|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
745-1498 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 686.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 745 DLDDPSSVRRAEPFHGSFPKLGPPTAISGKVHQKFAASVNSAHMILAGYE--HNINEVVQDLLNCLDNPELPFLQWQELM 822
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDnqVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 823 SVLATRLPKDLRNEFGciQLdgkYKEYELNpdfckSKDFPARLLRGVIEANLAYCSEK-DRVTNERLVEPLMSLVKSYEG 901
Cdd:pfam08326 81 SALSGRIPAKLEASLR--QL---VERAHSR-----SAEFPAKQLRKILDKFLAELVLKaDRDLFEATLAPLVDLVERYRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 902 GRESHARVVVKSLFEEYLSVEELFNDNL--QSDVIERLRLQHAKDLEKVVYIVFSHQGVRSKNKLILRLMEALVYPNPSA 979
Cdd:pfam08326 151 GLKGHEYSVFASLLEEYYDVEKLFSGGNvrEEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 980 ------YRDQLIRFSALNHTSYSELALKASQLLEHTKLSELRTSIARSLSEL-EMFTEEGERLSTPRRKMAINERMEDLV 1052
Cdd:pfam08326 231 snvakeLRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILkSSVVESGYGESGWKHREPSLEVLKELI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1053 CAPLAAEDALVALFDHSDPTLQRRVVETYIRRLYQPYLVsGSIRMQWHRAG-LIALWEFSeehLKQRSGQDVPLQQVENP 1131
Cdd:pfam08326 311 DSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSL-KSIQYHEGEDSpPIVSWQFQ---LPSSHSSEFGSPLSPSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1132 IEKS------------------------WGVMVVIKSLQFVATAIDVALKETSQYGIGVRSVSNSNHvhsnQSNMLHIAL 1187
Cdd:pfam08326 387 DSSPpfkriasvsdlsylvnksedeplrTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSSDE----PINVLNVAI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1188 VGINNQMstlqdsgDEDQTQERVNKLFKILKDNtitshLNGASVKVVSCIIQRDEGRPPMRHSFQWsvdKLYYEEDPMLR 1267
Cdd:pfam08326 463 RDAEGSD-------SDEELLERLEEILKENKEE-----LLAAGVRRITFIIGRKDGQYPKYFTFRG---PDNYEEDPIIR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1268 HVEPPLSTFLELEKVNlegYNEVKYTPSRDRQWHIYTLIKNKKDqrlNDQRMFLRTIVRQPSATNSFltgnidnevghtq 1347
Cdd:pfam08326 528 HIEPALAFQLELGRLS---NFDIKPVPTENRQIHLYEAVGKENP---TDKRFFVRAIIRPGRLRDDI------------- 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1348 ASSSFTSNSILRSLMGALEEIELhAHSETVRSGHSHMYLCLLREQQLhelipfsrmtgkiDKDEgtvctlLKHMVLNLYE 1427
Cdd:pfam08326 589 PTAEYLISEAERLLNDILDALEV-ASIGNSNSDLNHIFLNFVPVFNV-------------DPED------VEEAVGGFLE 648
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670402573 1428 HVGVRMHRLSVCQWEVKLWLVC--DGQASgAWRVVVTNVTGHTCTIDIYREVEDPtTHQLLYHSATTSaGPLH 1498
Cdd:pfam08326 649 RFGKRLWRLRVTQAEIRIIIRDpeTGPPI-PLRLVITNVSGYVVKVELYREVKDD-KGEWVFKSIGKP-GPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1602-2154 |
2.27e-164 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 515.27 E-value: 2.27e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1602 PEFPRGREIIVVANDVTFKAGSFGPREDAFFDAVTNLACERkLPLIYLAATAGARLGVAEEIKSCFHVGWSDYESPERGF 1681
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1682 QYIYlttqdysrlsssviAHELQLKNGETRWVVDTIVGKEDGLGCENLHGSGAIASAYSKAYKETFTLTFVTGRAVGIGA 1761
Cdd:pfam01039 80 KILR--------------AMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1762 YLARLGMRCIQRLD-QPIILTGFSALNKLLGrEVYSSHMQLGGPKIMATNGVVHQTVSDDLEGVSAILKWLSYVPPYVGG 1840
Cdd:pfam01039 146 YLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1841 ---PLPIMKPLDPPERP---VTYLPEN---ACDAlaaicgiqdgegRWL-GGMFDRESFVETLEGWAKTVITGRAKLGGI 1910
Cdd:pfam01039 225 nrePVPIVPTKDPPDRDaplVSIVPDDpkkPYDV------------REViAGIVDEGEFFEIKPGYAKTVVTGFARLGGI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1911 PVGVIAVETQtvmqvipadpgqldsaervvPQAGqVWFPDSATKTAQALLDFNREELPLFILANWRGFSGGQRDLFEGIL 1990
Cdd:pfam01039 293 PVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGIL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1991 QAGSTIVENLRTYKQPAFVYIPmgGELRGGAWVVVDSKINPDHIeMYAERTAKGNVLEPEGLVEIKFRPKELEDCMLRLD 2070
Cdd:pfam01039 352 KHGAKLLYALAEATVPKITVIP--RKAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRGKD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 2071 PEliglntrlkEMKKQNasISEMEtirrsmtirmKQLMPIYTQVATRFAELHDTSARMAAKGVIGKVVDWKESRaFFYRR 2150
Cdd:pfam01039 429 LA---------ATRKQK--IAEYE----------EELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWR 486
|
....
