLKAYAKgklAHFKVPR--YVI 559
Cdd:cd05931 447 RNHYPQDIEATAEEAHPALRPGcvaAFSVPDDGEERLvvVAEVERGADPADLAAIAAAIRAAVAR---EHGVAPAdvVLV 523
|
570 580
....*....|....*....|..
gi 24581924 560 PIDAFPKTTSGKIQKFKLVEAF 581
Cdd:cd05931 524 RPGSIPRTSSGKIQRRACRAAY 545
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
47-571 |
1.98e-45 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 173.12 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVV--FGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYqgPE--IAYCLNKVNVKAIIAPETfktqnyyeiLRDICPEISdadtgkirsekfphLRSVIIDSndslkgalr 204
Cdd:COG1020 554 VPLDPAY--PAerLAYMLEDAGARLVLTQSA---------LAARLPELG--------------VPVLALDA--------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 205 fddfLDLASKSEREEVAKMQksilPESACNIQFTSGTTGNPKAACLTHHNFVNngiHVGNRNEL----EGERicvqVPMF 280
Cdd:COG1020 600 ----LALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVN---LLAWMQRRyglgPGDR----VLQF 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 281 HAFGVIIS---IMAALTKGATMVL--PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKlqvPLGRIKKAVTGGA 355
Cdd:COG1020 665 ASLSFDASvweIFGALLSGATLVLapPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE---ALPSLRLVLVGGE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 356 IVSPQLIKDVRQVLNVEAVHSVYGLTETT-AVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRG 434
Cdd:COG1020 742 ALPPELVRRWRARLPGARLVNLYGPTETTvDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGG 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 435 YTTMLGYHDDEEKTKE-------TIGNDRWLRTGDQFVLEANG---Y-GRIVGRLKemlIRGgeniF---PKEIEDFLNA 500
Cdd:COG1020 822 AGLARGYLNRPELTAErfvadpfGFPGARLYRTGDLARWLPDGnleFlGRADDQVK---IRG----FrieLGEIEAALLQ 894
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 501 HPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPAsftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:COG1020 895 HPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAA---AALLRLALALLLPPYMVPAAVVLLLPLPLTGNGK 962
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
70-575 |
2.62e-45 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 166.85 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKA 149
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 IIApetfktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlaskSEREEVAKmqksilp 229
Cdd:cd05914 83 IFV--------------------------------------------------------------SDEDDVAL------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 esacnIQFTSGTTGNPKAACLTHHNFVNNgIHVGNRNEL--EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFS 307
Cdd:cd05914 94 -----INYTSGTTGNSKGVMLTYRNIVSN-VDGVKEVVLlgKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 PKDSLQAIvnEKCSVIHGTPTMYV-------DLVNT------QKKLQVPL------------------GRIKKAVTGGAI 356
Cdd:cd05914 168 AKIIALAF--AQVTPTLGVPVPLViekifkmDIIPKltlkkfKFKLAKKInnrkirklafkkvheafgGNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 357 VSPQLIKDVRQvLNVEAVHSvYGLTETTAVIFQSLPGdssDVVLNSVGHLTDHIEAKVVDAEgrcvPFGQPGELCVRGYT 436
Cdd:cd05914 246 INPDVEEFLRT-IGFPYTIG-YGMTETAPIISYSPPN---RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRG-GENIFPKEIEDFLNAHPQVIEAhVIGVPDE 515
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLES-LVVVQEK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 516 RLGEEVCAYVRLE---EGVDPASFTA---ETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKF 575
Cdd:cd05914 396 KLVALAYIDPDFLdvkALKQRNIIDAikwEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKRF 461
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
53-593 |
4.12e-45 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 168.48 E-value: 4.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:PLN02479 26 LERAAVVHPTRKSVV--HGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIApetfkTQNYYEILRDICPEISDADTGKIRsekfPHLRSVIIDS-------NDSL-KGALR 204
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMV-----DQEFFTLAEEALKILAEKKKSSFK----PPLLIVIGDPtcdpkslQYALgKGAIE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 205 FDDFL-----DLASKSEREEvakmQKSILpesacnIQFTSGTTGNPKAACLTHHnfvnnGIHVGNRNEL------EGERI 273
Cdd:PLN02479 175 YEKFLetgdpEFAWKPPADE----WQSIA------LGYTSGTTASPKGVVLHHR-----GAYLMALSNAliwgmnEGAVY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 274 CVQVPMFHAFGVIISIMAALTKGATMVLPAAgfSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQV-PLGRIKKAVT 352
Cdd:PLN02479 240 LWTLPMFHCNGWCFTWTLAALCGTNICLRQV--TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 353 GGAIVSPQLIKDVRQvLNVEAVHSvYGLTET---TAVI-----FQSLPGDSSdVVLNS------VG----HLTDHIEAKV 414
Cdd:PLN02479 318 AGAAPPPSVLFAMSE-KGFRVTHT-YGLSETygpSTVCawkpeWDSLPPEEQ-ARLNArqgvryIGleglDVVDTKTMKP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 415 VDAEGRCVpfgqpGELCVRGYTTMLGYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEI 494
Cdd:PLN02479 395 VPADGKTM-----GEIVMRGNMVMKGYLKNPKANEEAFANG-WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 495 EDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPA--SFTAETLKAYAKGKLAHFKVPRYVIpIDAFPKTTSGKI 572
Cdd:PLN02479 469 ENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKI 547
|
570 580
....*....|....*....|..
gi 24581924 573 QKFKLVEafKAKET-ELKAARL 593
Cdd:PLN02479 548 QKHVLRA--KAKEMgPVKKSRL 567
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
70-578 |
8.24e-45 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 164.91 E-value: 8.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYclnkvnvka 149
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEY--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 iiapetfktqnyyeilrdicpEISDADTgkirsekfphlRSVIIDSNDslkgalrfddflDLASksereevakmqksilp 229
Cdd:cd05971 73 ---------------------RLSNSGA-----------SALVTDGSD------------DPAL---------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 esacnIQFTSGTTGNPKAaCLTHHNFV--NNGIHVGNRNELEGERICVQVPMFHAF--GVIISIMAALTKGATMVL-PAA 304
Cdd:cd05971 93 -----IIYTSGTTGPPKG-ALHAHRVLlgHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLLPSLYFGVPVLAhRMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 305 GFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETT 384
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTECN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 385 AVIfqslpGDSSDVVL---NSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR--GYTTMLGYHDDEEKTKETIGNDrWLR 459
Cdd:cd05971 246 LVI-----GNCSALFPikpGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 460 TGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAE 539
Cdd:cd05971 320 TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAR 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 24581924 540 TLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLV 578
Cdd:cd05971 400 EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
65-580 |
9.26e-45 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 165.96 E-value: 9.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNK 144
Cdd:cd17655 15 AVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 145 VNVKAIIapetfkTQNYYEILRDICPEISDADTGKIRSEkfphlrsviidSNDSLKGALRFDDfldLASksereevakmq 224
Cdd:cd17655 93 SGADILL------TQSHLQPPIAFIGLIDLLDEDTIYHE-----------ESENLEPVSKSDD---LAY----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 ksilpesacnIQFTSGTTGNPKAACLTHHNfVNNGIHVGNRNELEGERicVQVPMFHAF---GVIISIMAALTKGATMVL 301
Cdd:cd17655 142 ----------VIYTSGSTGKPKGVMIEHRG-VVNLVEWANKVIYQGEH--LRVALFASIsfdASVTEIFASLLSGNTLYI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 -PAAGFSPKDSLQAIVNE-KCSVIHGTPTMYVDLVNTQKKLQVPlgrIKKAVTGGAIVSPQLIKDV--RQVLNVEaVHSV 377
Cdd:cd17655 209 vRKETVLDGQALTQYIRQnRITIIDLTPAHLKLLDAADDSEGLS---LKHLIVGGEALSTELAKKIieLFGTNPT-ITNA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 378 YGLTETT--AVIFQSLPGDSSDVVLnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND 455
Cdd:cd17655 285 YGPTETTvdASIYQYEPETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 ------RWLRTGDQFVLEANGY----GRIVGRLKemlIRGgENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYV 525
Cdd:cd17655 364 pfvpgeRMYRTGDLARWLPDGNieflGRIDHQVK---IRG-YRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 526 RLEEgvdpaSFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:cd17655 440 VSEK-----ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-509 |
1.14e-44 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 163.59 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 80 LLQEADALAAGFRKL-GLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYqgPE--IAYCLNKVNVKAIIAPETF 156
Cdd:TIGR01733 5 LDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAY--PAerLAFILEDAGARLLLTDSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 157 KTQNYYEILRDICPEISDADTGKirsekfphlrsviidsndslkgalrfddflDLASKSEREEVAKmqksilPESACNIQ 236
Cdd:TIGR01733 83 ASRLAGLVLPVILLDPLELAALD------------------------------DAPAPPPPDAPSG------PDDLAYVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGEricVQVPMFHAFGVIISIM---AALTKGATMVLP---AAGFSPKD 310
Cdd:TIGR01733 127 YTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD---DRVLQFASLSFDASVEeifGALLAGATLVVPpedEERDDAAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNEKCSVIHGTPTMYVDLVNTQKKlqvPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETT--AVIF 388
Cdd:TIGR01733 204 LAALIAEHPVTVLNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTvwSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 389 QSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND--------RWLRT 460
Cdd:TIGR01733 281 LVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgaRLYRT 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24581924 461 GDQFVLEANGYGRIVGRLKEML-IRgGENIFPKEIEDFLNAHPQVIEAHV 509
Cdd:TIGR01733 361 GDLVRYLPDGNLEFLGRIDDQVkIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-578 |
2.61e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 163.77 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 86 ALAAGFRKLGLQPGDAVGLWAPN---YLHWYLGM-MGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQny 161
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNrftYIELSFAVaYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 162 yeiLRDICPEISDADTgkirsekfphlrsviidsndslkgALRFDDFLDLASKSEREEVAKmqksilPESACnIQFTSGT 241
Cdd:cd05922 83 ---LRDALPASPDPGT------------------------VLDADGIRAARASAPAHEVSH------EDLAL-LLYTSGS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 242 TGNPKAACLTHHNFVNNGIHVGNRNELEG-ERICVQVPMFHAFGVIIsIMAALTKGATMVLPAAGFSPKDSLQAIVNEKC 320
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLGITAdDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 321 SVIHGTPTMYvDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIfQSLPGDSSDVVL 400
Cdd:cd05922 208 TGLAGVPSTY-AMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRM-TYLPPERILEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 401 NSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDE-EKTKETIGNDRwLRTGDQFVLEANGYGRIVGRLK 479
Cdd:cd05922 286 GSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGV-LHTGDLARRDEDGFLFIVGRRD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 480 EMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDErLGEEVCAYVRLEEGVDPasftAETLKAYAKgKLAHFKVPRYVI 559
Cdd:cd05922 365 RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDP----KDVLRSLAE-RLPPYKVPATVR 438
|
490
....*....|....*....
gi 24581924 560 PIDAFPKTTSGKIQKFKLV 578
Cdd:cd05922 439 VVDELPLTASGKVDYAALR 457
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
83-579 |
6.68e-44 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 162.93 E-value: 6.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 83 EADAL--AAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETfktqn 160
Cdd:cd05929 2 EARDLdrAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 161 yyeiLRDICPEISDadtgkirsekfpHLRSVIIDSNDSLKGAL-RFDDFldlasksEREEVAKMQKSILPESACN-IQFT 238
Cdd:cd05929 77 ----PRAEACAIIE------------IKAAALVCGLFTGGGALdGLEDY-------EAAEGGSPETPIEDEAAGWkMLYS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 239 SGTTGNPKAAcLTHHNFVNngIHV-------GNRNELEGERICVQVPMFHAFGVIISiMAALTKGATMVLpAAGFSPKDS 311
Cdd:cd05929 134 GGTTGRPKGI-KRGLPGGP--PDNdtlmaaaLGFGPGADSVYLSPAPLYHAAPFRWS-MTALFMGGTLVL-MEKFDPEEF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIvnEKCSVIHGT--PTMYVDLvntqkkLQVP--------LGRIKKAVTGGAIVSPQLiKDVRQVLNVEAVHSVYGLT 381
Cdd:cd05929 209 LRLI--ERYRVTFAQfvPTMFVRL------LKLPeavrnaydLSSLKRVIHAAAPCPPWV-KEQWIDWGGPIIWEYYGGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 382 ETTAVIF----QSL--PGDSSDVVLNSVghltdhieaKVVDAEGRCVPFGQPGELCVRGYTTMLgYHDDEEKTKETIGND 455
Cdd:cd05929 280 EGQGLTIingeEWLthPGSVGRAVLGKV---------HILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPAS 535
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGT 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24581924 536 FTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
71-572 |
3.51e-43 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 161.36 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAI 150
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 IApetfktqnyyeilrdicpeiSDADTGKIRSEKFPHLRsviidsndslkgalrfDDFLDLASKSEREEVAKMQksilPE 230
Cdd:cd17651 97 LT--------------------HPALAGELAVELVAVTL----------------LDQPGAAAGADAEPDPALD----AD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SACNIQFTSGTTGNPKAACLTHHNFVN-NGIHVGNRNELEGERIcVQVPMFhAFGVIIS-IMAALTKGATMVLP--AAGF 306
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRSLANlVAWQARASSLGPGART-LQFAGL-GFDVSVQeIFSTLCAGATLVLPpeEVRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPkDSLQAIVNEKCSVIHGTPTMYVD-LVNTQKKLQVPLGRIKKAVTGG-AIVSPQLIKDVRQVLNVEAVHSVYGLTETT 384
Cdd:cd17651 215 DP-PALAAWLDEQRISRVFLPTVALRaLAEHGRPLGVRLAALRYLLTGGeQLVLTEDLREFCAGLPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 385 AVIFQSLPGDSSD-VVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKET------IGNDRW 457
Cdd:cd17651 294 VVTALSLPGDPAAwPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpdpfVPGARM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 458 LRTGDQFVLEANGYGRIVGRLKEML-IRgGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasf 536
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVkIR-GFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV--- 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 24581924 537 TAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17651 450 DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
235-571 |
1.35e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 156.77 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNF---VNNGIHVGNRNEL------------EGERICVQVPMFHAFGVIiSIMAALTKGATM 299
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTpsedahkaaaaaAGTVMFPAPPLMHGTGSW-TAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 300 VLPAAGFSPKDSLQAIVNEKCSVIhgtpTMYVD-----LVNTQKKLQ-VPLGRIKKAVTGGAIVSPQlikdVRQVLnVEA 373
Cdd:cd05924 87 VLPDDRFDPEEVWRTIEKHKVTSM----TIVGDamarpLIDALRDAGpYDLSSLFAISSGGALLSPE----VKQGL-LEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 374 VHSV-----YGLTETTAVIF-QSLPGDSSDVVLNSVGHLTdhieaKVVDAEGRCVPFGQPGE--LCVRGYTTmLGYHDDE 445
Cdd:cd05924 158 VPNItlvdaFGSSETGFTGSgHSAGSGPETGPFTRANPDT-----VVLDDDGRVVPPGSGGVgwIARRGHIP-LGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 446 EKTKET---IGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVC 522
Cdd:cd05924 232 AKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24581924 523 AYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:cd05924 312 AVVQLREGAGV---DLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
38-583 |
1.07e-41 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 158.21 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 38 HIGKDPLVYRTIGQQLELSASNFGD--VEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLW---APNYLHW 112
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTkgITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQfddNEDFIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 113 YLGMMGAaragltsvGLNPAYQGPEIAYclnkvnvkAIIAPETFKTQNYYEILRDicPEISdadTGKIRSEKFPHLRSvi 192
Cdd:cd05906 81 FWACVLA--------GFVPAPLTVPPTY--------DEPNARLRKLRHIWQLLGS--PVVL---TDAELVAEFAGLET-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 193 IDSNDSLKGalrfdDFLDLASKSEREEVAKMQksiLPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGE 271
Cdd:cd05906 138 LSGLPGIRV-----LSIEELLDTAADHDLPQS---RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLtPQD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 272 RICVQVPMFHAFGVIISIMAALTKGATMVLPAAgfspkdslqaivnekcSVIHGTPTMYVDLVNTQK------------K 339
Cdd:cd05906 210 VFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPT----------------EEILADPLRWLDLIDRYRvtitwapnfafaL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 340 L--QVP--------LGRIKKAVTGGAIVSPQLIKDVRQVL-----NVEAVHSVYGLTETTAVIFQSL----PGDSSDVVL 400
Cdd:cd05906 274 LndLLEeiedgtwdLSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTETCSGVIYSRsfptYDHSQALEF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 401 NSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEaNGYGRIVGRLKE 480
Cdd:cd05906 354 VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 481 MLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVP--DERLGEEVCAYVRLEEgVDPASFTAETLKAyAKGKLAH-FKV-PR 556
Cdd:cd05906 433 TIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAvrDPGAETEELAIFFVPE-YDLQDALSETLRA-IRSVVSReVGVsPA 510
|
570 580
....*....|....*....|....*....
gi 24581924 557 YVIPI--DAFPKTTSGKIQKFKLVEAFKA 583
Cdd:cd05906 511 YLIPLpkEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
67-572 |
2.47e-41 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 155.91 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 67 VSChEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYclnkvn 146
Cdd:cd12116 6 VRD-DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 147 vkaiiapetfktqnyyeILRDICPeisdadtgkirsekfphlrSVIIDSNDSLKGALRFDDFLDLASKSEREEVAKMQKS 226
Cdd:cd12116 79 -----------------ILEDAEP-------------------ALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTP 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 227 ILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERI-CVQVPMFHafgviISIMAALT---KGATMVL 301
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLgPGDRLlAVTTYAFD-----ISLLELLLpllAGARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 PAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLgrikKAVTGGAIVSPQLIKdvRQVLNVEAVHSVYG 379
Cdd:cd12116 198 APREtqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGL----TALCGGEALPPDLAA--RLLSRVGSLWNLYG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETT--AVIFQSLPGDSSDVvlnsVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND-- 455
Cdd:cd12116 272 PTETTiwSTAARVTAAAGPIP----IGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDpf 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 -----RWLRTGDQFVLEANGYGRIVGRLKEML-IRgGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVcAYVRLEE 529
Cdd:cd12116 348 agpgsRLYRTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKA 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24581924 530 GvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd12116 426 G---AAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
74-577 |
4.98e-41 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 156.09 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKL-GLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIA 152
Cdd:cd05928 41 KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 153 PETfktqnyyeilrdICPEIsdaDTgkIRSEkFPHLRSVIIDSNDSLKGALRFDDFLDLASKserEEVAKMQKSILPESa 232
Cdd:cd05928 121 SDE------------LAPEV---DS--VASE-CPSLKTKLLVSEKSRDGWLNFKELLNEAST---EHHCVETGSQEPMA- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 cnIQFTSGTTGNPKAACLTHHNFvNNGIHVGNRNELEGERICVQVPMFH---AFGVIISIMAALTKGATM-VLPAAGFSP 308
Cdd:cd05928 179 --IYFTSGTTGSPKMAEHSHSSL-GLGLKVNGRYWLDLTASDIMWNTSDtgwIKSAWSSLFEPWIQGACVfVHHLPRFDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 309 KDSLQAIVNEKCSVIHGTPTMYVDLV-NTQKKLQVPlgRIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTET--TA 385
Cdd:cd05928 256 LVILKTLSSYPITTFCGAPTVYRMLVqQDLSSYKFP--SLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGYGQTETglIC 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 386 VIFQSL---PGdssdvvlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR-----GYTTMLGYHDDEEKTKETIGNDRW 457
Cdd:cd05928 333 ANFKGMkikPG--------SMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAATIRGDFY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 458 LrTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLE---EGVDPA 534
Cdd:cd05928 405 L-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApqfLSHDPE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24581924 535 SFTAEtLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05928 484 QLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
62-577 |
2.06e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 154.01 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 62 DVEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYC 141
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 142 LNKVNVKAIIAPETfktqnyyeiLRDICPEISDADTGKIrsekfphlrsviidsndSLKGalRFDDFLD----LASKSER 217
Cdd:PRK13390 92 VGDSGARVLVASAA---------LDGLAAKVGADLPLRL-----------------SFGG--EIDGFGSfeaaLAGAGPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 218 eevakmqksiLPESACN--IQFTSGTTGNPKA--ACLTHHNFVNNG-----IHVGNRNELEGERICVQVPMFHAFGV-II 287
Cdd:PRK13390 144 ----------LTEQPCGavMLYSSGTTGFPKGiqPDLPGRDVDAPGdpivaIARAFYDISESDIYYSSAPIYHAAPLrWC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 288 SIMAALtkGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLV----NTQKKLQVPLGRikkAVTGGAIVSPQlik 363
Cdd:PRK13390 214 SMVHAL--GGTVVL-AKRFDAQATLGHVERYRITVTQMVPTMFVRLLkldaDVRTRYDVSSLR---AVIHAAAPCPV--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 364 DVRQ---------VLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSVghltdHIeakvVDAEGRCVPFGQPGELCVRG 434
Cdd:PRK13390 285 DVKHamidwlgpiVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGDL-----HI----CDDDGNELPAGRIGTVYFER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 435 YTTMLGYHDDEEKTKET--IGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV 512
Cdd:PRK13390 356 DRLPFRYLNDPEKTAAAqhPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGV 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 513 PDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK13390 436 PDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
57-574 |
2.47e-40 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 154.19 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 57 ASNFGDVEAIVSCH---EGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLW-APNYLHWYlGMMGAARAGLTSVGLNPA 132
Cdd:cd05970 27 AKEYPDKLALVWCDdagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTlKRRYEFWY-SLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFKTQNYYEILRDICPEISdadtgkirsekfphlrsVIIDSNDSLKgalrfDDFLDLa 212
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKP-----------------KLVWVGDPVP-----EGWIDF- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 skseREEVAKMQKSILPESACN---------IQFTSGTTGNPKAACLTH-------------HNFVNNGIHVGNRNELEG 270
Cdd:cd05970 163 ----RKLIKNASPDFERPTANSypcgedillVYFSSGTTGMPKMVEHDFtyplghivtakywQNVREGGLHLTVADTGWG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 271 ERICVQVpmfhaFGVIISimaaltKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNtQKKLQVPLGRIKKA 350
Cdd:cd05970 239 KAVWGKI-----YGQWIA------GAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 351 VTGGAIVSPQLIKDVRQVLNVEAVHSvYGLTETTAVI-----FQSLPGdssdvvlnSVGHLTDHIEAKVVDAEGRCVPFG 425
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIKLMEG-FGQTETTLTIatfpwMEPKPG--------SMGKPAPGYEIDLIDREGRSCEAG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 426 QPGELCVR---GYTTML--GYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNA 500
Cdd:cd05970 378 EEGEIVIRtskGKPVGLfgGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQ 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 501 HPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd05970 457 HPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
48-577 |
4.42e-40 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 154.17 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 48 TIGQQLELSASNFGDVEaIVSCHEGKR--YSFKSLLQEADALAAGFR-KLGLQPGDAVGLWAPNYLHWYLGMMGAARAGL 124
Cdd:PRK05620 11 SLTRILEYGSTVHGDTT-VTTWGGAEQeqTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 125 TSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFKTQnYYEILRDiCPE------ISDADTGKIRSEKFPHLRsviidsnds 198
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQ-LGEILKE-CPCvravvfIGPSDADSAAAHMPEGIK--------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 199 lkgALRFDDFLDlaskserEEVAKMQKSILPE-SACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL---EGERIC 274
Cdd:PRK05620 159 ---VYSYEALLD-------GRSTVYDWPELDEtTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLavtHGESFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 275 VQVPMFH--AFGVIIsimAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLV-----NTQKKLQvplgrI 347
Cdd:PRK05620 229 CCVPIYHvlSWGVPL---AAFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMvhylkNPPERMS-----L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 KKAVTGGAIVSPQLIKDVRQVLNVEAVHsVYGLTETTAVIFQSLP-----GDSSDVVLNSVGHLTDHIEAKVVDaEGRCV 422
Cdd:PRK05620 301 QEIYVGGSAVPPILIKAWEERYGVDVVH-VWGMTETSPVGTVARPpsgvsGEARWAYRVSQGRFPASLEYRIVN-DGQVM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 423 PFG--QPGELCVRGYT-TMLGYHDDEEK---------------TKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIR 484
Cdd:PRK05620 379 ESTdrNEGEIQVRGNWvTASYYHSPTEEgggaastfrgedvedANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 485 GGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAF 564
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEI 538
|
570
....*....|...