gi 670402573 2151 LRRR 2154
Cdd:pfam01039 487 KHGN 490
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
38-553 |
1.35e-120 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 390.15 E-value: 1.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 38 PIHSVLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDLkiNAEHIRIADQFIEVPGGTNNNNYANVQLIVEI 117
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRT---------VAVYSDADR--DALHVRLADEAVCIGPAPAAESYLNIDAIIAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 118 AERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSgshvkvppeschsip 197
Cdd:COG4770 70 AKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 198 eelyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHL 273
Cdd:COG4770 135 -----DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 274 EVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLE 353
Cdd:COG4770 210 EVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGNFYFLE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 354 LNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPlynipeirrfygmdhgggyhnwrtisavatkfdLDKAQS-VRPKGHCV 432
Cdd:COG4770 289 MNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP---------------------------------LPFTQEdIKLRGHAI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 433 AVRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGe 512
Cdd:COG4770 336 ECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 670402573 513 IRTNVDYTVDLLNATEYRENKIHTGWLDSRIAMRVRAERPP 553
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
42-539 |
1.36e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 314.66 E-value: 1.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 42 VLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDlkINAEHIRIADQFIEVPGGTNNNNYANVQLIVEIAERT 121
Cdd:PRK06111 5 VLIANRGEIAVRIIRTCQKLGIRT---------VAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 122 RVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsgshvkvppeschSIPEELy 201
Cdd:PRK06111 74 GAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVP--------------GITTNL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 rnacvSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHLEVQL 277
Cdd:PRK06111 139 -----EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIEDPRHIEIQL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 278 LCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLELNPR 357
Cdd:PRK06111 214 LADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 358 LQVEHPVTEWIAEINLPAAQVAVGMGIPL-YNIPEIRRfygmdhgggyhnwrtisavatkfdldkaqsvrpKGHCVAVRV 436
Cdd:PRK06111 293 LQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR---------------------------------SGHAIEVRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 437 TSEDPDDgFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIRTN 516
Cdd:PRK06111 340 YAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTN 417
|
490 500
....*....|....*....|...
gi 670402573 517 VDYTVDLLNATEYRENKIHTGWL 539
Cdd:PRK06111 418 IPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
41-541 |
3.36e-82 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 296.74 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 41 SVLVANNGMAAVKFMRSiriwaletfGTEKAILLVAMATPEDLKinAEHIRIAD---QFIEVPGGTNNNNYANVQLIVEI 117
Cdd:TIGR01235 1 KILVANRGEIAIRVFRA---------ANELGIRTVAIYSEEDKL--SLHRQKADesyQVGEGPDLGPIEAYLSIDEIIRV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 118 AERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGShvkvPPEschsip 197
Cdd:TIGR01235 70 AKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDG----PPE------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 198 eelyrnacvsTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGS----PIFIMKVASQSRHL 273
Cdd:TIGR01235 140 ----------TMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYVEKLIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 274 EVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLE 353
Cdd:TIGR01235 210 EVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD-NDGKFYFIE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 354 LNPRLQVEHPVTEWIAEINLPAAQ--VAVGMGIPlynipeirrfygmdhgggyhnwrtisavATKFDLDKAQSVRPKGHC 431
Cdd:TIGR01235 289 VNPRIQVEHTVTEEITGIDIVQAQihIADGASLP----------------------------TPQLGVPNQEDIRTNGYA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 432 VAVRVTSEDPDDGFKPTSGRVEElnFKSKPNvwayFSVK-------SGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGL 504
Cdd:TIGR01235 341 IQCRVTTEDPANNFQPDTGRIEA--YRSAGG----FGIRldggnsyAGAIITPYYDSLLVKVSAWASTPEEAAAKMDRAL 414
|
490 500 510
....*....|....*....|....*....|....*..
gi 670402573 505 KEIQIRGeIRTNVDYTVDLLNATEYRENKIHTGWLDS 541
Cdd:TIGR01235 415 REFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFIDT 450
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
163-386 |
3.71e-53 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 185.97 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 163 DKIGSSLIAQAAGVPTLPWSgshvkvppeschsipeelyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHND 242
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGT--------------------AGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 243 DEVRALFKQVQGEVPGSP----IFIMKVASQSRHLEVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKE 318
Cdd:pfam02786 61 EELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQM 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670402573 319 LEQAARQLAKCVQYVGAATVEYLYSMETGEYYFLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPL 386
Cdd:pfam02786 141 LREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1607-1957 |
7.05e-18 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 89.70 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1607 GREIIVVANDVTFKAGSFGPREDAFFDAVTNLACERKLPLIYLAATAGARLGVAEEIKScfHVGwsdyespeRGFQYIYL 1686
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFA--GYG--------RIFYRNAR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1687 ttqdysrlSSSVIAhelQLkngetrwvvdTIVgkedglgcenlHGSGAIASAYSKAyketftLT------------FVTG 1754
Cdd:COG4799 151 --------SSGGIP---QI----------SVI-----------MGPCAAGGAYSPA------LSdfvimvkgtsqmFLGG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1755 ----RAVGigaylarlgmrciqrldqpiiltgfsalnkllGREVysSHMQLGGPKI-MATNGVVHQTVSDDLEGVSAILK 1829
Cdd:COG4799 193 ppvvKAAT--------------------------------GEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1830 WLSYVPPYVGGPLPIMKPlDPPERPVTYL----PEN---ACDALAAICGIqdgegrwlggmFDRESFVETLEGWAKTVIT 1902
Cdd:COG4799 239 LLSYLPSNNLEDPPRAEP-APPARDPEELygivPEDprkPYDMREVIARL-----------VDGGSFFEFKPLYGPNIVT 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 670402573 1903 GRAKLGGIPVGVIAvetqtvmqvipADPGQLdsaervvpqAGqVWFPDSATKTAQ 1957
Cdd:COG4799 307 GFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAAR 340
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
680-744 |
2.51e-13 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 66.67 E-value: 2.51e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670402573 680 LLADTPCKLLRFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIHFVM-PEGQAMKANDLIARL 744
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
690-744 |
4.16e-10 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 57.61 E-value: 4.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 670402573 690 RFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIHFVM-PEGQAMKANDLIARL 744
Cdd:pfam00364 18 EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILvPEGDTVEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
745-1498 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 686.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 745 DLDDPSSVRRAEPFHGSFPKLGPPTAISGKVHQKFAASVNSAHMILAGYE--HNINEVVQDLLNCLDNPELPFLQWQELM 822
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDnqVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 823 SVLATRLPKDLRNEFGciQLdgkYKEYELNpdfckSKDFPARLLRGVIEANLAYCSEK-DRVTNERLVEPLMSLVKSYEG 901
Cdd:pfam08326 81 SALSGRIPAKLEASLR--QL---VERAHSR-----SAEFPAKQLRKILDKFLAELVLKaDRDLFEATLAPLVDLVERYRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 902 GRESHARVVVKSLFEEYLSVEELFNDNL--QSDVIERLRLQHAKDLEKVVYIVFSHQGVRSKNKLILRLMEALVYPNPSA 979