gi 24581924 565 PKTTSGKIQKFKL 577
Cdd:PRK05620 539 DKTSVGKFDKKDL 551
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
80-577 |
1.37e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 150.91 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 80 LLQEADALAAGFRKLglqpgDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYclnkvnvkaiiapetfktq 159
Cdd:PRK07787 31 LAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRH------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 160 nyyeILRDicpeiSDADtgkirsekfphlrSVIIDSNDSLKGALRFDDFLDLASKSEREEVAkmqksilPESACNIQFTS 239
Cdd:PRK07787 87 ----ILAD-----SGAQ-------------AWLGPAPDDPAGLPHVPVRLHARSWHRYPEPD-------PDAPALIVYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 240 GTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQ-VPMFHAFGVIISIMAALTKGATMVlPAAGFSPKDSLQAiVNE 318
Cdd:PRK07787 138 GTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHgLPLFHVHGLVLGVLGPLRIGNRFV-HTGRPTPEAYAQA-LSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 319 KCSVIHGTPTMYVDLVNTQKKLQVpLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSvYGLTETtaVIFQSLPGDSsDV 398
Cdd:PRK07787 216 GGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVER-YGMTET--LITLSTRADG-ER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 399 VLNSVGHLTDHIEAKVVDAEGRCVPF-GQP-GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVG 476
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 477 RLKEMLIR-GGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasftaETLKAYAKGKLAHFKVP 555
Cdd:PRK07787 371 RESTDLIKsGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA-----DELIDFVAQQLSVHKRP 445
|
490 500
....*....|....*....|..
gi 24581924 556 RYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK07787 446 REVRFVDALPRNAMGKVLKKQL 467
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
64-577 |
2.78e-39 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 149.70 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIAPETfktQNYYeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevakm 223
Cdd:cd05945 86 AAKPALLIADGD---DNAY------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksilpesacnIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHaFGV-IISIMAALTKGATMVL- 301
Cdd:cd05945 102 -----------IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS-FDLsVMDLYPALASGATLVPv 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 -PAAGFSPKDSLQAIVNEKCSVIHGTPTmYVDLVNTQKKLQVP-LGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYG 379
Cdd:cd05945 170 pRDATADPKQLFRFLAEHGITVWVSTPS-FAAMCLLSPTFTPEsLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 380 LTETT----AVIFQSLPGDSSDVVlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE---TI 452
Cdd:cd05945 249 PTEATvavtYIEVTPEVLDGYDRL--PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVD 532
Cdd:cd05945 327 EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24581924 533 PAsFTAEtLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05945 407 AG-LTKA-IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
237-570 |
3.50e-39 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 146.29 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV-PMFHaFGVIISIMAALTKGATMVLpAAGFSPKDSLQAI 315
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSgPLFH-IGTLMFTLATFHAGGTNVF-VRRVDAEEVLELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 316 VNEKCSviHG---TPTMyvdlvntqkklqvplGRIKKAVTGG--------AIVSPQLIKDVRQVLNVEAVHSVYGLTETT 384
Cdd:cd17636 85 EAERCT--HAfllPPTI---------------DQIVELNADGlydlsslrSSPAAPEWNDMATVDTSPWGRKPGGYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 385 AVIFQSLPGDSSDVVLNSvGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETiGNDRWLRTGDQF 464
Cdd:cd17636 148 VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARR-TRGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 465 VLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpASFTAETLKAY 544
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG---ASVTEAELIEH 302
|
330 340
....*....|....*....|....*.
gi 24581924 545 AKGKLAHFKVPRYVIPIDAFPKTTSG 570
Cdd:cd17636 303 CRARIASYKKPKSVEFADALPRTAGG 328
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
237-577 |
3.87e-39 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 148.82 E-value: 3.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKA------ACLTHHNFVNNGIHVGNrnelEGERICVQVPMFhAFGVIISIMAALTKGATMVLPAAGFSPKD 310
Cdd:cd05973 95 FTSGTTGLPKGvpvplrALAAFGAYLRDAVDLRP----EDSFWNAADPGW-AYGLYYAITGPLALGHPTILLEGGFSVES 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQV-PLGRIKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIfQ 389
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPArPKGRLRRVSSAGEPLTPEVIRWFDAALGV-PIHDHYGQTELGMVL-A 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 390 SLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTML----GYHDDEEKTKEtignDRWLRTGDQFV 465
Cdd:cd05973 248 NHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID----GGYYLTGDTVE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 466 LEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYA 545
Cdd:cd05973 324 FDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHV 403
|
330 340 350
....*....|....*....|....*....|..
gi 24581924 546 KGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05973 404 KKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
61-572 |
1.29e-38 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 148.58 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 61 GDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAY 140
Cdd:cd17646 12 PDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 141 clnkvnvkaiiapetfktqnyyeILRDICPE--ISDADTGkirsekfphlrsviidsnDSLKGALRFDDFLDLASKSERE 218
Cdd:cd17646 90 -----------------------MLADAGPAvvLTTADLA------------------ARLPAGGDVALLGDEALAAPPA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 219 EVAkmQKSILPESACNIQFTSGTTGNPKAACLTHHNFVN------NGIHVGnrnelEGERICVQVPMfhAFGVII-SIMA 291
Cdd:cd17646 129 TPP--LVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNrllwmqDEYPLG-----PGDRVLQKTPL--SFDVSVwELFW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 292 ALTKGATMVLPAAGfSPKDS---LQAIVNEKCSVIHGTPTMYVDLVNtqkklQVPLGR---IKKAVTGGAIVSPQLIKDV 365
Cdd:cd17646 200 PLVAGARLVVARPG-GHRDPaylAALIREHGVTTCHFVPSMLRVFLA-----EPAAGScasLRRVFCSGEALPPELAARF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNVEaVHSVYGLTETT--AVIFQSLPGDSSDVVlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHD 443
Cdd:cd17646 274 LALPGAE-LHNLYGPTEAAidVTHWPVRGPAETPSV--PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 444 DEEKTKETIGND------RWLRTGDQFVLEANGYGRIVGRLKEML-IRGgENIFPKEIEDFLNAHPQVIEAHVIGVPDER 516
Cdd:cd17646 351 RPALTAERFVPDpfgpgsRMYRTGDLARWRPDGALEFLGRSDDQVkIRG-FRVEPGEIEAALAAHPAVTHAVVVARAAPA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 517 LGEEVCAYVRLEEGVDPASftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17646 430 GAARLVGYVVPAAGAAGPD--TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
237-572 |
6.09e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 146.46 E-value: 6.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKAACLTHHNFvnngIHVGNRNELE-----GERICVQVPMFHA---FGVIisimAALTKGATMVLpAAGFSP 308
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSW----LHSFDCNVHDfhmkrEDSVLIAGTLVHSlflYGAI----STLYVGQTVHL-MRKFIP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 309 KDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLgrikKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIF 388
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKENRVIENKM----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 389 qsLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKEtIGNDRWLRTGDQFVLEA 468
Cdd:PRK07638 297 --LVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 469 NGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRleegvdpASFTAETLKAYAKGK 548
Cdd:PRK07638 374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK-------GSATKQQLKSFCLQR 446
|
330 340
....*....|....*....|....
gi 24581924 549 LAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK07638 447 LSSFKIPKEWHFVDEIPYTNSGKI 470
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
57-572 |
1.25e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 146.96 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 57 ASNFGDVEAI--VSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGlTSVG-LNPAY 133
Cdd:PRK04319 54 DGGRKDKVALryLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNG-AIVGpLFEAF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 134 qGPE-IAYCLNKVNVKAIIApetfkTQNYYEilrdicpeisdadtgKIRSEKFPHLRSVII--DSNDSLKGALRFDDFLD 210
Cdd:PRK04319 133 -MEEaVRDRLEDSEAKVLIT-----TPALLE---------------RKPADDLPSLKHVLLvgEDVEEGPGTLDFNALME 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASKS-EREEVAKMQKSILpesacniQFTSGTTGNPKAAclthhnfvnngIHVgnRNELEGERICVQVPM-FH------- 281
Cdd:PRK04319 192 QASDEfDIEWTDREDGAIL-------HYTSGSTGKPKGV-----------LHV--HNAMLQHYQTGKYVLdLHeddvywc 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 ----------AFGVIisimAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPT---MYV----DLVntqKKLQVPl 344
Cdd:PRK04319 252 tadpgwvtgtSYGIF----APWLNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTairMLMgagdDLV---KKYDLS- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 345 grikkavtggaivSPQLIKDVRQVLNVEAV---HSVYGL--------TETTAVIFQSLPgdSSDVVLNSVGHLTDHIEAK 413
Cdd:PRK04319 324 -------------SLRHILSVGEPLNPEVVrwgMKVFGLpihdnwwmTETGGIMIANYP--AMDIKPGSMGKPLPGIEAA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 414 VVDAEGRCVPFGQPGELCVR-GYTTML-GYHDDEEKTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFP 491
Cdd:PRK04319 389 IVDDQGNELPPNRMGNLAIKkGWPSMMrGIWNNPEKYESYFAGD-WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 492 KEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:PRK04319 468 FEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
.
gi 24581924 572 I 572
Cdd:PRK04319 548 I 548
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
64-574 |
5.67e-37 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 143.22 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYcln 143
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 kvnvkaiiapetfktqnyyeILRDICPeisdadtgkirsekfphlrSVIIDSNDslkgalrfddflDLASksereevakm 223
Cdd:cd17643 79 --------------------ILADSGP-------------------SLLLTDPD------------DLAY---------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksilpesacnIQFTSGTTGNPKAACLTHHN----FVNNGiHVGNRNELEgericvQVPMFHAFGVIIS---IMAALTKG 296
Cdd:cd17643 98 -----------VIYTSGSTGRPKGVVVSHANvlalFAATQ-RWFGFNEDD------VWTLFHSYAFDFSvweIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 ATMVLP--AAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD--VRQVLNVE 372
Cdd:cd17643 160 GRLVVVpyEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPwaGRFGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 373 AVHSVYGLTETTA-VIFQSL-PGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE 450
Cdd:cd17643 240 QLVNMYGITETTVhVTFRPLdAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 -------TIGNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGgENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVC 522
Cdd:cd17643 320 rfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVkIRG-FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLV 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24581924 523 AYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd17643 399 AYVVADDGAAA---DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
87-583 |
1.52e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 144.01 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 87 LAAGFRKLGLQPGDAVGLWAPNY-----LHWYLGMMGAAragltsvgLNPayqgpeIAYCLNKVNVKAII---APET-FK 157
Cdd:PLN03102 52 LAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAV--------LNP------INTRLDATSIAAILrhaKPKIlFV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 158 TQNYYEILRDICPEISDADTGkirsekfPHLRSVIIDSNDSLKGALRFD-DFLDLASKSEREE--VAKMQKSILPESACN 234
Cdd:PLN03102 118 DRSFEPLAREVLHLLSSEDSN-------LNLPVIFIHEIDFPKRPSSEElDYECLIQRGEPTPslVARMFRIQDEHDPIS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHnfvnnGIHVGNRNELEGERICV------QVPMFHAFGVIISIMAAlTKGATMV----LPAA 304
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHR-----GAYLSTLSAIIGWEMGTcpvylwTLPMFHCNGWTFTWGTA-ARGGTSVcmrhVTAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 305 GFSPKDSLQAIVNEKCsvihgTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQvLNVEAVHSvYGLTETT 384
Cdd:PLN03102 265 EIYKNIEMHNVTHMCC-----VPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQR-LGFQVMHA-YGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 385 A-VIF-------QSLPgDSSDVVLNS---VGHLT-------DHIEAKVVDAEGRCVpfgqpGELCVRGYTTMLGYHDDEE 446
Cdd:PLN03102 338 GpVLFcewqdewNRLP-ENQQMELKArqgVSILGladvdvkNKETQESVPRDGKTM-----GEIVIKGSSIMKGYLKNPK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 447 KTKETIGNDrWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVR 526
Cdd:PLN03102 412 ATSEAFKHG-WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 527 LEEG-------VDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKA 583
Cdd:PLN03102 491 LEKGettkedrVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
73-518 |
2.69e-36 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 141.34 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 73 KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGltsvglnpayqgpeiayclnKVNVkaiia 152
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG--------------------AVDV----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 153 petfktqnyyeilrdicPEISDADTGKIRsEKFPHLRSVIIdsndslkgalrfddFLDLASKSereeVAkmqksilpesa 232
Cdd:cd17640 59 -----------------VRGSDSSVEELL-YILNHSESVAL--------------VVENDSDD----LA----------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 cNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELE-GERICVQVPMFHAFGVIISIMAaLTKGATMVLPaagfSPKDS 311
Cdd:cd17640 92 -TIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQpGDRFLSILPIWHSYERSAEYFI-FACGCSQAYT----SIRTL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 312 LQAIVNEKCSVIHGTPTMYVDL-VNTQKKLQ-------------VPLGRIKKAVTGGAIVSPQLIKDVRqVLNVEaVHSV 377
Cdd:cd17640 166 KDDLKRVKPHYIVSVPRLWESLySGIQKQVSksspikqflflffLSGGIFKFGISGGGALPPHVDTFFE-AIGIE-VLNG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 378 YGLTETTAVIFQSLPgdsSDVVLNSVGHLTDHIEAKVVDAEGRCV-PFGQPGELCVRGYTTMLGYHDDEEKTKETIGNDR 456
Cdd:cd17640 244 YGLTETSPVVSARRL---KCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581924 457 WLRTGDQFVLEANGYGRIVGRLKE-MLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLG 518
Cdd:cd17640 321 WFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG 383
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
75-536 |
3.14e-36 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 142.74 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDA--VGLWAPNYLHWYLGMMGAARAGLTSVglnPAYQ--GPE-IAYCLNKVNVKA 149
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTV---PLYDtlGPEaIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 IIAPETFKTqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgaLRFDDFLDLASKSEREEVAKMqksilP 229
Cdd:cd05927 83 VFCDAGVKV--------------------------------------------YSLEEFEKLGKKNKVPPPPPK-----P 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 ESACNIQFTSGTTGNPKAACLTHHNFVNNgIHVGNRNELEGERICVQ------VPMFHAFGVIIsIMAALTKGA------ 297
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSN-VAGVFKILEILNKINPTdvyisyLPLAHIFERVV-EALFLYHGAkigfys 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 298 ---------------TMV-----------------LPAAGFSPKDSLQAIVNEKCSVI---HGTPTMYVDLVnTQKKLQV 342
Cdd:cd05927 192 gdirlllddikalkpTVFpgvprvlnriydkifnkVQAKGPLKRKLFNFALNYKLAELrsgVVRASPFWDKL-VFNKIKQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 343 PLG-RIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTAVIFQSLPGDSSdvvLNSVGHLTDHIEAKVVDaegrc 421
Cdd:cd05927 271 ALGgNVRLMLTGSAPLSPEVLEFLRVALGCP-VLEGYGQTECTAGATLTLPGDTS---VGHVGGPLPCAEVKLVD----- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 422 VP------FGQP--GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGENIFPK 492
Cdd:cd05927 342 VPemnydaKDPNprGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPE 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 493 EIEDFLNAHPQV---------IEAHVIG--VPDerlgEEVCAYVRLEEGVDPASF 536
Cdd:cd05927 422 KIENIYARSPFVaqifvygdsLKSFLVAivVPD----PDVLKEWAASKGGGTGSF 472
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
70-577 |
3.33e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 142.13 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLgLQPGDA--VGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNV 147
Cdd:PRK07867 24 FEDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 148 KAIIApetfkTQNYYEILRDICP--EISDADTGKIRSEKFPHLRSVIIDSNDSLkgalrfDDFLDLAsksereevakmqk 225
Cdd:PRK07867 103 QLVLT-----ESAHAELLDGLDPgvRVINVDSPAWADELAAHRDAEPPFRVADP------DDLFMLI------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 226 silpesacniqFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERIC-VQVPMFHAFGVIISIMAALTKGATMVLPAA 304
Cdd:PRK07867 159 -----------FTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCyVSMPLFHSNAVMAGWAVALAAGASIALRRK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 305 gFSPKDSLQAI----------VNEKCSVIHGTPTMYVDLVNtqkklqvPLgRIKKAVTGGAivspqliKDVRQVLNVEAV 374
Cdd:PRK07867 228 -FSASGFLPDVrrygatyanyVGKPLSYVLATPERPDDADN-------PL-RIVYGNEGAP-------GDIARFARRFGC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 375 HSV--YGLTETtAVIFQSLPGDSSDvvlnSVGHLTDHIeaKVVDAEG--RCVP--FGQP---------GELC-VRGYTTM 438
Cdd:PRK07867 292 VVVdgFGSTEG-GVAITRTPDTPPG----ALGPLPPGV--AIVDPDTgtECPPaeDADGrllnadeaiGELVnTAGPGGF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 439 LGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLG 518
Cdd:PRK07867 365 EGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 519 EEVCAYVRLEEGV--DPASFtAETLKAYAkgKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK07867 444 DQVMAALVLAPGAkfDPDAF-AEFLAAQP--DLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
88-516 |
5.38e-36 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 142.50 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 88 AAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLnpayqgpeiaYCLNKVNVKAIIApETFKTQnyyeilrd 167
Cdd:cd05933 22 AKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGI----------YTTNSPEACQYVA-ETSEAN-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 168 ICPEISDADTGKIRS--EKFPHLRSVIIDSnDSLK----GALRFDDFLDLASKSEREEVAKMQKSILPESACNIQFTSGT 241
Cdd:cd05933 83 ILVVENQKQLQKILQiqDKLPHLKAIIQYK-EPLKekepNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 242 TGNPKAACLTHHNFV----NNGIHVGNRNELEGERICVQ-VPMFHAFGVIISIMAALTKGATM----------------- 299
Cdd:cd05933 162 TGMPKGVMLSHDNITwtakAASQHMDLRPATVGQESVVSyLPLSHIAAQILDIWLPIKVGGQVyfaqpdalkgtlvktlr 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 300 -VLPAAGFS-PK------DSLQAI---------------------VNEKCSVIHGTPTMYVDLVNTQ--KKLQVPLG--R 346
Cdd:cd05933 242 eVRPTAFMGvPRvwekiqEKMKAVgaksgtlkrkiaswakgvgleTNLKLMGGESPSPLFYRLAKKLvfKKVRKALGldR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 347 IKKAVTGGAIVSPQLiKDVRQVLNVeAVHSVYGLTETTAVIFQSLPGDssdVVLNSVGHLTDHIEAKVV--DAEGRcvpf 424
Cdd:cd05933 322 CQKFFTGAAPISRET-LEFFLSLNI-PIMELYGMSETSGPHTISNPQA---YRLLSCGKALPGCKTKIHnpDADGI---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 425 gqpGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIR-GGENIFPKEIEDFLNAH-P 502
Cdd:cd05933 393 ---GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIEDAVKKElP 469
|
490
....*....|....