Cdd:pfam08326 151 GLKGHEYSVFASLLEEYYDVEKLFSGGNvrEEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 980 ------YRDQLIRFSALNHTSYSELALKASQLLEHTKLSELRTSIARSLSEL-EMFTEEGERLSTPRRKMAINERMEDLV 1052
Cdd:pfam08326 231 snvakeLRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILkSSVVESGYGESGWKHREPSLEVLKELI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1053 CAPLAAEDALVALFDHSDPTLQRRVVETYIRRLYQPYLVsGSIRMQWHRAG-LIALWEFSeehLKQRSGQDVPLQQVENP 1131
Cdd:pfam08326 311 DSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSL-KSIQYHEGEDSpPIVSWQFQ---LPSSHSSEFGSPLSPSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1132 IEKS------------------------WGVMVVIKSLQFVATAIDVALKETSQYGIGVRSVSNSNHvhsnQSNMLHIAL 1187
Cdd:pfam08326 387 DSSPpfkriasvsdlsylvnksedeplrTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSSDE----PINVLNVAI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1188 VGINNQMstlqdsgDEDQTQERVNKLFKILKDNtitshLNGASVKVVSCIIQRDEGRPPMRHSFQWsvdKLYYEEDPMLR 1267
Cdd:pfam08326 463 RDAEGSD-------SDEELLERLEEILKENKEE-----LLAAGVRRITFIIGRKDGQYPKYFTFRG---PDNYEEDPIIR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1268 HVEPPLSTFLELEKVNlegYNEVKYTPSRDRQWHIYTLIKNKKDqrlNDQRMFLRTIVRQPSATNSFltgnidnevghtq 1347
Cdd:pfam08326 528 HIEPALAFQLELGRLS---NFDIKPVPTENRQIHLYEAVGKENP---TDKRFFVRAIIRPGRLRDDI------------- 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1348 ASSSFTSNSILRSLMGALEEIELhAHSETVRSGHSHMYLCLLREQQLhelipfsrmtgkiDKDEgtvctlLKHMVLNLYE 1427
Cdd:pfam08326 589 PTAEYLISEAERLLNDILDALEV-ASIGNSNSDLNHIFLNFVPVFNV-------------DPED------VEEAVGGFLE 648
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670402573 1428 HVGVRMHRLSVCQWEVKLWLVC--DGQASgAWRVVVTNVTGHTCTIDIYREVEDPtTHQLLYHSATTSaGPLH 1498
Cdd:pfam08326 649 RFGKRLWRLRVTQAEIRIIIRDpeTGPPI-PLRLVITNVSGYVVKVELYREVKDD-KGEWVFKSIGKP-GPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1602-2154 |
2.27e-164 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 515.27 E-value: 2.27e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1602 PEFPRGREIIVVANDVTFKAGSFGPREDAFFDAVTNLACERkLPLIYLAATAGARLGVAEEIKSCFHVGWSDYESPERGF 1681
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1682 QYIYlttqdysrlsssviAHELQLKNGETRWVVDTIVGKEDGLGCENLHGSGAIASAYSKAYKETFTLTFVTGRAVGIGA 1761
Cdd:pfam01039 80 KILR--------------AMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1762 YLARLGMRCIQRLD-QPIILTGFSALNKLLGrEVYSSHMQLGGPKIMATNGVVHQTVSDDLEGVSAILKWLSYVPPYVGG 1840
Cdd:pfam01039 146 YLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1841 ---PLPIMKPLDPPERP---VTYLPEN---ACDAlaaicgiqdgegRWL-GGMFDRESFVETLEGWAKTVITGRAKLGGI 1910
Cdd:pfam01039 225 nrePVPIVPTKDPPDRDaplVSIVPDDpkkPYDV------------REViAGIVDEGEFFEIKPGYAKTVVTGFARLGGI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1911 PVGVIAVETQtvmqvipadpgqldsaervvPQAGqVWFPDSATKTAQALLDFNREELPLFILANWRGFSGGQRDLFEGIL 1990
Cdd:pfam01039 293 PVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGIL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1991 QAGSTIVENLRTYKQPAFVYIPmgGELRGGAWVVVDSKINPDHIeMYAERTAKGNVLEPEGLVEIKFRPKELEDCMLRLD 2070
Cdd:pfam01039 352 KHGAKLLYALAEATVPKITVIP--RKAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRGKD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 2071 PEliglntrlkEMKKQNasISEMEtirrsmtirmKQLMPIYTQVATRFAELHDTSARMAAKGVIGKVVDWKESRaFFYRR 2150
Cdd:pfam01039 429 LA---------ATRKQK--IAEYE----------EELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWR 486
|
....