gi 24581924 503 QVIEAHVIGvpDER 516
Cdd:cd05933 470 IISNAMLIG--DKR 481
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-574 |
6.60e-36 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 141.03 E-value: 6.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNvkaiiaP 153
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAE------D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 ETFktqnyyeilrdicpeISDADTGKIRSEKFPHLRSVIIDSNDSLKGAlRFDDFLDLASKSereevakmQKSILPESAC 233
Cdd:cd05915 98 KVL---------------LFDPNLLPLVEAIRGELKTVQHFVVMDEKAP-EGYLAYEEALGE--------EADPVRVPER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 N---IQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICV---QVPMFHAFGVIIsIMAALTKGATMVLPAAGFS 307
Cdd:cd05915 154 AacgMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVvlpVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 PKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAiVSPQLIKDVRQvLNVEAVHSVYGLTET---- 383
Cdd:cd05915 233 PASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGS-AAPRSLIARFE-RMGVEVRQGYGLTETspvv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 384 TAVIF----QSLPGDSSdVVLNSVGHLTDHIEA-KVVDAEGRCVPfgQPGE----LCVRGYTTMLGYHDDEEKTKETIGN 454
Cdd:cd05915 311 VQNFVkshlESLSEEEK-LTLKAKTGLPIPLVRlRVADEEGRPVP--KDGKalgeVQLKGPWITGGYYGNEEATRSALTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEgvdpA 534
Cdd:cd05915 388 DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG----E 463
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24581924 535 SFTAETLKAYAKGKLAHFK-VPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd05915 464 KPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLK 504
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
235-574 |
3.60e-35 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 135.47 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHV--GNRNELEGERICVQVPMFHAFGvIISIMAALTKGATMVLPAAGFSPKDSL 312
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILqkEGLNWVVGDVTYLPLPATHIGG-LWWILTCLIHGGLCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVspqLIKDVRQVL---NVEAVHsVYGLTETTAVIFq 389
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRA---IAADVRFIEatgLTNTAQ-VYGLSETGTALC- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 390 sLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEAN 469
Cdd:cd17635 160 -LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERRED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 470 GYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAetLKAYAKGKL 549
Cdd:cd17635 238 GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRA--LKHTIRREL 315
|
330 340
....*....|....*....|....*
gi 24581924 550 AHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-589 |
1.28e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 140.68 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIA-PETFKTQNYYEILRDICPEiSDADTGKIRSEKFPHLRsviidsndslkgalrfddfldlasksereevak 222
Cdd:PRK12467 607 DSGVRLLLTqSHLLAQLPVPAGLRSLCLD-EPADLLCGYSGHNPEVA--------------------------------- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 223 mqksILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVL- 301
Cdd:PRK12467 653 ----LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLl 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 -PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVntQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGL 380
Cdd:PRK12467 729 pPDCARDAEAFAALMADQGVTVLKIVPSHLQALL--QASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGP 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 381 TETTAVIFQ-SLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND---- 455
Cdd:PRK12467 807 TETTVGVSTyELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfga 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 ---RWLRTGDQFVLEANGYGRIVGRLKEML-IRgGENIFPKEIEDFLNAHPQVIEAHVIGVPDERlGEEVCAYVRLEEGV 531
Cdd:PRK12467 887 dggRLYRTGDLARYRADGVIEYLGRMDHQVkIR-GFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVPAAVA 964
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 532 DPA--SFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE--------AFKAKETELK 589
Cdd:PRK12467 965 DGAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKpdasavqaTFVAPQTELE 1032
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
7-579 |
1.73e-34 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 138.08 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 7 TISRYMLRQKcafnsMRSISTSMPSLISH-KHHIGKDPLVYRTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEAD 85
Cdd:PRK08279 1 TITLMDLAAR-----LPRRLPDLPGILRGlKRTALITPDSKRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARAN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 86 ALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETfktqnyyeiL 165
Cdd:PRK08279 74 RYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEE---------L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 166 RDICPEISDADTGKIRsekfphLRSVIIDSNDSLKGALRFDDFLDLASKSEREEvakmQKSILPESACNIQFTSGTTGNP 245
Cdd:PRK08279 145 VEAFEEARADLARPPR------LWVAGGDTLDDPEGYEDLAAAAAGAPTTNPAS----RSGVTAKDTAFYIYTSGTTGLP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 246 KAACLTHHNFVNNGIHVGNRNELEGE-RICVQVPMFHAFGVIISIMAALTKGATMVL----PAAGFSPKdslqaIVNEKC 320
Cdd:PRK08279 215 KAAVMSHMRWLKAMGGFGGLLRLTPDdVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkfSASRFWDD-----VRRYRA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 321 SVIhgtptMYVD-----LVNTQKKlqvPLGR---IKKAVtgGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFqslp 392
Cdd:PRK08279 290 TAF-----QYIGelcryLLNQPPK---PTDRdhrLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFI---- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 gdSSDVVLNSVGHLTDHI-------------EAKVVDAEGRC--VPFGQPGELCVR--------GYTtmlgyhdDEEKTK 449
Cdd:PRK08279 356 --NVFNFDGTVGRVPLWLahpyaivkydvdtGEPVRDADGRCikVKPGEVGLLIGRitdrgpfdGYT-------DPEASE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 450 ETI-------GnDRWLRTGDQFVLEANGYGRIVGRL------KemlirgGENIFPKEIEDFLNAHPQVIEAHVIGVP--- 513
Cdd:PRK08279 427 KKIlrdvfkkG-DAWFNTGDLMRDDGFGHAQFVDRLgdtfrwK------GENVATTEVENALSGFPGVEEAVVYGVEvpg 499
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 514 -DERLGeevCAYVRLEEGVDpasFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK08279 500 tDGRAG---MAAIVLADGAE---FDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
64-572 |
4.23e-34 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 134.90 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIapetfktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevakm 223
Cdd:cd17650 82 DSGAKLLL------------------------------------------------------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksILPESACNIQFTSGTTGNPKAACLTHHNFVNngIHVGNRNELEGERICV---QVPMFhAFGVIISIMA-ALTKGATM 299
Cdd:cd17650 90 ---TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAH--AAHAWRREYELDSFPVrllQMASF-SFDVFAGDFArSLLNGGTL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 300 VLPAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD-VRQVLNVEAVHS 376
Cdd:cd17650 164 VICPDEvkLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTlAARFGQGMRIIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 377 VYGLTETT--AVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGN 454
Cdd:cd17650 244 SYGVTEATidSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 D------RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLE 528
Cdd:cd17650 324 NpfapgeRMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 24581924 529 EGVDpasfTAEtLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17650 404 ATLN----TAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
62-577 |
6.22e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 135.89 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 62 DVEAIVsCHEgKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEI-AY 140
Cdd:PRK10946 38 DAIAVI-CGE-RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELnAY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 141 CLnKVNVKAIIAP---ETFKTQNYYEILRDICPEISdadtgkirsekfphlrsVIIDSNDSlkGALRFDDFLD------L 211
Cdd:PRK10946 116 AS-QIEPALLIADrqhALFSDDDFLNTLVAEHSSLR-----------------VVLLLNDD--GEHSLDDAINhpaedfT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 212 ASKSEREEVAKMQKSilpesacniqftSGTTGNPKAACLTHHNFVNNgihVGNRNELEG----ERICVQVPMFH------ 281
Cdd:PRK10946 176 ATPSPADEVAFFQLS------------GGSTGTPKLIPRTHNDYYYS---VRRSVEICGftpqTRYLCALPAAHnypmss 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 --AFGVIISimaaltkGATMVLpAAGFSPKDSLQAIVNEKCSVIHGTP---TMYVDLVN---------TQKKLQVplgri 347
Cdd:PRK10946 241 pgALGVFLA-------GGTVVL-APDPSATLCFPLIEKHQVNVTALVPpavSLWLQAIAeggsraqlaSLKLLQV----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 kkavtGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTaVIFQSLpGDSSDVVLNSVGH-LTDHIEAKVVDAEGRCVPFGQ 426
Cdd:PRK10946 308 -----GGARLSETLARRIPAELGCQ-LQQVFGMAEGL-VNYTRL-DDSDERIFTTQGRpMSPDDEVWVADADGNPLPQGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 427 PGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIE 506
Cdd:PRK10946 380 VGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 507 AHVIGVPDERLGEEVCAYVRLEEGVDPAsftaeTLKAYAKGK-LAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK10946 460 AALVSMEDELMGEKSCAFLVVKEPLKAV-----QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
53-577 |
1.28e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 134.74 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPA 132
Cdd:PRK13383 41 LAVTAARWPGRTAIID--DDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 133 YQGPEIAYCLNKVNVKAIIAPETFKTQnyyeilrdicpeISDADtgkirsekfphlRSVIIdsndslkgalrfddfLDLA 212
Cdd:PRK13383 119 FRSDALAAALRAHHISTVVADNEFAER------------IAGAD------------DAVAV---------------IDPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 213 SKSEREEVAKmqksilPESACN---IQFTSGTTGNPKAacLTHHNFVNNGIHVG----NRNELE-GERICVQVPMFHAFG 284
Cdd:PRK13383 160 TAGAEESGGR------PAVAAPgriVLLTSGTTGKPKG--VPRAPQLRSAVGVWvtilDRTRLRtGSRISVAMPMFHGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 285 VIIsIMAALTKGATmVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQV--PLGRIKKAVTGGAIVSPQLI 362
Cdd:PRK13383 232 LGM-LMLTIALGGT-VLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDRLDPTLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQVLNvEAVHSVYGLTETtAVIFQSLPGDSSDVVlNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYH 442
Cdd:PRK13383 310 QRFMDTYG-DILYNGYGSTEV-GIGALATPADLRDAP-ETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 443 DDEEKTKEtignDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVC 522
Cdd:PRK13383 387 DGGGKAVV----DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 523 AYVRLEEGVDpasFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK13383 463 AFVVLHPGSG---VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
70-585 |
3.56e-33 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 134.54 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKR-----YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNK 144
Cdd:cd05968 82 WEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 145 VNVKAIIAPETFKTQNyyeilrdicPEISDADTGKIRSEKFPHLRSVIID--SNDSLKGALRFDDFLDLASKSEREEVAK 222
Cdd:cd05968 162 AEAKALITADGFTRRG---------REVNLKEEADKACAQCPTVEKVVVVrhLGNDFTPAKGRDLSYDEEKETAGDGAER 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 223 MQksilPESACNIQFTSGTTGNPKAACLTHHNF-VNNGIHVGNRNEL-EGERICVQVPMFHAFGVIIsIMAALTKGATMV 300
Cdd:cd05968 233 TE----SEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLkPGDLLTWFTDLGWMMGPWL-IFGGLILGATMV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 L--PAAGFSPKDSLQAIVNE--------KCSVIHGTPTMYVDLVNTQKKLQVPLgrikKAVTGGAIVSPQLIKDVRQVLN 370
Cdd:cd05968 308 LydGAPDHPKADRLWRMVEDheithlglSPTLIRALKPRGDAPVNAHDLSSLRV----LGSTGEPWNPEPWNWLFETVGK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 371 VEAVHSVY-GLTETTAVIF--------------QSLPGdssdvvlnsvghltdhIEAKVVDAEGRCVPfGQPGELCVR-- 433
Cdd:cd05968 384 GRNPIINYsGGTEISGGILgnvlikpikpssfnGPVPG----------------MKADVLDESGKPAR-PEVGELVLLap 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 434 --GYTTmlGYHDDEEKTKETIGN---DRWLRtGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAH 508
Cdd:cd05968 447 wpGMTR--GFWRDEDRYLETYWSrfdNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 509 VIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAFKAKE 585
Cdd:cd05968 524 AIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKE 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
72-580 |
1.01e-32 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 130.94 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 ApetfktqnyyeilrDICPEIsdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevakmqksilpes 231
Cdd:cd05940 81 V--------------DAALYI----------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 232 acniqFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGE-RICVQVPMFHAFGVIISIMAALTKGATMVLpAAGFSPKD 310
Cdd:cd05940 88 -----YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSdVLYTCLPLYHSTALIVGWSACLASGATLVI-RKKFSASN 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNEKCSVIH--GTPTMYvdLVNTQKKLQVPLGRIKKAVTGGaiVSPQLIKDVRQVLNVEAVHSVYGLTE-TTAVI 387
Cdd:cd05940 162 FWDDIRKYQATIFQyiGELCRY--LLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEgNSGFI 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 388 -FQSLPG--DSSDVVLNSVGHLT----DH-IEAKVVDAEGRC--VPFGQPGELCVR--GYTTMLGYHDDEEKTKETIGN- 454
Cdd:cd05940 238 nFFGKPGaiGRNPSLLRKVAPLAlvkyDLeSGEPIRDAEGRCikVPRGEPGLLISRinPLEPFDGYTDPAATEKKILRDv 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 ----DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERL-GEEVCAYVRLEE 529
Cdd:cd05940 318 fkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAGMAAIVLQP 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24581924 530 GvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:cd05940 398 N---EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
72-572 |
4.61e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 132.36 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLgLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:PRK08633 639 GGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVI 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 APETFktqnyyeilrdicpeisdadtgkirSEKfphLRSVIIDSNDSLKGALRF-DDFLDLASKSEREeVAKMQKSILP- 229
Cdd:PRK08633 718 TSRKF-------------------------LEK---LKNKGFDLELPENVKVIYlEDLKAKISKVDKL-TALLAARLLPa 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 ---ESACN----------IQFTSGTTGNPKAACLTHHNFVNN---GIHVGNRNEleGERICVQVPMFHAFGVIISIMAAL 293
Cdd:PRK08633 769 rllKRLYGptfkpddtatIIFSSGSEGEPKGVMLSHHNILSNieqISDVFNLRN--DDVILSSLPFFHSFGLTVTLWLPL 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 294 TKGATMVLPAagfSPKDSL---QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLN 370
Cdd:PRK08633 847 LEGIKVVYHP---DPTDALgiaKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFG 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 371 VEAVHSvYGLTETTAVIFQSLP----GDSSDVVLN---SVGHLTDHIEAKVVDAE-GRCVPFGQPGELCVRGYTTMLGYH 442
Cdd:PRK08633 924 IRILEG-YGATETSPVASVNLPdvlaADFKRQTGSkegSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYL 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 443 DDEEKTKE---TIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIED----FLNAHPQVIEahVIGVPDE 515
Cdd:PRK08633 1003 GDPEKTAEvikDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEelakALGGEEVVFA--VTAVPDE 1080
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 516 RLGEEVCAYVRLEEGvdpasFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK08633 1081 KKGEKLVVLHTCGAE-----DVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
228-585 |
1.12e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 128.76 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 228 LPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGAT-MVLPAAG 305
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWkTKDRILSWMPLTHDMGLIAFHLAPLIAGMNqYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 306 F--SPKDSLQAIVNEKCSVIhGTPT----MYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQV-----LNVEAV 374
Cdd:cd05908 184 FirRPILWLKKASEHKATIV-SSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHmskygLKRNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 375 HSVYGLTETTAVIfqSLP---------------------------GDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQP 427
Cdd:cd05908 263 LPVYGLAEASVGA--SLPkaqspfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 428 GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQ-FVLEANGYgrIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIE 506
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLgFIRNGRLV--ITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 507 AHV--IGVPDERL-GEEVCAYVRLEEGVDPASFTAETLKA--YAKGKLAHFKvpryVIPIDAFPKTTSGKIQKFKLVEAF 581
Cdd:cd05908 419 GRVvaCGVNNSNTrNEEIFCFIEHRKSEDDFYPLGKKIKKhlNKRGGWQINE----VLPIRRIPKTTSGKVKRYELAQRY 494
|
....
gi 24581924 582 KAKE 585
Cdd:cd05908 495 QSGE 498
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
69-579 |
3.22e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.84 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 69 CHEGKRYSFKSLLQEADALAAGFRKLgLQPGDA--VGLW---APNYLHWylgMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:PRK13388 21 RYGDRTWTWREVLAEAAARAAALIAL-ADPDRPlhVGVLlgnTPEMLFW---LAAAALGGYVLVGLNTTRRGAALAADIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIapetfktqnyyeilrdicpeISDADTGKIRSEKFPHLRSVIIDSndslkgalrfDDFLDLASkseREEVAKM 223
Cdd:PRK13388 97 RADCQLLV--------------------TDAEHRPLLDGLDLPGVRVLDVDT----------PAYAELVA---AAGALTP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERIC-VQVPMFHAFGVIISIMAALTKGATMVLP 302
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCyVSMPLFHSNAVMAGWAPAVASGAAVALP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAgFSPKDSLQAI----------VNEKCSVIHGTPTMYVDLVNTqkkLQVPLGriKKAvtggaivSPQLIKDVRQVLNVE 372
Cdd:PRK13388 224 AK-FSASGFLDDVrrygatyfnyVGKPLAYILATPERPDDADNP---LRVAFG--NEA-------SPRDIAEFSRRFGCQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 373 aVHSVYGLTETTAVIFQ-------SLPGDSSDVVLNSVGHLTDHIEAkVVDAEGRCVPFGQP-GELCVRGYTTML-GYHD 443
Cdd:PRK13388 291 -VEDGYGSSEGAVIVVRepgtppgSIGRGAPGVAIYNPETLTECAVA-RFDAHGALLNADEAiGELVNTAGAGFFeGYYN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 444 DEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCA 523
Cdd:PRK13388 369 NPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMA 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 524 YVRLEegvDPASFTAETLKAY--AKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK13388 448 ALVLR---DGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
73-522 |
8.76e-31 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 126.77 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 73 KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLnpaYQ---GPEIAYCLNKVNVKA 149
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGI---YQdsmAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 IIAPETFKTQNYYEILrdicPEIsdadtgkirsekfPHLRSVIIDSNDSLKG-----ALRFDDFLDLASKSEREEVAKMQ 224
Cdd:cd17641 87 VIAEDEEQVDKLLEIA----DRI-------------PSVRYVIYCDPRGMRKyddprLISFEDVVALGRALDRRDPGLYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 KSIL---PESACNIQFTSGTTGNPKAACLTHHNFVN---NGIHVGNRneLEGERICVQVPMFHAFGVIISIMAALTKG-- 296
Cdd:cd17641 150 REVAagkGEDVAVLCTTSGTTGKPKLAMLSHGNFLGhcaAYLAADPL--GPGDEYVSVLPLPWIGEQMYSVGQALVCGfi 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 -------ATM------VLPAAGFSPKDSLQAIVNEKCSVI------------HGTPTMYVDLVNTQKKLQVPLG------ 345
Cdd:cd17641 228 vnfpeepETMmedlreIGPTFVLLPPRVWEGIAADVRARMmdatpfkrfmfeLGMKLGLRALDRGKRGRPVSLWlrlasw 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 346 -----------------RIKKAVTGGAIVSPQLIK-------DVRQVlnveavhsvYGLTETTAVIFQSLPGDssdVVLN 401
Cdd:cd17641 308 ladallfrplrdrlgfsRLRSAATGGAALGPDTFRffhaigvPLKQL---------YGQTELAGAYTVHRDGD---VDPD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 402 SVGHLTDHIEAKVVDAegrcvpfgqpGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKE- 480
Cdd:cd17641 376 TVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDv 445
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24581924 481 MLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVC 522
Cdd:cd17641 446 GTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLTAFIC 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-591 |
1.59e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.36 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 42 DPLVYRTIGQQLELSAsnfgdvEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAAR 121
Cdd:PRK12467 3094 ERLVHQLIEAQVARTP------EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLK 3167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 122 AGLTSVGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQNYyeILrdicpeisdadtgkirsEKFPHLRSVIidsndslkg 201
Cdd:PRK12467 3168 AGGAYVPLDPEYPRERLAYMIEDSGVKLLL------TQAH--LL-----------------EQLPAPAGDT--------- 3213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 202 ALRFDDfLDLASKSEREEVAkmqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFH 281
Cdd:PRK12467 3214 ALTLDR-LDLNGYSENNPST----RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 282 AFGVIISIMAALTKGATMVLpAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQvpLGRIKKAVTGGAIVSP 359
Cdd:PRK12467 3289 FDGAQERFLWTLICGGCLVV-RDNdlWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAD--CASLDIYVFGGEAVPP 3365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 360 QLIKDVRQVLNVEAVHSVYGLTETT-AVIFQSLPGDS-SDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTT 437
Cdd:PRK12467 3366 AAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAvCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGL 3445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 438 MLGYHDDEEKTKETIGND-------RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVI 510
Cdd:PRK12467 3446 ARGYHQRPSLTAERFVADpfsgsggRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL 3525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 511 GVPDERlGEEVCAYVRLEegvDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK-------FKLVEAFKA 583
Cdd:PRK12467 3526 ARDGAG-GKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRkalpdpdAKGSREYVA 3601
|
....*...
gi 24581924 584 KETELKAA 591
Cdd:PRK12467 3602 PRSEVEQQ 3609
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
64-577 |
3.39e-30 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 123.13 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIApetfktqnyyeilrdicpeisdadtgkirsekfphlrsviidsndslkgalrfddfldlasksereevakm 223
Cdd:cd17652 82 DARPALLLT----------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksiLPESACNIQFTSGTTGNPKAACLTHHNfvnngihVGNRNELEGERICVQ----VPMFHAF---GVIISIMAALTKG 296
Cdd:cd17652 91 ----TPDNLAYVIYTSGSTGRPKGVVVTHRG-------LANLAAAQIAAFDVGpgsrVLQFASPsfdASVWELLMALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 ATMVL-PAAGFSPKDSLQAIVNEKcSVIHGT-PTMYVDLVNTQkklQVPLGRIkkAVTGGAIVSPQLIK---DVRQVLNV 371
Cdd:cd17652 160 ATLVLaPAEELLPGEPLADLLREH-RITHVTlPPAALAALPPD---DLPDLRT--LVVAGEACPAELVDrwaPGRRMINA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 372 eavhsvYGLTETTAVIFQSLPGDSSDVVlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE- 450
Cdd:cd17652 234 ------YGPTETTVCATMAGPLPGGGVP--PIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAEr 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 -------TIGnDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGgENIFPKEIEDFLNAHPQVIEAhVIGVPDERLGEE-V 521
Cdd:cd17652 306 fvadpfgAPG-SRMYRTGDLARWRADGQLEFLGRADDQVkIRG-FRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDKrL 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 522 CAYVrleEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd17652 383 VAYV---VPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
75-511 |
7.63e-30 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 123.35 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPE 154
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 155 TfktqNYYEILRDICPEisdadtGKIRSEKFPHlrsviidsnDSLKGALRFDDFLDLASKSEREEVAKmqksilPESACN 234
Cdd:cd05932 87 L----DDWKAMAPGVPE------GLISISLPPP---------SAANCQYQWDDLIAQHPPLEERPTRF------PEQLAT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNF---VNNGI-HVGNRnelEGERICVQVPMFHAFGVIISIMAALTKGATMVLPaagfspkD 310
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFawaAQAGIeHIGTE---ENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFA-------E 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVNE----KCSVIHGTPTMYV-------DLVNTQK---KLQVP---------------LGRIKKAVTGGAIVSPQL 361
Cdd:cd05932 212 SLDTFVEDvqraRPTLFFSVPRLWTkfqqgvqDKIPQQKlnlLLKIPvvnslvkrkvlkglgLDQCRLAGCGSAPVPPAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 362 IKDVRQV-LNveaVHSVYGLTETTAVIFQSLPGDSSdvvLNSVGHLTDHIEAKVvdaegrcvpfGQPGELCVRGYTTMLG 440
Cdd:cd05932 292 LEWYRSLgLN---ILEAYGMTENFAYSHLNYPGRDK---IGTVGNAGPGVEVRI----------SEDGEILVRSPALMMG 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 441 YHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGENIFPKEIEDFLNAHPQVIEAHVIG 511
Cdd:cd05932 356 YYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
73-572 |
9.34e-30 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 123.84 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 73 KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAG-LTSV---GLNPAYQGPEIAYCLNKVNVK 148
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGaVHSVifgGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 149 AIIAPETFKTQNYYeilrdicPEISDADTGKIrsekfPHLRSVIIdsNDSLKGALRFDDFLDL------ASKSEREEVAK 222
Cdd:cd17634 163 ADGGVRAGRSVPLK-------KNVDDALNPNV-----TSVEHVIV--LKRTGSDIDWQEGRDLwwrdliAKASPEHQPEA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 223 MQksilPESACNIQFTSGTTGNPKAACLTHHNFVNNG---------IHVGNRNELEGEricVQVPMFHAFgviiSIMAAL 293
Cdd:cd17634 229 MN----AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAattmkyvfdYGPGDIYWCTAD---VGWVTGHSY----LLYGPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 294 TKGATMVL-------PAAGfspkdslqaivnEKCSVI--HGTPTMYvdLVNTQKKLQVPLGriKKAVTGGAIVSPQLIKD 364
Cdd:cd17634 298 ACGATTLLyegvpnwPTPA------------RMWQVVdkHGVNILY--TAPTAIRALMAAG--DDAIEGTDRSSLRILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 365 VRQVLNVEA--------------VHSVYGLTETTAVIFQSLPGdSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGEL 430
Cdd:cd17634 362 VGEPINPEAyewywkkigkekcpVVDTWWQTETGGFMITPLPG-AIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNL 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 431 CVR-----GYTTMLGYHDDEEKTKETIGNDRWLrTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVI 505
Cdd:cd17634 441 VITdpwpgQTRTLFGDHERFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 506 EAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17634 520 EAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
47-589 |
1.60e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQNYYeilrdicpeisdadtgkirSEKFPhlrsvIIDSNDSLkgalrfd 206
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLL------TQSHL-------------------LQRLP-----IPDGLASL------- 4671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 dFLDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVI 286
Cdd:PRK12316 4672 -ALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSH 4750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 287 ISIMAALTKGATMVLPAAGFS-PKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKlQVPLGRIKKAVTGGAIVSPQLIKDV 365
Cdd:PRK12316 4751 EGLYHPLINGASVVIRDDSLWdPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER-DGEPPSLRVYCFGGEAVAQASYDLA 4829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNVEAVHSVYGLTETTAVI--FQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHD 443
Cdd:PRK12316 4830 WRALKPVYLFNGYGPTETTVTVllWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLE 4909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 444 DEEKTKETIGND-------RWLRTGDQFVLEANGYGRIVGRLKEML-IRGGEnIFPKEIEDFLNAHPQVIEAHVIGVPDE 515
Cdd:PRK12316 4910 RPALTAERFVPDpfgapggRLYRTGDLARYRADGVIDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVIAQEGA 4988
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 516 rLGEEVCAYV-----RLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL--------VEAFK 582
Cdd:PRK12316 4989 -VGKQLVGYVvpqdpALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALpqpdasllQQAYV 5067
|
....*..
gi 24581924 583 AKETELK 589
Cdd:PRK12316 5068 APRSELE 5074
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
229-577 |
1.04e-28 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 119.01 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAG--F 306
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPKDSLQAIVNEKCSVIHGTPTMYVDLVN-TQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQ--VLNVEAvhsvYGLTET 383
Cdd:cd17649 173 SADELAEMVRELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALSPELLRRWLKapVRLFNA----YGPTEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 384 --TAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND------ 455
Cdd:cd17649 249 tvTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapg 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 -RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDErLGEEVCAYVRLEEGVDPA 534
Cdd:cd17649 329 sRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQP 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24581924 535 SfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd17649 408 E-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-577 |
1.30e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.37 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 42 DPLVYRTIGQQLELSAsnfgdvEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAAR 121
Cdd:PRK12316 2002 GPGVHQRIAEQAARAP------EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 122 AGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPETFktqnyyeilrdicpeisdadtgkirSEKFPHLRSVIidsndslkg 201
Cdd:PRK12316 2076 AGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHL-------------------------LERLPLPAGVA--------- 2121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 202 ALRFDDFLDLA-SKSEREEVAkmqksILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELeGERICVQVPMF 280
Cdd:PRK12316 2122 RLPLDRDAEWAdYPDTAPAVQ-----LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYEL-SPADCELQFMS 2195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 281 HAF-GVIISIMAALTKGATMVL-PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLgRIKKAVTGGAIVS 358
Cdd:PRK12316 2196 FSFdGAHEQWFHPLLNGARVLIrDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVP 2274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 359 PQLIKDVRQVLNVEAVHSVYGLTET--TAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYT 436
Cdd:PRK12316 2275 AASLRLAWEALRPVYLFNGYGPTEAvvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEG 2354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETIGND-------RWLRTGDQFVLEANGYGRIVGRLKEML-IRGGEnIFPKEIEDFLNAHPQVIEAH 508
Cdd:PRK12316 2355 LARGYLNRPGLTAERFVPDpfsasgeRLYRTGDLARYRADGVVEYLGRIDHQVkIRGFR-IELGEIEARLQAHPAVREAV 2433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 509 VIGVpDERLGEEVCAYVrleEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:PRK12316 2434 VVAQ-DGASGKQLVAYV---VPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
44-574 |
1.37e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 122.19 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 44 LVYRTIGQQLELSASNFGdveaivscheGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAG 123
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFG----------EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAG 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 124 LTSVGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQnyyeilRDICPEISDADTgkirsekfphLRSVIIDSNDSLkgal 203
Cdd:PRK12467 1649 GAYVPLDPEYPRERLAYMIEDSGIELLL------TQ------SHLQARLPLPDG----------LRSLVLDQEDDW---- 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 204 rfddfldLASKSEreevAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQvpmFHAF 283
Cdd:PRK12467 1703 -------LEGYSD----SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQ---FTSF 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 284 GVIIS---IMAALTKGATMVL--PAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLgRIKKAVTGGAIVS 358
Cdd:PRK12467 1769 AFDVSvweLFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPL-SLRRVVCGGEALE 1847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 359 PQLIKDVRQVLNVEAVHSVYGLTETTA-VIFQSL-PGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYT 436
Cdd:PRK12467 1848 VEALRPWLERLPDTGLFNLYGPTETAVdVTHWTCrRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVG 1927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETI-------GNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGEnIFPKEIEDFLNAHPQVIEAH 508
Cdd:PRK12467 1928 LARGYLNRPALTAERFvadpfgtVGSRLYRTGDLARYRADGVIEYLGRIDHQVkIRGFR-IELGEIEARLREQGGVREAV 2006
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 509 VIGVpDERLGEEVCAYV------RLEEGVDPASFtAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK12467 2007 VIAQ-DGANGKQLVAYVvptdpgLVDDDEAQVAL-RAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDR 2076
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
64-577 |
1.70e-28 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 119.12 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIAPETFKT---QNYYEILRDIcPEISDADTGKIRsekfphlrsvIIDSNDSLkgalrfddfldlasksereev 220
Cdd:cd17656 83 DSGVRVVLTQRHLKSklsFNKSTILLED-PSISQEDTSNID----------YINNSDDL--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 221 akmqksilpesaCNIQFTSGTTGNPKAACLTHHNFVN-NGIHVGNRNELEGERicvqVPMFHAFGVIIS---IMAALTKG 296
Cdd:cd17656 131 ------------LYIIYTSGTTGKPKGVQLEHKNMVNlLHFEREKTNINFSDK----VLQFATCSFDVCyqeIFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 ATM-VLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGR-IKKAVTGG-AIVSPQLIKDVRQVLNVeA 373
Cdd:cd17656 195 GTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTcVKHIITAGeQLVITNEFKEMLHEHNV-H 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 374 VHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETI- 452
Cdd:cd17656 274 LHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFf 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 -----GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRL 527
Cdd:cd17656 354 pdpfdPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24581924 528 EEGVdpasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd17656 434 EQEL-----NISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
72-555 |
3.35e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 117.67 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLH---WYLgmmgAA-RAGLTSVGLNPAYQGPEIAYCLNKVNV 147
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPEtllAYL----ALlQCGARVLPLNPQLPQPLLEELLPSLTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 148 KAIIAPETFKTqnyyeilrdicpeisdadtgkirsekFPHLRSVIIDSNDSLkGALRFDdfldlasksereevakmqksi 227
Cdd:PRK09029 102 DFALVLEGENT--------------------------FSALTSLHLQLVEGA-HAVAWQ--------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 228 lPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVgnrneLE------GERICVQVPMFHAFGVIIsIMAALTKGATMVL 301
Cdd:PRK09029 134 -PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGV-----LSlmpftaQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 PAAGfspkDSLQAIvnEKCSviHgtptmyVDLVNTQ-----KKLQVPLGrIKKAVTGGAIVSPQLIKDVRQvLNVEAvHS 376
Cdd:PRK09029 207 RDKQ----PLEQAL--AGCT--H------ASLVPTQlwrllDNRSEPLS-LKAVLLGGAAIPVELTEQAEQ-QGIRC-WC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 377 VYGLTET----TAVIFQSLPGdssdvvlnsVGHLTDHIEAKVVDaegrcvpfgqpGELCVRGYTTMLGYHDDEEKTKETi 452
Cdd:PRK09029 270 GYGLTEMastvCAKRADGLAG---------VGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVPLV- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 GNDRWLRTGDQFVLEaNGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVD 532
Cdd:PRK09029 329 NDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAA 407
|
490 500
....*....|....*....|...
gi 24581924 533 PASftaetLKAYAKGKLAHFKVP 555
Cdd:PRK09029 408 VVN-----LAEWLQDKLARFQQP 425
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
73-513 |
3.95e-28 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 118.85 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 73 KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAyqgpeiaycLNKVNVKAIIA 152
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPG---------MGIKNLKQCLA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 153 ---PETFKTQNYYEILRdicpeisdadtgKIRSEKFPHLRSVIIDSNDSLKGALRFDDFLDLASKSEREeVAKMQksilP 229
Cdd:PRK09274 111 eaqPDAFIGIPKAHLAR------------RLFGWGKPSVRRLVTVGGRLLWGGTTLATLLRDGAAAPFP-MADLA----P 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 230 ESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELE-GERICVQVPMFHAFGviisimAALtkGATMVLPAAGFS- 307
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEpGEIDLPTFPLFALFG------PAL--GMTSVIPDMDPTr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 -----PKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEA-VHSVYGLT 381
Cdd:PRK09274 246 patvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAeILTPYGAT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 382 EttavifqSLPGDS--SDVVLNS------------VGHLTDHIEAKVVD---------AEGRCVPFGQPGELCVRGYTTM 438
Cdd:PRK09274 326 E-------ALPISSieSREILFAtraatdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVT 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 439 LGYHDDEEKTKETIGNDR----WLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVP 513
Cdd:PRK09274 399 RSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-574 |
7.34e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 7.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 45 VYRTIGQQLELSAsnfgdvEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGL 124
Cdd:PRK12316 513 VHRLFEEQVERTP------EAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 125 TSVGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQNYYEILRDICPEISDADTGKIRSEkfphlrsviidsndslkgalr 204
Cdd:PRK12316 587 AYVPLDPEYPAERLAYMLEDSGVQLLL------SQSHLGRKLPLAAGVQVLDLDRPAAW--------------------- 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 205 fddfldLASKSEREEVAkmqkSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELE-GERICVQVPMfhAF 283
Cdd:PRK12316 640 ------LEGYSEENPGT----ELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGvGDTVLQKTPF--SF 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 284 GV-IISIMAALTKGATMVLPAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQV-PLGRIkkaVTGGAIVSP 359
Cdd:PRK12316 708 DVsVWEFFWPLMSGARLVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCtSLRRI---VCSGEALPA 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 360 QLIKDVRQVLNVEAVHSVYGLTETTA-VIFQSLPGDSSDVVlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTM 438
Cdd:PRK12316 785 DAQEQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGGDSV--PIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 439 LGYHDDEEKTKET------IGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV 512
Cdd:PRK12316 863 RGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 942
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 513 PderlGEEVCAYVRLEegvDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK12316 943 D----GKQLVGYVVLE---SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
229-572 |
1.07e-27 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 116.49 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQvpmF--HAFGV-IISIMAALTKGATMVLPAAg 305
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ---FasYTFDVsILEIFTTLAAGGCLCIPSE- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 306 FSPKDSLQAIVNE-KCSVIHGTPTMyVDLVNTQkklQVPlgRIKKAVTGGAIVSPQLI----KDVRqvlnveaVHSVYGL 380
Cdd:cd05918 181 EDRLNDLAGFINRlRVTWAFLTPSV-ARLLDPE---DVP--SLRTLVLGGEALTQSDVdtwaDRVR-------LINAYGP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 381 TETT--AVIFQSLPG-DSSDV--VLNSVGHltdhieakVVDAE--GRCVPFGQPGELCVRGYTTMLGYHDDEEKTKET-I 452
Cdd:cd05918 248 AECTiaATVSPVVPStDPRNIgrPLGATCW--------VVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 GNDRWL------------RTGDQFVLEANG---Y-GRIVGRLKemlIRG-----GenifpkEIEDFLNAHP---QVIEAH 508
Cdd:cd05918 320 EDPAWLkqegsgrgrrlyRTGDLVRYNPDGsleYvGRKDTQVK---IRGqrvelG------EIEHHLRQSLpgaKEVVVE 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 509 VIGVPDERLGEEVCAYVRL----EEGVDPASF----------TAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05918 391 VVKPKDGSSSPQLVAFVVLdgssSGSGDGDSLflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
51-577 |
1.42e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 115.88 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 51 QQLELSASNFGDVEAIVSCHEgkRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLN 130
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDE--SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 131 PAYQGPEIAYclnkvnvkaiiapetfktqnyyeILRDICPEIsdadtgkirsekfphlrsVIIDSNDslkgalrfddfld 210
Cdd:cd12115 81 PAYPPERLRF-----------------------ILEDAQARL------------------VLTDPDD------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASksereevakmqksilpesacnIQFTSGTTGNPKAACLTHHN---FVNNGIHVGNRNELEG----ERICVQVPMFHAF 283
Cdd:cd12115 107 LAY---------------------VIYTSGSTGRPKGVAIEHRNaaaFLQWAAAAFSAEELAGvlasTSICFDLSVFELF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 284 GviisimaALTKGATMVLPAAGFSPKDSLQAivnEKCSVIHGTPTMYVDLVNtQKKLQVPLGRIKKAvtgGAIVSPQLIK 363
Cdd:cd12115 166 G-------PLATGGKVVLADNVLALPDLPAA---AEVTLINTVPSAAAELLR-HDALPASVRVVNLA---GEPLPRDLVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 364 DVRQVLNVEAVHSVYGLTETT--AVIFQSLPGDSSDVvlnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGY 441
Cdd:cd12115 232 RLYARLQVERVVNLYGPSEDTtySTVAPVPPGASGEV---SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 442 HDDEEKTKETI------GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDE 515
Cdd:cd12115 309 LGRPGLTAERFlpdpfgPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 516 RLGEEVCAYVRLEegvDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd12115 389 AGERRLVAYIVAE---PGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
64-579 |
2.54e-27 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 114.71 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLN 143
Cdd:cd17653 12 DAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIAPetfktqnyyeilrdicpeisdadtgkirsekfphlrsviiDSNDslkgalrfddfldlasksereevakm 223
Cdd:cd17653 92 TSGATLLLTT----------------------------------------DSPD-------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 qksilpESACNIqFTSGTTGNPKAACLTHHN------FVNNGIHVGnrnelEGERIcVQVPMFhAFGVIIS-IMAALTKG 296
Cdd:cd17653 106 ------DLAYII-FTSGSTGIPKGVMVPHRGvlnyvsQPPARLDVG-----PGSRV-AQVLSI-AFDACIGeIFSTLCNG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 297 ATMVLPaagfSPKDSLQAiVNEKCSVIHGTPTMYVDLVNTqkklqvPLGRIKKAVTGGAIVSPQLIKD---VRQVLNVea 373
Cdd:cd17653 172 GTLVLA----DPSDPFAH-VARTVDALMSTPSILSTLSPQ------DFPNLKTIFLGGEAVPPSLLDRwspGRRLYNA-- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 374 vhsvYGLTETT-AVIFQSLPGDSSDVVLNSVGHLTDHIeakvVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETI 452
Cdd:cd17653 239 ----YGPTECTiSSTMTELLPGQPVTIGKPIPNSTCYI----LDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKF 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 GNDRW------LRTGDQFVLEANGYGRIVGRL-KEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIgVPDERLgeevCAYV 525
Cdd:cd17653 311 VPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREdNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI-VVNGRL----VAFV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24581924 526 RleegvdPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd17653 386 T------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
51-577 |
2.58e-27 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 114.96 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 51 QQLELSASNFGDVEAIVscHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLN 130
Cdd:cd17645 2 QLFEEQVERTPDHVAVV--DRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 131 PAYQGPEIAYCLNKVNVKAIIapetfktqnyyeilrdicpeiSDADtgkirsekfphlrsviidsndslkgalrfddflD 210
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILL---------------------TNPD---------------------------------D 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 211 LASksereevakmqksilpesacnIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVIISIM 290
Cdd:cd17645 106 LAY---------------------VIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 291 AALTKGATM-VLPAAGFSPKDSLQAIVNEKCSVIHGTPT----MYVDLVNTQkklqvplgrIKKAVTGGAIVSpQLIKDV 365
Cdd:cd17645 165 PHLTAGAALhVVPSERRLDLDALNDYFNQEGITISFLPTgaaeQFMQLDNQS---------LRVLLTGGDKLK-KIERKG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 366 RQVLNVeavhsvYGLTETTaVIFQSLPGDSSDVVLnSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDE 445
Cdd:cd17645 235 YKLVNN------YGPTENT-VVATSFEIDKPYANI-PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 446 EKTKET-IGN-----DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGE 519
Cdd:cd17645 307 ELTAEKfIVHpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRK 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 520 EVCAYVRLEEGVDPasftaETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd17645 387 YLVAYVTAPEEIPH-----EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
45-574 |
4.76e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.37 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 45 VYRTIGQQLELSAsnfgdvEAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGL 124
Cdd:PRK12316 3059 VHRLFEEQVERTP------DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGG 3132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 125 TSVGLNPAYQGPEIAYCLNkvnvkaiiapetfktqnyyeilrdicpeisdaDTGKIRSEKFPHLRSVIIDSNDSLkgalr 204
Cdd:PRK12316 3133 AYVPLDPEYPEERLAYMLE--------------------------------DSGAQLLLSQSHLRLPLAQGVQVL----- 3175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 205 fddflDLASKSEREEVAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFG 284
Cdd:PRK12316 3176 -----DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDV 3250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 285 VIISIMAALTKGATMVLPAAGF--SPKDSLQAIVNEKCSVIHGTPTMYVDLVntQKKLQVPLGRIKKAVTGGAIVSPQLI 362
Cdd:PRK12316 3251 FVEELFWPLMSGARVVLAGPEDwrDPALLVELINSEGVDVLHAYPSMLQAFL--EEEDAHRCTSLKRIVCGGEALPADLQ 3328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KdvrQVLNVEAVHSVYGLTETTaVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYH 442
Cdd:PRK12316 3329 Q---QVFAGLPLYNLYGPTEAT-ITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYH 3404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 443 DDEEKTKETIGND------RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDER 516
Cdd:PRK12316 3405 NRPGLTAERFVPDpfvpgeRLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ 3484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24581924 517 LgeevCAYVRLEegvDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK12316 3485 L----VAYVVPE---DEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
76-558 |
6.14e-27 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 114.62 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIApet 155
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 fktqnyyeilrdicpeisdadtgkirsekfphlrsviiDSNDSlkgalrfddfldlasksereevakmqksilpESACnI 235
Cdd:cd17639 84 --------------------------------------DGKPD-------------------------------DLAC-I 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFVNnGIH--VGNRNELEG--ERICVQVPMFHAFGVIISiMAALTKGATMvlpaaGF-SPK- 309
Cdd:cd17639 94 MYTSGSTGNPKGVMLTHGNLVA-GIAglGDRVPELLGpdDRYLAYLPLAHIFELAAE-NVCLYRGGTI-----GYgSPRt 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 310 ----------------------------DSLQAIVNEKCS--------------------VIHGTPTMYVDLVNTQKKLQ 341
Cdd:cd17639 167 ltdkskrgckgdltefkptlmvgvpaiwDTIRKGVLAKLNpmgglkrtlfwtayqsklkaLKEGPGTPLLDELVFKKVRA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 342 VPLGRIKKAVTGGAIVSPqlikDVRQVLNVEAVHSV--YGLTETTAVIFQSLPGDSSDvvlNSVGHLTDHIEAKVVD-AE 418
Cdd:cd17639 247 ALGGRLRYMLSGGAPLSA----DTQEFLNIVLCPVIqgYGLTETCAGGTVQDPGDLET---GRVGPPLPCCEIKLVDwEE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 419 GRCVPFGQP--GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGENIFPKEIE 495
Cdd:cd17639 320 GGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 496 DFLNAHPQV--IEAHV---------IGVPDE--------RLG------EEVCAYVRLEEGVdpasfTAETLKAYAKGKLA 550
Cdd:cd17639 400 SIYRSNPLVnnICVYAdpdksypvaIVVPNEkhltklaeKHGvinsewEELCEDKKLQKAV-----LKSLAETARAAGLE 474
|
....*...