gi 670402573 2151 LRRR 2154
Cdd:pfam01039 487 KHGN 490
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
38-553 |
1.35e-120 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 390.15 E-value: 1.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 38 PIHSVLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDLkiNAEHIRIADQFIEVPGGTNNNNYANVQLIVEI 117
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRT---------VAVYSDADR--DALHVRLADEAVCIGPAPAAESYLNIDAIIAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 118 AERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSgshvkvppeschsip 197
Cdd:COG4770 70 AKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 198 eelyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHL 273
Cdd:COG4770 135 -----DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 274 EVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLE 353
Cdd:COG4770 210 EVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGNFYFLE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 354 LNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPlynipeirrfygmdhgggyhnwrtisavatkfdLDKAQS-VRPKGHCV 432
Cdd:COG4770 289 MNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP---------------------------------LPFTQEdIKLRGHAI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 433 AVRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGe 512
Cdd:COG4770 336 ECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 670402573 513 IRTNVDYTVDLLNATEYRENKIHTGWLDSRIAMRVRAERPP 553
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
42-539 |
1.36e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 314.66 E-value: 1.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 42 VLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDlkINAEHIRIADQFIEVPGGTNNNNYANVQLIVEIAERT 121
Cdd:PRK06111 5 VLIANRGEIAVRIIRTCQKLGIRT---------VAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 122 RVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsgshvkvppeschSIPEELy 201
Cdd:PRK06111 74 GAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVP--------------GITTNL- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 rnacvSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHLEVQL 277
Cdd:PRK06111 139 -----EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIEDPRHIEIQL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 278 LCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLELNPR 357
Cdd:PRK06111 214 LADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 358 LQVEHPVTEWIAEINLPAAQVAVGMGIPL-YNIPEIRRfygmdhgggyhnwrtisavatkfdldkaqsvrpKGHCVAVRV 436
Cdd:PRK06111 293 LQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR---------------------------------SGHAIEVRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 437 TSEDPDDgFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIRTN 516
Cdd:PRK06111 340 YAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTN 417
|
490 500
....*....|....*....|...
gi 670402573 517 VDYTVDLLNATEYRENKIHTGWL 539
Cdd:PRK06111 418 IPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
42-551 |
6.93e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 311.53 E-value: 6.93e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 42 VLVANNGMAAVKFMRSIRiwaletfgtEKAILLVAMATPEDlkINAEHIRIADQFIEVPGGTNNNNYANVQLIVEIAERT 121
Cdd:PRK08654 5 ILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 122 RVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGShvkvppeschsipeely 201
Cdd:PRK08654 74 GADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEE----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 rnaCVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDE-VRAL--FKQVQGEVPGSP-IFIMKVASQSRHLEVQL 277
Cdd:PRK08654 137 ---GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEElEDAIesTQSIAQSAFGDStVFIEKYLEKPRHIEIQI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 278 LCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmeTGEYYFLELNPR 357
Cdd:PRK08654 214 LADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 358 LQVEHPVTEWIAEINLPAAQVAVGMGIPLYNipeirrfygmdhgggyhnwrtisavatkfdldKAQSVRPKGHCVAVRVT 437
Cdd:PRK08654 292 LQVEHPITEMVTGIDIVKEQIKIAAGEELSF--------------------------------KQEDITIRGHAIECRIN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 438 SEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIRTNV 517
Cdd:PRK08654 340 AEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG-VKTNI 418
|
490 500 510
....*....|....*....|....*....|....