gi 24581924 551 HFKVPRYV 558
Cdd:cd17639 475 KFEIPQGV 482
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
75-576 |
3.34e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.18 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 75 YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLN-PAYQGPEIAYC------LNKVNV 147
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIaqlrgmLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 148 KAIIAPEtfktqnyyeilrDICPEISDADTGKirsekfphlrsviidsndSLKGALRFDDFLdlasksEREEVAKMQKSI 227
Cdd:PRK09192 130 AAIITPD------------ELLPWVNEATHGN------------------PLLHVLSHAWFK------ALPEADVALPRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 228 LPESACNIQFTSGTTGNPKAACLTHHNFVNN-------GIHVGnrnelEGERiCVQ-VPMFHAFGVIISIMAALTKGATM 299
Cdd:PRK09192 174 TPDDIAYLQYSSGSTRFPRGVIITHRALMANlraishdGLKVR-----PGDR-CVSwLPFYHDMGLVGFLLTPVATQLSV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 300 -VLPAAGFS--PKDSLQAIVNEKCSVIHgTPTMYVDL----VNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVrqvlnVE 372
Cdd:PRK09192 248 dYLPTRDFArrPLQWLDLISRNRGTISY-SPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQF-----AE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 373 AVHSV----------YGLTETT-AVIF--------------QSLPGDSSDVVLNSVGH-----------LTDHiEAKVVD 416
Cdd:PRK09192 322 AFAPAgfddkafmpsYGLAEATlAVSFsplgsgivveevdrDRLEYQGKAVAPGAETRrvrtfvncgkaLPGH-EIEIRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 417 AEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKeTIGNDRWLRTGDQFVLeANGYGRIVGRLKEMLIRGGENIFPKEIED 496
Cdd:PRK09192 401 EAGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEW 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 497 FLNAHPQVI--EAHVIGVPDERlGEEVCAYV--RLEEGVDPASftaetLKAYAKGKL-AHFKVPRYVI--PIDAFPKTTS 569
Cdd:PRK09192 479 IAEQEPELRsgDAAAFSIAQEN-GEKIVLLVqcRISDEERRGQ-----LIHALAALVrSEFGVEAAVElvPPHSLPRTSS 552
|
....*..
gi 24581924 570 GKIQKFK 576
Cdd:PRK09192 553 GKLSRAK 559
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
224-572 |
3.95e-26 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 111.76 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSIL---PESACNIQFTSGTTGNPKAACLTHHNFVN--NGIHvgnrnELEGERICVQVPMFHAFGVIIS---IMAALTK 295
Cdd:cd17644 97 QISVLltqPENLAYVIYTSGSTGKPKGVMIEHQSLVNlsHGLI-----KEYGITSSDRVLQFASIAFDVAaeeIYVTLLS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 296 GATMVL-PAAGF-SPKDSLQAIVNEKCSVIHGTPTMYVDLVN--TQKKLQVPlGRIKKAVTGGAIVSPQLIKDVRQVL-N 370
Cdd:cd17644 172 GATLVLrPEEMRsSLEDFVQYIQQWQLTVLSLPPAYWHLLVLelLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVgN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 371 VEAVHSVYGLTE-TTAVIFQSLPGDSSDVVLN-SVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKT 448
Cdd:cd17644 251 FIQLINVYGPTEaTIAATVCRLTQLTERNITSvPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 449 KETIGND--------RWLRTGDQFVLEANG----YGRIVGRLKemlIRGGEnIFPKEIEDFLNAHPQVIEAHVIGVPDER 516
Cdd:cd17644 331 AEKFISHpfnsseseRLYKTGDLARYLPDGnieyLGRIDNQVK---IRGFR-IELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24581924 517 LGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17644 407 GNKRLVAYIVPHYEESP---STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
229-577 |
7.43e-26 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 110.98 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAA------CLTHHNFVNNGIHVGNrneleGERICVQVPMFHAFGVIISIMAALTKGATMVLp 302
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAaiswrrTLVTSNLLSHDLNLKN-----GDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAGFSPK-------DSLQAI---VNEKCS-VIHGTPTMYvdlvntQKKLQVplgrikKAVTGGAIvSPQLIKDVRQVLNV 371
Cdd:cd05937 160 SRKFSASqfwkdvrDSGATIiqyVGELCRyLLSTPPSPY------DRDHKV------RVAWGNGL-RPDIWERFRERFNV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 372 EAVHSVYGLTETTAVIFQSLPGD-----------------SSDVVLNSVGHLTDHIEAKvvDAEGRCV--PFGQPGELCV 432
Cdd:cd05937 227 PEIGEFYAATEGVFALTNHNVGDfgagaighhglirrwkfENQVVLVKMDPETDDPIRD--PKTGFCVraPVGEPGEMLG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 433 R----GYTTMLGYHDDEEKTKETI------GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHP 502
Cdd:cd05937 305 RvpfkNREAFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHP 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 503 QVIEAHVIGVP----DERLGeevCAYVRLEE-GVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd05937 385 DIAEANVYGVKvpghDGRAG---CAAITLEEsSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
237-580 |
9.18e-26 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 110.35 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKAACLTHHNFvnngiHVGNRNEL------EGE-RICVQVPMF--HAFGviiSIMAALTKGATMVL-PAAGF 306
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSY-----PVGHLSTMywiglkPGDvHWNISSPGWakHAWS---CFFAPWNAGATVFLfNYARF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQ-KKLQVPLgriKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTA 385
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLIQQDlASFDVKL---REVVGAGEPLNPEVIEQVRRAWGL-TIRDGYGQTETTA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 386 VIFQSlPGdsSDVVLNSVGHLTDHIEAKVVDAEGRCVpfgQPGELCV-----RGYTTMLGYHDDEEKTKETIGnDRWLRT 460
Cdd:cd05974 240 LVGNS-PG--QPVKAGSMGRPLPGYRVALLDPDGAPA---TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 461 GDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPD-ERLGEEVcAYVRLEEGVDPASFTAE 539
Cdd:cd05974 313 GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDpVRLSVPK-AFIVLRAGYEPSPETAL 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24581924 540 TLKAYAKGKLAHFKVPRYvIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:cd05974 392 EIFRFSRERLAPYKRIRR-LEFAELPKTISGKIRRVELRRR 431
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
236-574 |
2.29e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 110.09 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFVNN--GIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLpaagFSPKDSLQ 313
Cdd:PRK07768 158 QLTSGSTGSPKAVQITHGNLYANaeAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVK----VTPMDFLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 314 AIV--NEKCSVIHGTPTM-----YV----DLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKD-----VRQVLNVEAVHSV 377
Cdd:PRK07768 234 DPLlwAELISKYRGTMTAapnfaYAllarRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDlldagARFGLRPEAILPA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 378 YGLTETT-AVIF---------------------QSLPGDSSDVV-LNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRG 434
Cdd:PRK07768 314 YGMAEATlAVSFspcgaglvvdevdadllaalrRAVPATKGNTRrLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 435 ------YTTMLGyhddeekTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDflnahpqvIEAH 508
Cdd:PRK07768 394 esvtpgYLTMDG-------FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER--------AAAR 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 509 VIGVpdeRLGEEVCayVRLEEGVDPASFT--AET------------LKAYAKGKLAHFKV-PR--YVIPIDAFPKTTSGK 571
Cdd:PRK07768 459 VEGV---RPGNAVA--VRLDAGHSREGFAvaVESnafedpaevrriRHQVAHEVVAEVGVrPRnvVVLGPGSIPKTPSGK 533
|
...
gi 24581924 572 IQK 574
Cdd:PRK07768 534 LRR 536
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-580 |
4.78e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 109.33 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 65 AIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIA-YCLN 143
Cdd:PRK05857 32 ALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIErFCQI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIAPEtfktqnyyeilrdicpeisdadtGKIRSEKFPH-LRSVIIDSNDSLKGALRFDDFLDLASksereevAK 222
Cdd:PRK05857 112 TDPAAALVAPG-----------------------SKMASSAVPEaLHSIPVIAVDIAAVTRESEHSLDAAS-------LA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 223 MQKSILPESACNIQFTSGTTGNPKAACLTHHNFVnnGIHVGNRNE-------LEGERICVQVPMFHaFGVIISIMAALTK 295
Cdd:PRK05857 162 GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFF--AVPDILQKEglnwvtwVVGETTYSPLPATH-IGGLWWILTCLMH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 296 GATMVlpaAGFSPKDSLQAI-----VNEKCSVihgtPTMYVDLVNTQKKLQVPLGRIKKAVTGGaivSPQLIKDVRqVLN 370
Cdd:PRK05857 239 GGLCV---TGGENTTSLLEIlttnaVATTCLV----PTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVR-FIE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 371 VEAVHS--VYGLTET--TAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGR--CVPFGQP----GELCVRGYTTMLG 440
Cdd:PRK05857 308 ATGVRTaqVYGLSETgcTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgpTAPGAGPsasfGTLWIKSPANMLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 441 YHDDEEKTKETIGnDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEE 520
Cdd:PRK05857 388 YWNNPERTAEVLI-DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581924 521 VCAYVRLEEGVDPASFTA--ETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEA 580
Cdd:PRK05857 467 VGLAVVASAELDESAARAlkHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
64-572 |
5.37e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 108.51 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYqgPeiaycln 143
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQ--P------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 KVNVKAIIApetfktqnyyeilrdicpeisDAdtgkirsekfpHLRSVIIDSNDSLKGALRFDDFLDLASKSEREEVAKM 223
Cdd:cd12114 73 AARREAILA---------------------DA-----------GARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSILPESACNIqFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPA 303
Cdd:cd12114 121 VDVAPDDLAYVI-FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 304 AG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLT 381
Cdd:cd12114 200 EArrRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGAT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 382 ETT--AVIFQSLPGDSSDVvlnSV--GHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND-- 455
Cdd:cd12114 280 EASiwSIYHPIDEVPPDWR---SIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHpd 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 --RWLRTGDQFVLEANGY----GRIVGRLKemlIRgGENIFPKEIEDFLNAHPQVIEAHVIGVpDERLGEEVCAYVRLEE 529
Cdd:cd12114 357 geRLYRTGDLGRYRPDGTleflGRRDGQVK---VR-GYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDN 431
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24581924 530 GVDPASftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd12114 432 DGTPIA--PDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
273-581 |
1.15e-24 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 107.00 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 273 ICVqVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCsvihgtptmyVDLVNTQKK--LQVP---LGRI 347
Cdd:PRK07445 164 FCV-LPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSGQELPPNPSDFF----------LSLVPTQLQrlLQLRpqwLAQF 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 KKAVTGGAIVSPQLIKDVRQvlnveavHSV-----YGLTETTAVIFQSLPGDSSDVVlNSVGHLTDHIEAKVVDaegrcv 422
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQARQ-------LQLrlaptYGMTETASQIATLKPDDFLAGN-NSSGQVLPHAQITIPA------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 423 pfGQPGELCVRGYTTMLGYHddeektKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHP 502
Cdd:PRK07445 299 --NQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 503 QVIEAHVIGVPDERLGEEVCA-YVrleeGVDPaSFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAF 581
Cdd:PRK07445 371 LVQDVCVLGLPDPHWGEVVTAiYV----PKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-546 |
1.66e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 108.26 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 86 ALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVglnPAYQ--GPE-IAYCLNKVNVKAI-IAPETFKTqny 161
Cdd:PLN02736 90 AIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSV---PLYDtlGPDaVKFIVNHAEVAAIfCVPQTLNT--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 162 yeiLRDICPEIsdadtgkirsekfPHLRSVIIDSND-----SLKGA-----LRFDDFLDLASKSEREEVAKMqksilPES 231
Cdd:PLN02736 164 ---LLSCLSEI-------------PSVRLIVVVGGAdeplpSLPSGtgveiVTYSKLLAQGRSSPQPFRPPK-----PED 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 232 ACNIQFTSGTTGNPKAACLTHHNFVNNGihVGNRNELEG----------------ERIcVQVPMFHaFGVIISI------ 289
Cdd:PLN02736 223 VATICYTSGTTGTPKGVVLTHGNLIANV--AGSSLSTKFypsdvhisylplahiyERV-NQIVMLH-YGVAVGFyqgdnl 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 290 -----MAALT---------------KGATMVLPAAGFSPKDSLQAIVN-EKCSVIHGTPT--MYVDLVNTqkKLQVPLG- 345
Cdd:PLN02736 299 klmddLAALRptifcsvprlynriyDGITNAVKESGGLKERLFNAAYNaKKQALENGKNPspMWDRLVFN--KIKAKLGg 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 346 RIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTAVIFQSLPGDssdvvlNSVGHL---TDHIEAKVVDaegrcV 422
Cdd:PLN02736 377 RVRFMSSGASPLSPDVMEFLRICFGGR-VLEGYGMTETSCVISGMDEGD------NLSGHVgspNPACEVKLVD-----V 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 423 P------FGQP---GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGENIFPK 492
Cdd:PLN02736 445 PemnytsEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPE 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 24581924 493 EIEDFLNAHPQVIEAHVIGvpdERLGEEVCAYVrleeGVDPasftaETLKAYAK 546
Cdd:PLN02736 525 KIENVYAKCKFVAQCFVYG---DSLNSSLVAVV----VVDP-----EVLKAWAA 566
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
235-572 |
2.88e-23 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 102.86 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVqVPMF--HAFGVIISIMA-ALTKGATM-VLPAAGFSPKD 310
Cdd:cd17648 99 AIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEA-VLFFsnYVFDFFVEQMTlALLNGQKLvVPPDEMRFDPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIVN-EKCSVIHGTPTMYVdlvntqkklQVPLGRIK--KAVT--GGAIVSPQLIKdVRQ-----VLNVeavhsvYGL 380
Cdd:cd17648 178 RFYAYINrEKVTYLSGTPSVLQ---------QYDLARLPhlKRVDaaGEEFTAPVFEK-LRSrfaglIINA------YGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 381 TET--TAVIFQSLPGDSSDvvlNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETI------ 452
Cdd:cd17648 242 TETtvTNHKRFFPGDQRFD---KSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfq 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 453 --------GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEE---- 520
Cdd:cd17648 319 teqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqk 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24581924 521 --VCAYVRLEEGVDPASftaetLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd17648 399 ylVGYYLPEPGHVPESD-----LLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
493-571 |
4.39e-23 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 92.99 E-value: 4.39e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 493 EIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
410-572 |
1.11e-22 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 102.25 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 410 IEAKVVDAEGRCVPFGQPGELCV-RGYTTML-GYHDDEEKTKETIgndrWLR------TGDQFVLEANGYGRIVGRLKEM 481
Cdd:cd05966 419 IEPAILDEEGNEVEGEVEGYLVIkRPWPGMArTIYGDHERYEDTY----FSKfpgyyfTGDGARRDEDGYYWITGRVDDV 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 482 LIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPI 561
Cdd:cd05966 495 INVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFV 574
|
170
....*....|.
gi 24581924 562 DAFPKTTSGKI 572
Cdd:cd05966 575 PGLPKTRSGKI 585
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
64-591 |
1.46e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.32 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCln 143
Cdd:PRK05691 2203 QAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYM-- 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 kvnvkaiiapetfktqnyyeilrdicpeISDADTGKIRSEKfphlrsVIIDSNDSL-KGALRF---DDFLDLASKSEree 219
Cdd:PRK05691 2281 ----------------------------IEDSGIGLLLSDR------ALFEALGELpAGVARWcleDDAAALAAYSD--- 2323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 220 vAKMQKSILPESACNIQFTSGTTGNPKAACLTHHNFvnnGIHvgnrnelegeriCVQVpmFHAFGV--------IISI-- 289
Cdd:PRK05691 2324 -APLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEI---AMH------------CQAV--IERFGMraddcelhFYSInf 2385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 290 -------MAALTKGATMVLPAAG-FSPKDSLQAIVNEKCSVIHGTPTMYVDL---VNTQKKlQVPlgrIKKAVTGGAIVS 358
Cdd:PRK05691 2386 daaserlLVPLLCGARVVLRAQGqWGAEEICQLIREQQVSILGFTPSYGSQLaqwLAGQGE-QLP---VRMCITGGEALT 2461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 359 PQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSDVVLNSV--GHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYT 436
Cdd:PRK05691 2462 GEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVpiGRVVGARVAYILDADLALVPQGATGELYVGGAG 2541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 437 TMLGYHDDEEKTKETIGND-------RWLRTGDQFVLEANGYGRIVGRLKEML-IRGGEnIFPKEIEDFLNAHPQVIEAH 508
Cdd:PRK05691 2542 LAQGYHDRPGLTAERFVADpfaadggRLYRTGDLVRLRADGLVEYVGRIDHQVkIRGFR-IELGEIESRLLEHPAVREAV 2620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 509 VIGVpDERLGEEVCAYV---RLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL-------- 577
Cdd:PRK05691 2621 VLAL-DTPSGKQLAGYLvsaVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALpapdpeln 2699
|
570
....*....|....