gi 670402573 518 DYTVDLLNATEYRENKIHTGWLDSRIAMRVRAER 551
Cdd:PRK08654 419 PFHKAVMENENFVRGNLHTHFIEEETTILEEMKR 452
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
39-549 |
5.10e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 307.11 E-value: 5.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 39 IHSVLVANNGMAAVKFMRSIRiwaletfgtEKAILLVAMATPEDLkiNAEHIRIADQFIEVPGGTNNNNYANVQLIVEIA 118
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTADR--DALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 119 ERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsGShvkvppeschsipe 198
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 199 elyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHLE 274
Cdd:PRK08591 135 ----DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYLENPRHIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 275 VQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLEL 354
Cdd:PRK08591 211 IQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 355 NPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLynipeirRFygmdhgggyhnwrtisavatkfdldKAQSVRPKGHCVAV 434
Cdd:PRK08591 290 NTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL-------SI-------------------------KQEDIVFRGHAIEC 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 435 RVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIR 514
Cdd:PRK08591 338 RINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IK 416
|
490 500 510
....*....|....*....|....*....|....*
gi 670402573 515 TNVDYTVDLLNATEYRENKIHTGWLDSRIAMRVRA 549
Cdd:PRK08591 417 TTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
38-542 |
5.28e-92 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 326.71 E-value: 5.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 38 PIHSVLVANNGMAAVKFMRSIriwaletfgTEKAILLVAMATPEDLkiNAEHIRIADQFIEVpgGTNNNN---YANVQLI 114
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDK--LSLHRFKADEAYLI--GEGKHPvraYLDIDEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 115 VEIAERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsGShvKVPPESch 194
Cdd:PRK12999 71 IRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIP--GS--EGPIDD-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 195 sipeelyrnacvstTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQS 270
Cdd:PRK12999 145 --------------IEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGNDeVYLEKYVENP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 271 RHLEVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSMEtGEYY 350
Cdd:PRK12999 211 RHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDAD-GNFY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 351 FLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLYnipeirrfygmDHGGGyhnwrtisavatkfdLDKAQSVRPKGH 430
Cdd:PRK12999 290 FIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLH-----------DLEIG---------------IPSQEDIRLRGY 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 431 CVAVRVTSEDPDDGFKPTSGRVEelnfkskpnvwAY-----FSVK-------SGGAIHEFSDSQFGHVFAFGESRSLAIA 498
Cdd:PRK12999 344 AIQCRITTEDPANNFMPDTGRIT-----------AYrspggFGVRldggnafAGAEITPYYDSLLVKLTAWGRTFEQAVA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 670402573 499 NMVLGLKEIQIRGeIRTNVDYTVDLLNATEYRENKIHTGWLDSR 542
Cdd:PRK12999 413 RMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFIDET 455
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
37-563 |
5.57e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 298.98 E-value: 5.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 37 SPIHSVLVANNGMAAVKFMRSIRiwaletfgtekAILLVAMATPEDLKINAEHIRIADQFIEVPGGTNNNNYANVQLIVE 116
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAAR-----------ELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 117 IAERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSgshvkvppeschsi 196
Cdd:PRK12833 72 AARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 197 peelyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRH 272
Cdd:PRK12833 138 ------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFIARARH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 273 LEVQLLCDKHgNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSMETGEYYFL 352
Cdd:PRK12833 212 IEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 353 ELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLynipeirRFygmdhgggyhnwrtisavatkfdldKAQSVRPKGHCV 432
Cdd:PRK12833 291 EMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL-------RF-------------------------AQGDIALRGAAL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 433 AVRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGe 512
Cdd:PRK12833 339 ECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAARALRELRIDG- 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 670402573 513 IRTNVDYTVDLLNATEYRENKIHTGWLDSRIAMRvRAERPPWYLSVVGGAL 563
Cdd:PRK12833 418 MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEW-RAALDAAASAAVGEAA 467
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
38-542 |
5.75e-89 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 317.41 E-value: 5.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 38 PIHSVLVANNGMAAVKFMRSiriwaletfGTEKAILLVAMATPEDlkINAEHIRIADQFIEVpgGTNNN---NYANVQLI 114
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRA---------ATELGIRTVAIYSEED--RYSLHRFKADEAYLI--GEGKGpvdAYLDIEEI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 115 VEIAERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGshvkvPPesch 194
Cdd:COG1038 70 IRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTE-----GP---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 195 sipeelyrnacVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQS 270
Cdd:COG1038 141 -----------VDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafGDDeVFLEKYIERP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 271 RHLEVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGP-ITIaAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEY 349
Cdd:COG1038 210 KHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPaPNL-DEELREAICEAAVKLAKAVGYVNAGTVEFLVD-DDGNF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 350 YFLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLyNIPEIrrfygmdhgggyhnwrtisavatkfDLDKAQSVRPKG 429
Cdd:COG1038 288 YFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL-DDPEI-------------------------GIPSQEDIRLNG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 430 HCVAVRVTSEDPDDGFKPTSGRVEelnfkskpnvwAY-----FSVK-------SGGAIHEFSDSQFGHVFAFGESRSLAI 497
Cdd:COG1038 342 YAIQCRITTEDPANNFMPDTGRIT-----------AYrsaggFGIRldggnayTGAVITPYYDSLLVKVTAWGRTFEEAI 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 670402573 498 ANMVLGLKEIQIRGeIRTNVDYTVDLLNATEYRENKIHTGWLDSR 542
Cdd:COG1038 411 RKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFIDET 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
42-543 |
1.19e-86 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 291.62 E-value: 1.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 42 VLVANNGMAAVKFMRSIRiwaletfgtEKAILLVAMATPEDLkiNAEHIRIADQFIEVPGGTNNNNYANVQLIVEIAERT 121
Cdd:PRK05586 5 ILIANRGEIAVRIIRACR---------EMGIETVAVYSEADK--DALHVQLADEAVCIGPASSKDSYLNIQNIISATVLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 122 RVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSgshvkvppeschsipeely 201
Cdd:PRK05586 74 GAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 rNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGS----PIFIMKVASQSRHLEVQL 277
Cdd:PRK05586 135 -EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 278 LCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLELNPR 357
Cdd:PRK05586 214 LGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 358 LQVEHPVTEWIAEINLPAAQVAVGmgiplynipeirrfYGMdhgggyhnwrtisavatkfDLDKAQS-VRPKGHCVAVRV 436
Cdd:PRK05586 293 IQVEHPITEMITGVDLVKEQIKIA--------------YGE-------------------KLSIKQEdIKINGHSIECRI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 437 TSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIRTN 516
Cdd:PRK05586 340 NAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTN 418
|
490 500
....*....|....*....|....*..
gi 670402573 517 VDYTVDLLNATEYRENKIHTGWLDSRI 543
Cdd:PRK05586 419 IDFQFIILEDEEFIKGTYDTSFIEKKL 445
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
41-541 |
3.36e-82 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 296.74 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 41 SVLVANNGMAAVKFMRSiriwaletfGTEKAILLVAMATPEDLKinAEHIRIAD---QFIEVPGGTNNNNYANVQLIVEI 117
Cdd:TIGR01235 1 KILVANRGEIAIRVFRA---------ANELGIRTVAIYSEEDKL--SLHRQKADesyQVGEGPDLGPIEAYLSIDEIIRV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 118 AERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGShvkvPPEschsip 197
Cdd:TIGR01235 70 AKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDG----PPE------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 198 eelyrnacvsTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGS----PIFIMKVASQSRHL 273
Cdd:TIGR01235 140 ----------TMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYVEKLIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 274 EVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLE 353
Cdd:TIGR01235 210 EVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD-NDGKFYFIE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 354 LNPRLQVEHPVTEWIAEINLPAAQ--VAVGMGIPlynipeirrfygmdhgggyhnwrtisavATKFDLDKAQSVRPKGHC 431
Cdd:TIGR01235 289 VNPRIQVEHTVTEEITGIDIVQAQihIADGASLP----------------------------TPQLGVPNQEDIRTNGYA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 432 VAVRVTSEDPDDGFKPTSGRVEElnFKSKPNvwayFSVK-------SGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGL 504
Cdd:TIGR01235 341 IQCRVTTEDPANNFQPDTGRIEA--YRSAGG----FGIRldggnsyAGAIITPYYDSLLVKVSAWASTPEEAAAKMDRAL 414
|
490 500 510
....*....|....*....|....*....|....*..
gi 670402573 505 KEIQIRGeIRTNVDYTVDLLNATEYRENKIHTGWLDS 541
Cdd:TIGR01235 415 REFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFIDT 450
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-540 |
5.43e-75 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 257.75 E-value: 5.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 39 IHSVLVANNGMAAVKFMRSIRiwaleTFGtEKAILLVAMATPEdlkinAEHIRIADQFIEVPGGTNNNNYANVQLIVEIA 118
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ-----EMG-KEAIAIYSTADKD-----ALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 119 ERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGSHVKvppeschsipe 198
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALK----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 199 elyrnacvsTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGS----PIFIMKVASQSRHLE 274
Cdd:PRK08462 142 ---------SYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFINNPRHIE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 275 VQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLEL 354
Cdd:PRK08462 213 VQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 355 NPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLYnipeirrfygmdhgggyhnwrtisavatkfdldKAQSVRPKGHCVAV 434
Cdd:PRK08462 292 NTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP---------------------------------SQESIKLKGHAIEC 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 435 RVTSEDPDDgFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeIR 514
Cdd:PRK08462 339 RITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-IK 416
|
490 500
....*....|....*....|....*.