gi 24581924 578 VEAFKAKETELKAA 591
Cdd:PRK05691 2700 RQAYQAPRSELEQQ 2713
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-579 |
1.73e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.94 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSchEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVW--DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAY 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIapetfktqnyyeilrdicpeisdadTGKIRSEKFPHLRSVIIDSNDSLKgalrfd 206
Cdd:PRK05691 1209 VPLDPDYPAERLAYMLADSGVELLL-------------------------TQSHLLERLPQAEGVSAIALDSLH------ 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 dfldLASKSEREEVAKMQKSILpesaCNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQ-VPMfhAFGV 285
Cdd:PRK05691 1258 ----LDSWPSQAPGLHLHGDNL----AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQkAPI--SFDV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 II-SIMAALTKGATMVLPAAG--FSPKDSLQAIVNEKCSVIHGTPTMYVDLVntQKKLQVPLGRIKKAVTGGAIVSPQLI 362
Cdd:PRK05691 1328 SVwECFWPLITGCRLVLAGPGehRDPQRIAELVQQYGVTTLHFVPPLLQLFI--DEPLAAACTSLRRLFSGGEALPAELR 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQVLNVEAVHSVYGLTEtTAVIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYH 442
Cdd:PRK05691 1406 NRVLQRLPQVQLHNRYGPTE-TAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYL 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 443 DDEEKTKE-----TIGND--RWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIgVPDE 515
Cdd:PRK05691 1485 GRPALTAErfvpdPLGEDgaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREG 1563
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 516 RLGEEVCAYVRLEEGVDPAsftAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:PRK05691 1564 AAGAQLVGYYTGEAGQEAE---AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
235-580 |
1.44e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 97.41 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNfVNNGIHVGNR--NELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGfSPKDSL 312
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTE-IDREIEAYNEalNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNK-NPKFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYvdlvNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQvlNVEAVHSVYGLTETTAVifqSLP 392
Cdd:PRK08308 184 NILRNTPQHILYAVPLML----HILGRLLPGTFQFHAVMTSGTPLPEAWFYKLRE--RTTYMMQQYGCSEAGCV---SIC 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 393 GDSSDVvlNSVGHLTDHIEAKVVDAEGrcvpfgQPGELCVRGyttmlgyhddeektketigNDRWLRTGDQFVLEANGYG 472
Cdd:PRK08308 255 PDMKSH--LDLGNPLPHVSVSAGSDEN------APEEIVVKM-------------------GDKEIFTKDLGYKSERGTL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASftaetLKAYAKGKLAHF 552
Cdd:PRK08308 308 HFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQ-----LREWCIQHLAPY 382
|
330 340
....*....|....*....|....*...
gi 24581924 553 KVPRYVIPIDAFPKTTSGKIQKfKLVEA 580
Cdd:PRK08308 383 QVPHEIESVTEIPKNANGKVSR-KLLEL 409
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
71-572 |
3.74e-21 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 98.58 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAI 150
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 IAPETFktqnyyeilrdicpeisdadtgkirSEKFPHLRSVIIDSNDSLkgalrfddfldLASKSEREEVakmqkSILPE 230
Cdd:PRK10252 560 ITTADQ-------------------------LPRFADVPDLTSLCYNAP-----------LAPQGAAPLQ-----LSQPH 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMfhAFGVII-----SIMAaltkGATMVL--P 302
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLtADDVVLQKTPC--SFDVSVweffwPFIA----GAKLVMaeP 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVN--TQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEaVHSVYGL 380
Cdd:PRK10252 673 EAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVAslTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAP-LHNLYGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 381 TETtAV---IFQSLPGDSSDVVLNSV--GHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGND 455
Cdd:PRK10252 752 TEA-AVdvsWYPAFGEELAAVRGSSVpiGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAD 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 456 ------RWLRTGDQFVLEANGYGRIVGRLKEML-IRGgENIFPKEIEDFLNAHPQVIEAH----VIGVPDERLGEE--VC 522
Cdd:PRK10252 831 pfapgeRMYRTGDVARWLDDGAVEYLGRSDDQLkIRG-QRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLV 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24581924 523 AYVRLEEGvdpASFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK10252 910 GYLVSQSG---LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
73-572 |
7.17e-21 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 96.62 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 73 KRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLT-SV---GLNPAYQGPEIAYCLNKVNVK 148
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhSVvfgGFAAKELASRIDDAKPKLIVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 149 AIIAPETFKTQNYYEILRDicpEISDADTgkirseKFPHlrsVIIDSNDSLKGAL----RFDDFLDLASKSEREEVAkmq 224
Cdd:cd05967 161 ASCGIEPGKVVPYKPLLDK---ALELSGH------KPHH---VLVLNRPQVPADLtkpgRDLDWSELLAKAEPVDCV--- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 kSILPESACNIQFTSGTTGNPK---------AACLTHHNFVNNGIHVGNrnelegericvqvpMFHA-------FGVIIS 288
Cdd:cd05967 226 -PVAATDPLYILYTSGTTGKPKgvvrdngghAVALNWSMRNIYGIKPGD--------------VWWAasdvgwvVGHSYI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 289 IMAALTKGATMVL--------PAAG--------------FSPKDSLQAIVNEKCSVIHGTptmyvdlvntqkklQVPLGR 346
Cdd:cd05967 291 VYGPLLHGATTVLyegkpvgtPDPGafwrviekyqvnalFTAPTAIRAIRKEDPDGKYIK--------------KYDLSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 347 IKKAVTGGAIVSPQLIKDVRQVLNVeAVHSVYGLTETTAVIFQSLPG-DSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFG 425
Cdd:cd05967 357 LRTLFLAGERLDPPTLEWAENTLGV-PVIDHWWQTETGWPITANPVGlEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 426 QPGELCVRGY---TTMLGYHDDEEKTKET-IGNDR-WLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNA 500
Cdd:cd05967 436 ELGNIVIKLPlppGCLLTLWKNDERFKKLyLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLS 515
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24581924 501 HPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAET-LKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:cd05967 516 HPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
238-581 |
7.72e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 94.34 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 238 TSGTTGNPKAACLTHHNFVNNGIHVGNRneLEGE-RICVQVPMFHAFGV---IISIMAALTKGATMVlpAAGFSPKDsLQ 313
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDR--LGGPgQWLLALPAHHIAGLqvlVRSVIAGSEPVELDV--SAGFDPTA-LP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 314 AIVNEKcsvihGTPTMYVDLVNTQ--KKLQVP-----LGRIKKAVTGGAIVSPQLIKDVRQvLNVEAVHSvYGLTETTA- 385
Cdd:PRK07824 118 RAVAEL-----GGGRRYTSLVPMQlaKALDDPaataaLAELDAVLVGGGPAPAPVLDAAAA-AGINVVRT-YGMSETSGg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 386 VIFQSLPGDSsdvvlnsvghltdhieAKVVDAEGRcVPFGqpGELCVRGYTTMLGYHDDEEKTketigndrWLRTGDQFV 465
Cdd:PRK07824 191 CVYDGVPLDG----------------VRVRVEDGR-IALG--GPTLAKGYRNPVDPDPFAEPG--------WFRTDDLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 466 LEaNGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPasfTAETLKAYA 545
Cdd:PRK07824 244 LD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAP---TLEALRAHV 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 24581924 546 KGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKLVEAF 581
Cdd:PRK07824 320 ARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
47-572 |
1.72e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.19 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 47 RTIGQQLELSASNFGDVEAIVSCHEGKRYSFKSLLQEADALAAGFRKlGLQPGDAVGLWAPNylhwylgMMGAARA--GL 124
Cdd:PRK06814 631 RTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPN-------ANGAAVTffAL 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 125 TSVGLNPAY----QGPE--IAYClNKVNVKAIIAPETFktqnyyeilrdicpeISDADTGKIRSEKFPHLRSVIIDSnds 198
Cdd:PRK06814 703 QSAGRVPAMinfsAGIAniLSAC-KAAQVKTVLTSRAF---------------IEKARLGPLIEALEFGIRIIYLED--- 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 199 LKGALRFDDFLDLASKSEREEVAKMQKSilPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV- 277
Cdd:PRK06814 764 VRAQIGLADKIKGLLAGRFPLVYFCNRD--PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNAl 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 278 PMFHAFGviisimaaLTKGatMVLPA-AGF------SPKDSL---QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVplgRI 347
Cdd:PRK06814 842 PVFHSFG--------LTGG--LVLPLlSGVkvflypSPLHYRiipELIYDTNATILFGTDTFLNGYARYAHPYDF---RS 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 348 KKAVTGGAivspQLIKD-VRQV-LNVEAVHSV--YGLTETTAVIFQSLPGDSSdvvLNSVGHLTDHIEAKVVDAEGrcVP 423
Cdd:PRK06814 909 LRYVFAGA----EKVKEeTRQTwMEKFGIRILegYGVTETAPVIALNTPMHNK---AGTVGRLLPGIEYRLEPVPG--ID 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 424 FGqpGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNA-HP 502
Cdd:PRK06814 980 EG--GRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWP 1057
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 503 QVIEAhVIGVPDERLGEEVcayVRLEEGVDpasFTAETLKAYAKGK-LAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK06814 1058 DALHA-AVSIPDARKGERI---ILLTTASD---ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
71-579 |
5.04e-20 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 93.51 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRK-LGLQPGDAVGLW---APNYLHWYLGMmgaARAGLTSVGLNPAYQGPEIAYCLNKVN 146
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLlgnEPAFLWIWLGL---AKLGCPVAFLNTNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 147 VKA-IIAPETFktqnyyEILRDICPEISDADtgkirsekfphLRSVIIDSNDSLKGalrFDDFLDLASKSEREEV-AKMQ 224
Cdd:cd05938 79 AKVlVVAPELQ------EAVEEVLPALRADG-----------VSVWYLSHTSNTEG---VISLLDKVDAASDEPVpASLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 KSILPESACNIQFTSGTTGNPKAACLTHHNFvnngIHVGNRNELEGER----ICVQVPMFHAFGVIISIMAALTKGATMV 300
Cdd:cd05938 139 AHVTIKSPALYIYTSGTTGLPKAARISHLRV----LQCSGFLSLCGVTaddvIYITLPLYHSSGFLLGIGGCIELGATCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 LpAAGFSP----KDSLQAIVnekcSVIH--GTPTMYvdLVNTQKKLQVPLGRIKKAVTGGaiVSPQLIKD-VRQVLNVEa 373
Cdd:cd05938 215 L-KPKFSAsqfwDDCRKHNV----TVIQyiGELLRY--LCNQPQSPNDRDHKVRLAIGNG--LRADVWREfLRRFGPIR- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 374 VHSVYGLTETTaVIFQSLPGDSSDVvlNSVGHLTDHI------------EAKVVDAEGRC--VPFGQPGELC--VRGYTT 437
Cdd:cd05938 285 IREFYGSTEGN-IGFFNYTGKIGAV--GRVSYLYKLLfpfelikfdvekEEPVRDAQGFCipVAKGEPGLLVakITQQSP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 438 MLGYHDDEEKTKETI------GNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIG 511
Cdd:cd05938 362 FLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24581924 512 VP----DERLGeevCAYVRLEEG-----VDPASFTAETLKAYAKgklahfkvPRYVIPIDAFPKTTSGKIQKFKLVE 579
Cdd:cd05938 442 VTvpghEGRIG---MAAVKLKPGhefdgKKLYQHVREYLPAYAR--------PRFLRIQDSLEITGTFKQQKVRLVE 507
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
238-544 |
1.67e-19 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 90.98 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 238 TSGTTGNPKAACLThhnfvnngihvgnRNELEGERICVQvPMFHAFGV----IISIMA---------ALTKGAT----MV 300
Cdd:COG1541 91 SSGTTGKPTVVGYT-------------RKDLDRWAELFA-RSLRAAGVrpgdRVQNAFgyglftgglGLHYGAErlgaTV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 301 LPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGR--IKKAVTGGAIVSPQLIKDVRQVLNVEAVhSVY 378
Cdd:COG1541 157 IPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDlsLKKGIFGGEPWSEEMRKEIEERWGIKAY-DIY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 379 GLTETTAVIFQSLPGDSSdvvlnsvGHL-TDHIEAKVVDAE-GRCVPFGQPGELCVrgytTMLgyhddeekTKET---Ig 453
Cdd:COG1541 236 GLTEVGPGVAYECEAQDG-------LHIwEDHFLVEIIDPEtGEPVPEGEEGELVV----TTL--------TKEAmplI- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 454 ndRWlRTGD--QFVLEANGYGR-------IVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAY 524
Cdd:COG1541 296 --RY-RTGDltRLLPEPCPCGRthprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVR 372
|
330 340
....*....|....*....|...
gi 24581924 525 VRLEEGVDPASFT---AETLKAY 544
Cdd:COG1541 373 VELAPGASLEALAeaiAAALKAV 395
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
74-565 |
1.20e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.06 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 74 RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAp 153
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 154 etfktqnyyeilrdicpeISDADtgkirsekfphlrsviidsndslkgalrfddfldlasksereEVAKmqksilpesac 233
Cdd:cd05910 81 ------------------IPKAD------------------------------------------EPAA----------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 234 nIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIIsimaaltkGATMVLPA------AGF 306
Cdd:cd05910 90 -ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrPGEVDLATFPLFALFGPAL--------GLTSVIPDmdptrpARA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 307 SPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEA-VHSVYGLTEtta 385
Cdd:cd05910 161 DPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATE--- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 386 vifqSLPGDS--SDVVLNS------------VGHLTDHIEAKVV--DAEG-------RCVPFGQPGELCVRGYTTMLGYH 442
Cdd:cd05910 238 ----ALPVSSigSRELLATttaatsggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYV 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 443 DDEEKTK----ETIGNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV--PDER 516
Cdd:cd05910 314 NRPVATAlakiDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGCQ 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24581924 517 LGeeVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPiDAFP 565
Cdd:cd05910 394 LP--VLCVEPLPGTITPRARLEQELRALAKDYPHTQRIGRFLIH-PSFP 439
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
235-574 |
2.38e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 88.28 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEG--ERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGF--SPKD 310
Cdd:PRK05851 157 LQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAatDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFsaSPFR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 311 SLQAIvNEKCSVIHGTPTMYVDLVN--TQKKLQVPLGRIKKAVTGGAIVSPQ-----LIKDVRQVLNVEAVHSVYGLTET 383
Cdd:PRK05851 237 WLSWL-SDSRATLTAAPNFAYNLIGkyARRVSDVDLGALRVALNGGEPVDCDgferfATAMAPFGFDAGAAAPSYGLAES 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 384 TAVIFQSLPGDS---SDVVLNS---------VGHLTDHIEAKVVDAEGRCVPFGQP-GELCVRGYTTMLGYHDDEektke 450
Cdd:PRK05851 316 TCAVTVPVPGIGlrvDEVTTDDgsgarrhavLGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGASMMSGYLGQA----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 TIGNDRWLRTGDQFVLEANGYgRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV-PDE---RLGEEVCAYVR 526
Cdd:PRK05851 391 PIDPDDWFPTGDLGYLVDGGL-VVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEgsaRPGLVIAAEFR 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24581924 527 leeGVDPASFTAETLKAYAK--GklahfKVPRYVI--PIDAFPKTTSGKIQK 574
Cdd:PRK05851 470 ---GPDEAGARSEVVQRVASecG-----VVPSDVVfvAPGSLPRTSSGKLRR 513
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
206-577 |
1.03e-17 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 85.99 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 206 DDFLDLASKSEREEVAKMQKSiLPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQVPMFHAFGV 285
Cdd:cd17654 95 NKELDNAPLSFTPEHRHFNIR-TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 286 IISIMAALTKGATMVL-PAAGFSPKDSLQAIVNE--KCSVIHGTPTMYVDLVNTQKKLQVpLGRIKK----AVTGGAIVS 358
Cdd:cd17654 174 VVEIFLSLSSGATLLIvPTSVKVLPSKLADILFKrhRITVLQATPTLFRRFGSQSIKSTV-LSATSSlrvlALGGEPFPS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 359 PQLIKDVRQVLNVEAVHSVYGLTETTA-VIFQSLPGDSSDV-----VLNSVghltdhIEakVVDAEGrcvpFGQPGELCV 432
Cdd:cd17654 253 LVILSSWRGKGNRTRIFNIYGITEVSCwALAYKVPEEDSPVqlgspLLGTV------IE--VRDQNG----SEGTGQVFL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 433 RGyTTMLGYHDDEEKTKETIgndrWLRTGDqFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGV 512
Cdd:cd17654 321 GG-LNRVCILDDEVTVPKGT----MRATGD-FVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581924 513 PDERLgeeVCAYVRLEEgvdpasfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQKFKL 577
Cdd:cd17654 395 DQQRL---IAFIVGESS-------SSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
71-479 |
1.16e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 86.57 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRY-SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNpAYQGPE-IAYCLNKVNVK 148
Cdd:PTZ00216 117 NETRYiTYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVY-ANLGEDaLAYALRETECK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 149 AIIApetfKTQNYYEILRdicpeisdadtgKIRSEKFPHlrsVIIDSNDSLKGALRFDDfLDLASKSEREEVAKMQKSIL 228
Cdd:PTZ00216 196 AIVC----NGKNVPNLLR------------LMKSGGMPN---TTIIYLDSLPASVDTEG-CRLVAWTDVVAKGHSAGSHH 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACN-------IQFTSGTTGNPKAACLTHHNFVNnGIH-VGNR-NEL-----EGERICVQVPMFH--AFGVIiSIMaa 292
Cdd:PTZ00216 256 PLNIPEnnddlalIMYTSGTTGDPKGVMHTHGSLTA-GILaLEDRlNDLigppeEDETYCSYLPLAHimEFGVT-NIF-- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 293 LTKGATMvlpaaGF-SPKDSLQA-------IVNEKCSVIHGTPTMYvDLV--NTQKKLQvPLGRIKKAVTGGAIVSP--- 359
Cdd:PTZ00216 332 LARGALI-----GFgSPRTLTDTfarphgdLTEFRPVFLIGVPRIF-DTIkkAVEAKLP-PVGSLKRRVFDHAYQSRlra 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 360 ------------QLIKDVRQVL--NV---------------EAVHSV-------YGLTETTAVIFQSLPGDssdVVLNSV 403
Cdd:PTZ00216 405 lkegkdtpywneKVFSAPRAVLggRVramlsgggplsaatqEFVNVVfgmviqgWGLTETVCCGGIQRTGD---LEPNAV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 404 GHLTDHIEAKVVDAEG---------RcvpfgqpGELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANGYGRI 474
Cdd:PTZ00216 482 GQLLKGVEMKLLDTEEykhtdtpepR-------GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRI 554
|
....*
gi 24581924 475 VGRLK 479
Cdd:PTZ00216 555 IGRVK 559
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
174-510 |
3.40e-17 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 84.21 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 174 DADTGKIRS----EKFPHLRsviidsndslKGALRfDDFLDLASKSEREEVAKMQKSilpesacniqftSGTTGNPKAAC 249
Cdd:cd05913 41 GIDPDDIKSlddlRKLPFTT----------KEDLR-DNYPFGLFAVPREKVVRIHAS------------SGTTGKPTVVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 250 LTHHNFvnngihvgnRNELEGERICvqvpmFHAFGV----IISIMAA---LTKGAT----------MVLPAAGFSPKDSL 312
Cdd:cd05913 98 YTKNDL---------DVWAELVARC-----LDAAGVtpgdRVQNAYGyglFTGGLGfhygaerlgaLVIPAGGGNTERQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 313 QAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRI--KKAVTGGAIVSPQLIKDVRQVLNVEAvHSVYGLTETTAvifqs 390
Cdd:cd05913 164 QLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELslKVGIFGAEPWTEEMRKRIERRLGIKA-YDIYGLTEIIG----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 391 lPGDSSDVVLNSVGHL-TDHIEAKVVDAE-GRCVPFGQPGELCVrgyTTMlgyhddeekTKETIGNDRWlRTGD--QFVL 466
Cdd:cd05913 238 -PGVAFECEEKDGLHIwEDHFIPEIIDPEtGEPVPPGEVGELVF---TTL---------TKEAMPLIRY-RTRDitRLLP 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24581924 467 EANGYGR-------IVGRLKEMLIRGGENIFPKEIEDFLNAHPQV-IEAHVI 510
Cdd:cd05913 304 GPCPCGRthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLgPHYQLI 355
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
72-577 |
4.96e-17 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 84.01 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 72 GKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAII 151
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 152 apetfktqnyyeilrdicpeisdadtgkirsekFPHLrsviidsndslkgalrfDDFLDLASKSEREEVAKMQKSILpes 231
Cdd:cd05939 81 ---------------------------------FNLL-----------------DPLLTQSSTEPPSQDDVNFRDKL--- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 232 aCNIqFTSGTTGNPKAACLTH--HNFVNNGIHVGNRNELEgERICVQVPMFHAFGVIISIMAALTKGATMVLPAAgFSPK 309
Cdd:cd05939 108 -FYI-YTSGTTGLPKAAVIVHsrYYRIAAGAYYAFGMRPE-DVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKK-FSAS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 310 DSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGaiVSPQLIKDVRQVLNVEAVHSVYGLTETTAVI-- 387
Cdd:cd05939 184 NFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLvn 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 388 ---------FQSLPGDS-SDVVLNSVGHLTDHIEAkvvDAEGRCVPF--GQPGELCVR-----GYTTMLGYHDDEEKTKE 450
Cdd:cd05939 262 idnhvgacgFNSRILPSvYPIRLIKVDEDTGELIR---DSDGLCIPCqpGEPGLLVGKiiqndPLRRFDGYVNEGATNKK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 TIGN-----DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVP----DERLGeeV 521
Cdd:cd05939 339 IARDvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvpgvEGRAG--M 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581924 522 CAYVRLEEGVDPASFTAETLKAyakgklahfkVPRYVIPI-----DAFPKTTSGKIQKFKL 577
Cdd:cd05939 417 AAIVDPERKVDLDRFSAVLAKS----------LPPYARPQfirllPEVDKTGTFKLQKTDL 467
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
410-572 |
5.30e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.42 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 410 IEAKVVDAEGRCVPFGQPGELCV-RGYTTML-GYHDDEEKTKETIgndrWLR------TGDQFVLEANGYGRIVGRLKEM 481
Cdd:PRK00174 433 IQPAVVDEEGNPLEGGEGGNLVIkDPWPGMMrTIYGDHERFVKTY----FSTfkgmyfTGDGARRDEDGYYWITGRVDDV 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 482 LIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAY-AK--GKLAHFKVPRYV 558
Cdd:PRK00174 509 LNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWvRKeiGPIAKPDVIQFA 588
|
170
....*....|....
gi 24581924 559 ipiDAFPKTTSGKI 572
Cdd:PRK00174 589 ---PGLPKTRSGKI 599
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
71-574 |
1.28e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.06 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 71 EGKRYSFKSLLQEADALAAGFRKLGlQPGD-AVGLW--APNYLHWYLGMMgaaRAGLTSVglnPAYqgpeiayclnkvnv 147
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARA-SFGDrAVLLFpsGPDYVAAFFGCL---YAGVIAV---PAY-------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 148 kaiiAPETFKtQNYYEILRDIcpeISDADtgkirsekfPHLRSVIIDSNDSLK--GALRFD--------DFLDLASKSER 217
Cdd:PRK05691 96 ----PPESAR-RHHQERLLSI---IADAE---------PRLLLTVADLRDSLLqmEELAAAnapellcvDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 218 EEVAkmqksILPESACNIQFTSGTTGNPKAACLTHHNFVNN--------GIHVGnrnelEGERICVQVPMFHAFGVIISI 289
Cdd:PRK05691 159 QEPA-----LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANeqlirhgfGIDLN-----PDDVIVSWLPLYHDMGLIGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 290 MAALTKGATMVLPAAGF---SPKDSLQAIvNEKCSVIHGTPTMYVDL----VNTQKKLQVPLGRIKKAVTGGaivspqli 362
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYfleRPLRWLEAI-SEYGGTISGGPDFAYRLcserVSESALERLDLSRWRVAYSGS-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 363 KDVRQ-------------VLNVEAVHSVYGLTETT---------------AVIFQSL------PGDSSdvVLNSVG-HLT 407
Cdd:PRK05691 300 EPIRQdslerfaekfaacGFDPDSFFASYGLAEATlfvsggrrgqgipalELDAEALarnraePGTGS--VLMSCGrSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 408 DHiEAKVVD-AEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKETIGN---DRWLRTGD-QFVLEANGYgrIVGRLKEML 482
Cdd:PRK05691 378 GH-AVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhdgRTWLRTGDlGFLRDGELF--VTGRLKDML 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 483 IRGGENIFPKEIEdflnahpQVIEAHVIGVPDERlgeeVCAY---VRLEEGVDPA---------SFTAETL-----KAYA 545
Cdd:PRK05691 455 IVRGHNLYPQDIE-------KTVEREVEVVRKGR----VAAFavnHQGEEGIGIAaeisrsvqkILPPQALiksirQAVA 523
|
570 580 590
....*....|....*....|....*....|.
gi 24581924 546 KgklAHFKVPRYVIPID--AFPKTTSGKIQK 574
Cdd:PRK05691 524 E---ACQEAPSVVLLLNpgALPKTSSGKLQR 551
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
76-571 |
2.55e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 82.17 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAgfrKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIApet 155
Cdd:PRK06334 47 SYNQVRKAVIALAT---KVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLT--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 fkTQNYYEILRDICPEISDADTGKIRSEKFPHLRSVIIDSNDSLKGALRFDDFLDLASKSEREevakmqksilPESACNI 235
Cdd:PRK06334 121 --SKQLMQHLAQTHGEDAEYPFSLIYMEEVRKELSFWEKCRIGIYMSIPFEWLMRWFGVSDKD----------PEDVAVI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 236 QFTSGTTGNPKAACLTHHNFV-NNGIHVGNRNELEGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPKDSLQA 314
Cdd:PRK06334 189 LFTSGTEKLPKGVPLTHANLLaNQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 315 IVNEKCSVIHGTPTMYVDLVNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIfqSLPGD 394
Cdd:PRK06334 269 IDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVI--TINTV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 395 SSDVVLNSVGHLTDHIEAKVVDAEGRC-VPFGQPGELCVRGYTTMLGY-HDDEEKTKETIGNDRWLRTGDQFVLEANGYG 472
Cdd:PRK06334 347 NSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYlGEDFGQGFVELGGETWYVTGDLGYVDRHGEL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 473 RIVGRLKEMLIRGGENIFPKEIEDFL------NAHPQVIEAHVIGVPDERlgEEVCAYVRLEEGVDPASFTAETLKAYAK 546
Cdd:PRK06334 427 FLKGRLSRFVKIGAEMVSLEALESILmegfgqNAADHAGPLVVCGLPGEK--VRLCLFTTFPTSISEVNDILKNSKTSSI 504
|
490 500
....*....|....*....|....*
gi 24581924 547 GKLAhfkvprYVIPIDAFPKTTSGK 571
Cdd:PRK06334 505 LKIS------YHHQVESIPMLGTGK 523
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
210-572 |
4.82e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 81.62 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 210 DLASKSEREEVAKMQkSILPESACNIQFTSGTTGNPKAACLTHHN---FVNNGIHVGNRNELEGERICvQVPMFHAFGVI 286
Cdd:PRK06060 126 ELMSEAARVAPGGYE-PMGGDALAYATYTSGTTGPPKAAIHRHADpltFVDAMCRKALRLTPEDTGLC-SARMYFAYGLG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 287 ISIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTqkklqvplgrikkavtggaiVSPQLIKDVR 366
Cdd:PRK06060 204 NSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDS--------------------CSPDSFRSLR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 367 QVLNV-EAVHSvyGLTETTAVIFQSLP----GDSSDV----VLNSV--------GHLTDHIEAKVVDAEGRCVPFGQPGE 429
Cdd:PRK06060 264 CVVSAgEALEL--GLAERLMEFFGGIPildgIGSTEVgqtfVSNRVdewrlgtlGRVLPPYEIRVVAPDGTTAGPGVEGD 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 430 LCVRGYTTMLGYHDDEEKTKEtigNDRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHV 509
Cdd:PRK06060 342 LWVRGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAV 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 510 IGVpderlgEEVCAYVRLEEGVDPAS--FTAETLKAYAK----GKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK06060 419 VAV------RESTGASTLQAFLVATSgaTIDGSVMRDLHrgllNRLSAFKVPHRFAVVDRLPRTPNGKL 481
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
86-572 |
6.73e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 80.93 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 86 ALAAGFRKLGlQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGL-NPAYQGpeiayclnkvnvkaiiapetfKTQNYYEI 164
Cdd:PRK07769 67 AVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPG---------------------HVGRLHAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 165 LRDICPeisdadtgkirsekfphlrSVIIDSNDSLKGALRFddFLDLASKsER----------EEVAKMQKSILP--ESA 232
Cdd:PRK07769 125 LDDCTP-------------------SAILTTTDSAEGVRKF--FRARPAK-ERprviavdavpDEVGATWVPPEAneDTI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 233 CNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNEL-EGERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFSPK-- 309
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGqEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRpg 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 310 ---DSLQAIVNEKCSVIHGTPTMYVDL-----VNTQKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQV-----LNVEAVHS 376
Cdd:PRK07769 263 rwiRELARKPGGTGGTFSAAPNFAFEHaaargLPKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAfapygLPPTAIKP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 377 VYGLTETT------------AVI-----------FQSLPGDSSDVVLN-SVGHLTDHIEAKVVDAE-GRCVPFGQPGELC 431
Cdd:PRK07769 343 SYGMAEATlfvsttpmdeepTVIyvdrdelnagrFVEVPADAPNAVAQvSAGKVGVSEWAVIVDPEtASELPDGQIGEIW 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 432 VRGYTTMLGYHDDEEKTKETIGN-----------------DRWLRTGDQFV-LEANGYgrIVGRLKEMLIRGGENIFPKE 493
Cdd:PRK07769 423 LHGNNIGTGYWGKPEETAATFQNilksrlseshaegapddALWVRTGDYGVyFDGELY--ITGRVKDLVIIDGRNHYPQD 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 494 IE-DFLNAHPQVIEAHV--IGVPDERLGEEVCAYVRLEEGVDPASfTAETL-----KAYAKGKL---------------A 550
Cdd:PRK07769 501 LEyTAQEATKALRTGYVaaFSVPANQLPQVVFDDSHAGLKFDPED-TSEQLvivaeRAPGAHKLdpqpiaddiraaiavR 579
|
570 580
....*....|....*....|....
gi 24581924 551 HFKVPRYV--IPIDAFPKTTSGKI 572
Cdd:PRK07769 580 HGVTVRDVllVPAGSIPRTSSGKI 603
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-507 |
1.12e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.45 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 87 LAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIA-----PETFKT-QN 160
Cdd:PLN02614 92 LGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVeekkiSELFKTcPN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 161 YYEILRDICPEISDADTGKIRSEKFphlrSVIIDSndslkgalrFDDFLDLASKSEREEVAKMQKSIlpesaCNIQFTSG 240
Cdd:PLN02614 172 STEYMKTVVSFGGVSREQKEEAETF----GLVIYA---------WDEFLKLGEGKQYDLPIKKKSDI-----CTIMYTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 241 TTGNPKAACLTHHNFVN---NGIH-VGNRNELEGER--ICVQVPMFHAFGVII--------------------------- 287
Cdd:PLN02614 234 TTGDPKGVMISNESIVTliaGVIRlLKSANAALTVKdvYLSYLPLAHIFDRVIeecfiqhgaaigfwrgdvklliedlge 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 288 ---SIMAALTK-------GATMVLPAAGFSPKDSLQAIVNEKCSVI-----HGTPTMYVDLVNTQKKLQVPLGRIKKAVT 352
Cdd:PLN02614 314 lkpTIFCAVPRvldrvysGLQKKLSDGGFLKKFVFDSAFSYKFGNMkkgqsHVEASPLCDKLVFNKVKQGLGGNVRIILS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 353 GGAivspQLIKDVRQVLNVEAVHSV---YGLTETTAVIFQSLPgDSSDVvLNSVGHLTDHIEAK---VVDAEGRCVPFGQ 426
Cdd:PLN02614 394 GAA----PLASHVESFLRVVACCHVlqgYGLTESCAGTFVSLP-DELDM-LGTVGPPVPNVDIRlesVPEMEYDALASTP 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 427 PGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGGENIFPKEIEDfLNAHPQVI 505
Cdd:PLN02614 468 RGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIEN-IYGEVQAV 545
|
..
gi 24581924 506 EA 507
Cdd:PLN02614 546 DS 547
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
76-588 |
7.29e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 77.93 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVglnPAYQ--GP-EIAYCLNKVNVKAIIA 152
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICV---PLYDtlGPgAVDYIVDHAEIDFVFV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 153 PETfKTQnyyeilrdicpEISDADTGKIRSEK----FPHLRSVIIDSNDSLK-GALRFDDFLDLAsKSEREEVAKMQksi 227
Cdd:PLN02430 155 QDK-KIK-----------ELLEPDCKSAKRLKaivsFTSVTEEESDKASQIGvKTYSWIDFLHMG-KENPSETNPPK--- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 228 lPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQ------VPMFHAFGVIISiMAALTKGAtmvl 301
Cdd:PLN02430 219 -PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDKMTHDdvylsfLPLAHILDRMIE-EYFFRKGA---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 302 pAAGF------SPKDSLQAIvneKCSVIHGTPTMYVDLVN-TQKKLQ------------------------------VPL 344
Cdd:PLN02430 293 -SVGYyhgdlnALRDDLMEL---KPTLLAGVPRVFERIHEgIQKALQelnprrrlifnalykyklawmnrgyshkkaSPM 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 345 --------------GRIKKAVTGGAIVSPQlIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSdvVLNSVGHLTDHI 410
Cdd:PLN02430 369 adflafrkvkaklgGRLRLLISGGAPLSTE-IEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMC--MLGTVGAPAVYN 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 411 EAKVVDA-EGRCVPFGQP--GELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLKEML-IRGG 486
Cdd:PLN02430 446 ELRLEEVpEMGYDPLGEPprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQG 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 487 ENIFPKEIEDFLNAHPQVIEAHVIG-----------VPDER--------LG-----EEVCAYVRLEEGVdpasfTAETLK 542
Cdd:PLN02430 525 EYVALEYLENVYGQNPIVEDIWVYGdsfksmlvavvVPNEEntnkwakdNGftgsfEELCSLPELKEHI-----LSELKS 599
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 24581924 543 AYAKGKLAHFKVPRYVI----PIDAFPK--TTSGKIQKFKLVEAFKAKETEL 588
Cdd:PLN02430 600 TAEKNKLRGFEYIKGVIletkPFDVERDlvTATLKKRRNNLLKYYQVEIDEM 651
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
62-573 |
1.32e-14 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 76.93 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 62 DVEAIVSCHEGKR--YSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAAragltSVGlnpayqgpeia 139
Cdd:cd05943 84 DPAAIYAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATA-----SIG----------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 140 yclnkvnvkAI---IAPEtFKTQNYYEILRDICPEISDADTGKIRSEK-FPHLRSV--IIDSNDSLKGALrfddFLDLAS 213
Cdd:cd05943 148 ---------AIwssCSPD-FGVPGVLDRFGQIEPKVLFAVDAYTYNGKrHDVREKVaeLVKGLPSLLAVV----VVPYTV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 214 KSEREEVAKMQKS------ILPESACNIQFT-------------SGTTGNPKaaCLTH--------HnFVNNGIHVGNRn 266
Cdd:cd05943 214 AAGQPDLSKIAKAltledfLATGAAGELEFEplpfdhplyilysSGTTGLPK--CIVHgaggtllqH-LKEHILHCDLR- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 267 elEGERICVQVP----MFHafgviiSIMAALTKGATMVL----PaaGFSPKDSLQAIVNEKCSVIHGTPTMYVDlvNTQK 338
Cdd:cd05943 290 --PGDRLFYYTTcgwmMWN------WLVSGLAVGATIVLydgsP--FYPDTNALWDLADEEGITVFGTSAKYLD--ALEK 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 339 KLQVP-----LGRIKKAVTGGAIVSPQLIKDVRqvlnvEAVHSvygltettavifqslpgdssDVVLNSVGHLTDHIEA- 412
Cdd:cd05943 358 AGLKPaethdLSSLRTILSTGSPLKPESFDYVY-----DHIKP--------------------DVLLASISGGTDIISCf 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 413 -----------------------KVVDAEGRCVPfGQPGEL-CVRGYTTM-LGYHDDEEKTK------ETIGNdRWlRTG 461
Cdd:cd05943 413 vggnpllpvyrgeiqcrglgmavEAFDEEGKPVW-GEKGELvCTKPFPSMpVGFWNDPDGSRyraayfAKYPG-VW-AHG 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 462 DQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETL 541
Cdd:cd05943 490 DWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRI 569
|
570 580 590
....*....|....*....|....*....|..
gi 24581924 542 KAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQ 573
Cdd:cd05943 570 RSTIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
76-465 |
2.82e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 75.85 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQ-----GPEIAYCLNKVNVKAI 150
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSlmshdHAKLKHLFDLVKPRVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 151 IAPETFKTQNYYEILRDICPEIsdadtgkirsekfphlrsVIIDSNDSLKGALRFDDfldLASKSEREEVAKMQKSILPE 230
Cdd:PRK12582 162 FAQSGAPFARALAALDLLDVTV------------------VHVTGPGEGIASIAFAD---LAATPPTAAVAAAIAAITPD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SACNIQFTSGTTGNPKAACLTHHNF-VNNGIHVGNRNELEGERICVQV---PMFHAFGVIISIMAALTKGATMVL----P 302
Cdd:PRK12582 221 TVAKYLFTSGSTGMPKAVINTQRMMcANIAMQEQLRPREPDPPPPVSLdwmPWNHTMGGNANFNGLLWGGGTLYIddgkP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 303 AAG-FSPkdSLQAIVNEKCSVIHGTPTMYVDLVNTQKKLQVpLGR-----IKKAVTGGAIVsPQLIKDVRQVLNVEA--- 373
Cdd:PRK12582 301 LPGmFEE--TIRNLREISPTVYGNVPAGYAMLAEAMEKDDA-LRRsffknLRLMAYGGATL-SDDLYERMQALAVRTtgh 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 374 ---VHSVYGLTETTAVIFQS-------------LPGdssdvvlnsvghltdhIEAKVvdaegrcVPFGQPGELCVRGYTT 437
Cdd:PRK12582 377 ripFYTGYGATETAPTTTGThwdtervgliglpLPG----------------VELKL-------APVGDKYEVRVKGPNV 433
|
410 420 430
....*....|....*....|....*....|
gi 24581924 438 MLGYHDDEEKTKETIGNDRWLRTGD--QFV 465
Cdd:PRK12582 434 TPGYHKDPELTAAAFDEEGFYRLGDaaRFV 463
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
70-462 |
5.50e-14 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 74.78 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 70 HEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYqgpeiayclnkvnvkA 149
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY---------------S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 150 IIAPETFKTQNYYEILRDICPEISDADT--GKIRSEKFPHLRSVIIDSNDSLKGALRFDdflDLASKSEREEVAKMQKSI 227
Cdd:cd05921 86 LMSQDLAKLKHLFELLKPGLVFAQDAAPfaRALAAIFPLGTPLVVSRNAVAGRGAISFA---ELAATPPTAAVDAAFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 228 LPESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEGERICVQV---PMFHAFGVIISIMAALTKGATMVLPAA 304
Cdd:cd05921 163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwlPWNHTFGGNHNFNLVLYNGGTLYIDDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 305 GFSPKDSLQAIVN--EKCSVIHGT-PTMYVDLVNTQKKLQVP----LGRIKKAVTGGAIVsPQLIKDVRQVLNVEAV-HS 376
Cdd:cd05921 243 KPMPGGFEETLRNlrEISPTVYFNvPAGWEMLVAALEKDEALrrrfFKRLKLMFYAGAGL-SQDVWDRLQALAVATVgER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 377 V-----YGLTETTAVIF-----QSLPGdssdvvlnSVGHLTDHIEAKVvdaegrcVPFGQPGELCVRGYTTMLGYHDDEE 446
Cdd:cd05921 322 IpmmagLGATETAPTATfthwpTERSG--------LIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPE 386
|
410
....*....|....*.
gi 24581924 447 KTKETIGNDRWLRTGD 462
Cdd:cd05921 387 LTAQAFDEEGFYCLGD 402
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
76-490 |
9.49e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 74.11 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIAPET 155
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 156 fktqnyyeilrdicpeisdadtgkirseKFPHLRSVIIDSNDSLKGALRFDDFLDLASKSER---------EEVAKM--Q 224
Cdd:PLN02861 159 ----------------------------KISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEelgvscfswEEFSLMgsL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 225 KSILP----ESACNIQFTSGTTGNPKAACLTHHNFVNnGIHVGNRNELEGERICVQ-------VPMFHAFGVIISIMAaL 293
Cdd:PLN02861 211 DCELPpkqkTDICTIMYTSGTTGEPKGVILTNRAIIA-EVLSTDHLLKVTDRVATEedsyfsyLPLAHVYDQVIETYC-I 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 294 TKGATMvlpaaGFSPKDS---LQAIVNEKCSVIHGTPTMY---------------------------VDLVNTQKKL--- 340
Cdd:PLN02861 289 SKGASI-----GFWQGDIrylMEDVQALKPTIFCGVPRVYdriytgimqkissggmlrkklfdfaynYKLGNLRKGLkqe 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 341 -------QVPLGRIKKAVTG-------GAIVSPQLIKDVRQVLNVEAVHSVYGLTETTAVIFQSLPGDSSdvVLNSVGHL 406
Cdd:PLN02861 364 easprldRLVFDKIKEGLGGrvrlllsGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFS--MVGTVGVP 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 407 TDHIEAKVV-------DAEGRcVPfgqPGELCVRGYTTMLGYHDDEEKTKETIgNDRWLRTGDQFVLEANGYGRIVGRLK 479
Cdd:PLN02861 442 MTTIEARLEsvpemgyDALSD-VP---RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKK 516
|
490
....*....|.
gi 24581924 480 emlirggeNIF 490
Cdd:PLN02861 517 --------NIF 519
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
64-579 |
1.23e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.39 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 64 EAIVSCHEGKRYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGltsvglnpayqgpeIAYcln 143
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--------------HAY--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 144 kVNVKAIIAPEtfktqnyyEILRDIcpEISDAdtgkirsekfphlrSVIIDSNDSLKGalrfDDFLDLASKSEREEVAKM 223
Cdd:PRK04813 80 -IPVDVSSPAE--------RIEMII--EVAKP--------------SLIIATEELPLE----ILGIPVITLDELKDIFAT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 224 QKSILPESACN------IQFTSGTTGNPKAACLTHHN---FVNNGIhvgNRNEL-EGERICVQVPmfhaFGVIISIMA-- 291
Cdd:PRK04813 131 GNPYDFDHAVKgddnyyIIFTSGTTGKPKGVQISHDNlvsFTNWML---EDFALpEGPQFLNQAP----YSFDLSVMDly 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 292 -ALTKGATMV-LPAAGFS-PKDSLQAIVNEKCSVIHGTPT--------------MYVDL-----------VNTQKKLqvp 343
Cdd:PRK04813 204 pTLASGGTLVaLPKDMTAnFKQLFETLPQLPINVWVSTPSfadmclldpsfneeHLPNLthflfcgeelpHKTAKKL--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 344 LGRIKKAVtggaivspqlikdvrqvlnveaVHSVYGLTETT-AVI-----------FQSLPgdssdvvlnsVGHLTDHIE 411
Cdd:PRK04813 281 LERFPSAT----------------------IYNTYGPTEATvAVTsieitdemldqYKRLP----------IGYAKPDSP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 412 AKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE---TIGNDRWLRTGDQFVLEaNGYGRIVGRLKEMLIRGGEN 488
Cdd:PRK04813 329 LLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYR 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 489 IFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGvdpaSFTAE-TLKAYAKGKLAHFkVPRYVIP-----ID 562
Cdd:PRK04813 408 IELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEE----DFEREfELTKAIKKELKER-LMEYMIPrkfiyRD 482
|
570
....*....|....*..
gi 24581924 563 AFPKTTSGKIQKFKLVE 579
Cdd:PRK04813 483 SLPLTPNGKIDRKALIE 499
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
229-571 |
4.75e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.05 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEG-ERICVQVPMFHAFGVIISIMAALTKGATMVLPAAGFS 307
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPnDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 308 PKDSLQAIVNEKCSVIHGTPTM---YVDLVNTQKklqvpLGRIKKAVTGGAIVSP---QLIKDVRQVLNVEAvhsvYGLT 381
Cdd:PRK08043 444 YRIVPELVYDRNCTVLFGTSTFlgnYARFANPYD-----FARLRYVVAGAEKLQEstkQLWQDKFGLRILEG----YGVT 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 382 ETTAVIFQSLPGDSSdvvLNSVGHLTDHIEAKVVDAEGrcvpFGQPGELCVRGYTTMLGY-------------HDDEEKT 448
Cdd:PRK08043 515 ECAPVVSINVPMAAK---PGTVGRILPGMDARLLSVPG----IEQGGRLQLKGPNIMNGYlrvekpgvlevptAENARGE 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 449 KETigndRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDF-LNAHPQVIEAHVIgVPDERLGEEVCAYVrl 527
Cdd:PRK08043 588 MER----GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KSDASKGEALVLFT-- 660
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24581924 528 eegVDpASFTAETLKAYAKGK-LAHFKVPRYVIPIDAFPKTTSGK 571
Cdd:PRK08043 661 ---TD-SELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
207-585 |
1.70e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 69.97 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 207 DFLDLASksEREEVAKMQKsiLPESAcNIQFTSGTTGNPKAACLTHHNFVNN------GIHVGNRNELEGERICVQ-VPM 279
Cdd:PRK05850 142 DLLDLDS--PRGSDARPRD--LPSTA-YLQYTSGSTRTPAGVMVSHRNVIANfeqlmsDYFGDTGGVPPPDTTVVSwLPF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 280 FHAFGVIISIMAALTKGATMVL--PAAgF--SPKDSLQAIVNEkCSVIHGTPTMYVDLvnTQKKLQ------VPLGRIKK 349
Cdd:PRK05850 217 YHDMGLVLGVCAPILGGCPAVLtsPVA-FlqRPARWMQLLASN-PHAFSAAPNFAFEL--AVRKTSdddmagLDLGGVLG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 350 AVTGGAIVSPQLIKdvRQV-------LNVEAVHSVYGLTETTAVIFQSLPGDSSDVV------LnSVGH----------- 405
Cdd:PRK05850 293 IISGSERVHPATLK--RFAdrfapfnLRETAIRPSYGLAEATVYVATREPGQPPESVrfdyekL-SAGHakrcetgggtp 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 406 -----LTDHIEAKVVDAEGR--CvPFGQPGELCVRGYTTMLGYHDDEEKTKETIG-----------NDRWLRTGDQ-FVL 466
Cdd:PRK05850 370 lvsygSPRSPTVRIVDPDTCieC-PAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpEGPWLRTGDLgFIS 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 467 EANGYgrIVGRLKEMLIRGGENIFPKEIEdflnAHPQVI---EAHVIGVPDERlGEEVCAYVRLEEGVDPASFTAETLKA 543
Cdd:PRK05850 449 EGELF--IVGRIKDLLIVDGRNHYPDDIE----ATIQEItggRVAAISVPDDG-TEKLVAIIELKKRGDSDEEAMDRLRT 521
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 24581924 544 Y------AKGKLAHFKVPRYV-IPIDAFPKTTSGKIQKFKLVEAFKAKE 585
Cdd:PRK05850 522 VkrevtsAISKSHGLSVADLVlVAPGSIPITTSGKIRRAACVEQYRQDE 570
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
410-574 |
4.38e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 68.77 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 410 IEAKVVDAEGRCvpfgqPGELCVRG-----YTTMLGYHDDEEKT--KETIGndrWLRTGDQFVLEANGYGRIVGRLKEML 482
Cdd:PLN02654 468 VDEKGKEIEGEC-----SGYLCVKKswpgaFRTLYGDHERYETTyfKPFAG---YYFSGDGCSRDKDGYYWLTGRVDDVI 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 483 IRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDPASFTAETLKAYAKGKLAHFKVPRYVIPID 562
Cdd:PLN02654 540 NVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAP 619
|
170
....*....|..
gi 24581924 563 AFPKTTSGKIQK 574
Cdd:PLN02654 620 GLPKTRSGKIMR 631
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
76-504 |
4.44e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.99 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 76 SFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIA-PE 154
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICdSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 155 TFKTqnyyeiLRDIcpeisdadtgkirSEKFPHLRSVII--DSNDSLKGALRFDDFLDLASKSEREEVAKMQKS--ILPE 230
Cdd:PLN02387 188 QLKK------LIDI-------------SSQLETVKRVIYmdDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVdpDLPS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 231 SA--CNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNR-NELEGERICVQ-VPMFHAF-----GVIISIMAAL-------- 293
Cdd:PLN02387 249 PNdiAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAyLPLAHILelaaeSVMAAVGAAIgygspltl 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 294 ----------TKG-ATMV-------LPAAGFSPKDSLQAIVNEK---------------CSVIHGT-------PTMYVDL 333
Cdd:PLN02387 329 tdtsnkikkgTKGdASALkptlmtaVPAILDRVRDGVRKKVDAKgglakklfdiaykrrLAAIEGSwfgawglEKLLWDA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 334 VNTQKKLQVPLGRIKKAVTGGAIVSPqlikDVRQVLNV---EAVHSVYGLTETTAVIFQSLPGDSSdvvLNSVGHLTDHI 410
Cdd:PLN02387 409 LVFKKIRAVLGGRIRFMLSGGAPLSG----DTQRFINIclgAPIGQGYGLTETCAGATFSEWDDTS---VGRVGPPLPCC 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 411 EAKVVD-AEGRCVPFGQP---GELCVRGYTTMLGYHDDEEKTKETIGND----RWLRTGD--QFvlEANGYGRIVGRLKE 480
Cdd:PLN02387 482 YVKLVSwEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmRWFYTGDigQF--HPDGCLEIIDRKKD 559
|
490 500
....*....|....*....|....*
gi 24581924 481 ML-IRGGENIFPKEIEDFLNAHPQV 504
Cdd:PLN02387 560 IVkLQHGEYVSLGKVEAALSVSPYV 584
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
229-470 |
1.18e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 64.35 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEgeRICVQ-----VPMFHAFGVIISIMAaLTKGATMVLPA 303
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFK--KYNPKthlsyLPISHIYERVIAYLS-FMLGGTINIWS 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 304 ---AGFSpKDslqaIVNEKCSVIHGTPT----MYVDLVNTQKKLQVP----------LGR-------------------- 346
Cdd:PTZ00342 380 kdiNYFS-KD----IYNSKGNILAGVPKvfnrIYTNIMTEINNLPPLkrflvkkilsLRKsnnnggfskflegithissk 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 347 IKKAV--------TGGAIVSPQLIKDVRQVLNVEaVHSVYGLTETTAVIFQSlpgDSSDVVLNSVG-HLTDHIEAKVV-- 415
Cdd:PTZ00342 455 IKDKVnpnlevilNGGGKLSPKIAEELSVLLNVN-YYQGYGLTETTGPIFVQ---HADDNNTESIGgPISPNTKYKVRtw 530
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24581924 416 ---DAEGRCvpfgqP-GELCVRGYTTMLGYHDDEEKTKETIGNDRWLRTGDQFVLEANG 470
Cdd:PTZ00342 531 etyKATDTL-----PkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNG 584
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
229-574 |
5.97e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 229 PESACNIQFTSGTTGNPKAACLTHHNFVNNGIHVGNRNELEgERICVQVPMFHAFGviISI---MAALTKGATM-VLP-A 303
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALS-EADVIAQTASQSFD--ISVwqfLAAPLFGARVeIVPnA 3944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 304 AGFSPKDSLQAIVNEKCSVIHGTPTMYVDLVNTQkklQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVHSVYGLTET 383
Cdd:PRK05691 3945 IAHDPQGLLAHVQAQGITVLESVPSLIQGMLAED---RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEC 4021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 384 TA-VIFQSLPGDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVRGYTTMLGYHDDEEKTKE--------TIGn 454
Cdd:PRK05691 4022 SDdVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALafvphpfgAPG- 4100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAhVIGVPDERLGEEVCAYVRLEEGVDPA 534
Cdd:PRK05691 4101 ERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREA-AVAVQEGVNGKHLVGYLVPHQTVLAQ 4179
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24581924 535 SFTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PRK05691 4180 GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
235-574 |
3.39e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 59.76 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 235 IQFTSGTTGNPKAA---------CLTHHNFVnngIHVGNRNELEGERICVQVPMFHAFgviisIMAALTKGATMVLPAAG 305
Cdd:PTZ00237 259 ILYTSGTTGNSKAVvrsngphlvGLKYYWRS---IIEKDIPTVVFSHSSIGWVSFHGF-----LYGSLSLGNTFVMFEGG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 306 F-SPK----DSLQAIVNEKCSVIHGTPTMYVDLVNT-----QKKLQVPLGRIKKAVTGGAIVSPQLIKDVRQVLNVEAVH 375
Cdd:PTZ00237 331 IiKNKhiedDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 376 sVYGLTETTAVIFQSLpgDSSDVVLNSVGHLTDHIEAKVVDAEGRCVPFGQPGELCVR-----GYTTMlgYHDDEEKTKE 450
Cdd:PTZ00237 411 -GYGQTEIGITYLYCY--GHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmppSFATT--FYKNDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 451 TIGN-DRWLRTGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEE 529
Cdd:PTZ00237 486 LFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24581924 530 GVDPASFTAETLKA----YAKGKLAHFKVPRYVIPIDAFPKTTSGKIQK 574
Cdd:PTZ00237 566 DQSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
460-572 |
4.76e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 59.19 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 460 TGDQFVLEANGYGRIVGRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYV------RLEEGVDP 533
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVvpkdsdSLADREAR 556
|
90 100 110
....*....|....*....|....*....|....*....
gi 24581924 534 ASFTAETLKAYAKgKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK10524 557 LALEKEIMALVDS-QLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
392-572 |
1.29e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.83 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 392 PGDSSDVVLN-SVGHLTDHIEAKVVDAEGRC-VPFGQPGELCVRGYTTMLGYHDDEEKTKETIGN--------------- 454
Cdd:PRK12476 392 AADAPNAVAHvSCGQVARSQWAVIVDPDTGAeLPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshadga 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 ---DRWLRTGD-QFVLEANGYgrIVGRLKEMLIRGGENIFPKEIEDFL-NAHPQVIEAHVIG--VPDERlGEEVCAYVRL 527
Cdd:PRK12476 472 addGTWLRTGDlGVYLDGELY--ITGRIADLIVIDGRNHYPQDIEATVaEASPMVRRGYVTAftVPAED-NERLVIVAER 548
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24581924 528 EEG---VDPASfTAETLKAYAKGKLAHFKVPRYVIPIDAFPKTTSGKI 572
Cdd:PRK12476 549 AAGtsrADPAP-AIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKL 595
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
237-462 |
1.92e-08 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 57.08 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 237 FTSGTTGNPKAACLTHHNFVNNGIHV-GNRNELEGERICVQ-VPMFHAFGVIiSIMAALTKGATmvlpaAGFSPKDSLQ- 313
Cdd:cd17632 230 YTSGSTGTPKGAMYTERLVATFWLKVsSIQDIRPPASITLNfMPMSHIAGRI-SLYGTLARGGT-----AYFAAASDMSt 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 314 -------------AIVNEKCSVIH--------GTPTMYVDLVNTQKKLQVPL------GRIKKAVTGGAIVSPQLIKDVR 366
Cdd:cd17632 304 lfddlalvrptelFLVPRVCDMLFqryqaeldRRSVAGADAETLAERVKAELrervlgGRLLAAVCGSAPLSAEMKAFME 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 367 QVLNVEaVHSVYGLTETTAVIFqslpgdsSDVVLNSvgHLTDHieaKVVDaegrcVP-FG-----QP---GELCVRGYTT 437
Cdd:cd17632 384 SLLDLD-LHDGYGSTEAGAVIL-------DGVIVRP--PVLDY---KLVD-----VPeLGyfrtdRPhprGELLVKTDTL 445
|
250 260
....*....|....*....|....*
gi 24581924 438 MLGYHDDEEKTKETIGNDRWLRTGD 462
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGD 470
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
53-253 |
1.18e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 54.70 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 53 LELSASNFGDVEAIVSCHEGK------RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAGLTS 126
Cdd:PLN03052 181 LTPKPSKTDDSIAIIWRDEGSddlpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 127 VGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQNYyeILRDicpeisdadtGKirseKFPhLRSVIIDSN---------- 196
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAIF------TQDV--IVRG----------GK----SIP-LYSRVVEAKapkaivlpad 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581924 197 -DSLKGALR-----FDDFLDLASKSER-EEVAKMQKSIlpESACNIQFTSGTTGNPKAACLTHH 253
Cdd:PLN03052 318 gKSVRVKLRegdmsWDDFLARANGLRRpDEYKAVEQPV--EAFTNILFSSGTTGEPKAIPWTQL 379
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
61-573 |
1.91e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.40 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 61 GDVEAIVSCHEGK---RYSFKSLLQEADALAAGFRKLGLQPGDAVGLWAPNYLHWYLGMMGAARAG--LTSVglnpayqG 135
Cdd:PRK03584 98 DDRPAIIFRGEDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiWSSC-------S 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 136 PEIAyclnkvnVKAI------IAPETFKTQNYY-----EIlrDICPEISDadtgkIRsEKFPHLRSVII-------DSND 197
Cdd:PRK03584 171 PDFG-------VQGVldrfgqIEPKVLIAVDGYryggkAF--DRRAKVAE-----LR-AALPSLEHVVVvpylgpaAAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 198 SLKGALRFDDFLDLASKSEREEVAkmqksiLP-ESACNIQFTSGTTGNPKaaCLTH--------HnFVNNGIHVGNRnel 268
Cdd:PRK03584 236 ALPGALLWEDFLAPAEAAELEFEP------VPfDHPLWILYSSGTTGLPK--CIVHghggilleH-LKELGLHCDLG--- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 269 EGERIC-----------VQVpmfhafgviisimAALTKGATMVL----PAAGfSPKDSLQAIVNEKCSVIhGTPTMYVDL 333
Cdd:PRK03584 304 PGDRFFwyttcgwmmwnWLV-------------SGLLVGATLVLydgsPFYP-DPNVLWDLAAEEGVTVF-GTSAKYLDA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 334 VntQKKLQVP-----LGRIkKAV--TGgaivSPqlikdvrqvLNVEAVHSVYgltetTAVifqslpgdSSDVVLNSVGHL 406
Cdd:PRK03584 369 C--EKAGLVPgethdLSAL-RTIgsTG----SP---------LPPEGFDWVY-----EHV--------KADVWLASISGG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 407 TDHIEA------------------------KVVDAEGRCVpFGQPGEL-CVRGYTTM-LGYHDDEEKTK------ETIGN 454
Cdd:PRK03584 420 TDICSCfvggnpllpvyrgeiqcrglgmavEAWDEDGRPV-VGEVGELvCTKPFPSMpLGFWNDPDGSRyrdayfDTFPG 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 455 dRWlRTGDQFVLEANGyGRIV-GRLKEMLIRGGENIFPKEIEDFLNAHPQVIEAHVIGVPDERLGEEVCAYVRLEEGVDp 533
Cdd:PRK03584 499 -VW-RHGDWIEITEHG-GVVIyGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVT- 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 24581924 534 asFTaETLKAYAKGKLA------HfkVPRYVIPIDAFPKTTSGKIQ 573
Cdd:PRK03584 575 --LD-DALRARIRTTIRtnlsprH--VPDKIIAVPDIPRTLSGKKV 615
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
117-572 |
3.52e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 43.27 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 117 MGAARAGLTSVGLNPAYQGPEIAYCLNKVNVKAIIapetfkTQNYyeILR--DICPEISDAdtgkirSEKFPHLRSVIID 194
Cdd:PLN03051 12 LAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVF------TQDV--VLRggRALPLYSKV------VEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 195 SNDSLKGALRFD-----DFLDLASKSEREEVAKMQKSILP-ESACNIQFTSGTTGNPKAACLTH----HNFVNNGIHVGN 264
Cdd:PLN03051 78 AGEPVAVPLREQdlswcDFLGVAAAQGSVGGNEYSPVYAPvESVTNILFSSGTTGEPKAIPWTHlsplRCASDGWAHMDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 265 RnelEGERICVQVPMFHAFGVIIsIMAALTKGATMVLPAAGFSPKDSLQAIVNEKCSVIHGTPTMyvdlVNTQKKLQ--- 341
Cdd:PLN03051 158 Q---PGDVVCWPTNLGWMMGPWL-LYSAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGLVPSI----VKAWRHTGafa 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 342 ---VPLGRIKKAVTGGAIVSPQlikDVRQVLNVEA----VHSVYGLTETTAVIFQSLPGDSSDVVLNSVGHLTDHIeaKV 414
Cdd:PLN03051 230 megLDWSKLRVFASTGEASAVD---DVLWLSSVRGyykpVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRF--VL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 415 VDAEGRCVPFGQP--GELCVRgyTTMLGYHD-----DEEKT------KETIGNDRWLRTGDQFVLEANGYGRIVGRLKEM 481
Cdd:PLN03051 305 LNDNGVPYPDDQPcvGEVALA--PPMLGASDrllnaDHDKVyykgmpMYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581924 482 LIRGGENIFPKEIEDFLNAHPQ-VIEAHVIGVPDERLGEE----VCAYVRLEEGVDPASFTAETLK---AYAKGKLAHFK 553
Cdd:PLN03051 383 MNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGPEllviFLVLGEEKKGFDQARPEALQKKfqeAIQTNLNPLFK 462
|
490
....*....|....*....
gi 24581924 554 VPRYVIpIDAFPKTTSGKI 572
Cdd:PLN03051 463 VSRVKI-VPELPRNASNKL 480
|
|
| |