gi 670402573 515 TNVDYTVDLLNATEYRENKIHTGWLD 540
Cdd:PRK08462 417 TTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-541 |
1.08e-73 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 255.03 E-value: 1.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 39 IHSVLVANNGMAAVKFMRSIRiwaletfgtEKAILLVAMATPEDLkiNAEHIRIADQFIEVpGGTNNNNYANVQLIVEIA 118
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEADR--HALHVKRADEAYSI-GADPLAGYLNPRRLVNLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 119 ERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsGSHvkvppeschsipe 198
Cdd:PRK07178 70 VETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTP--GSE------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 199 elyrnACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVP---GSP-IFIMKVASQSRHLE 274
Cdd:PRK07178 135 -----GNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVFLEKCIVNPKHIE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 275 VQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGP---ITIAAPDTVKELeqaARQLAKCVQYVGAATVEYLYSMEtGEYYF 351
Cdd:PRK07178 210 VQILADSHGNVVHLFERDCSIQRRNQKLIEIAPspqLTPEQRAYIGDL---AVRAAKAVGYENAGTVEFLLDAD-GEVYF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 352 LELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPL-YNIPEIRRfygmdhgggyhnwrtisavatkfdldkaqsvrpKGH 430
Cdd:PRK07178 286 MEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH---------------------------------RGF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 431 CVAVRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIR 510
Cdd:PRK07178 333 ALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRRALDDMRVQ 412
|
490 500 510
....*....|....*....|....*....|.
gi 670402573 511 GeIRTNVDYTVDLLNATEYRENKIHTGWLDS 541
Cdd:PRK07178 413 G-VKTTIPYYQEILRNPEFRSGQFNTSFVES 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
39-543 |
1.04e-68 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 240.49 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 39 IHSVLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDLkiNAEHIRIADQFIEVpGGTNNNNYANVQLIVEIA 118
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKS---------VAIYTEPDR--ECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 119 ERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPwsGSHvKVPPESCHSIPE 198
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP--GTE-KLNSESMEEIKI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 199 ELYRnacvstteeavascqvVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPG----SPIFIMKVASQSRHLE 274
Cdd:PRK08463 147 FARK----------------IGYPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAyfnnDEVFMEKYVVNPRHIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 275 VQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmETGEYYFLEL 354
Cdd:PRK08463 211 FQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNRFYFMEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 355 NPRLQVEHPVTEWIAEINLPAAQVAVGMGiplynipEIrrfygmdhgggyhnwrtisavatkfdLDKAQS-VRPKGHCVA 433
Cdd:PRK08463 290 NTRIQVEHGVTEEITGIDLIVRQIRIAAG-------EI--------------------------LDLEQSdIKPRGFAIE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 434 VRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeI 513
Cdd:PRK08463 337 ARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG-I 415
|
490 500 510
....*....|....*....|....*....|
gi 670402573 514 RTNVDYTVDLLNATEYRENKIHTGWLDSRI 543
Cdd:PRK08463 416 RTTIPFLIAITKTREFRRGYFDTSYIETHM 445
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
163-386 |
3.71e-53 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 185.97 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 163 DKIGSSLIAQAAGVPTLPWSgshvkvppeschsipeelyrNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHND 242
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGT--------------------AGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 243 DEVRALFKQVQGEVPGSP----IFIMKVASQSRHLEVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITIAAPDTVKE 318
Cdd:pfam02786 61 EELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQM 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 670402573 319 LEQAARQLAKCVQYVGAATVEYLYSMETGEYYFLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPL 386
Cdd:pfam02786 141 LREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
39-157 |
1.68e-43 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 154.18 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 39 IHSVLVANNGMAAVKFMRSIRIWALETfgtekaillVAMATPEDlkINAEHIRIADQFIEVPGGTNNNNYANVQLIVEIA 118
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRT---------VAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 670402573 119 ERTRVSAVWPGWGHASENPELPDALDEKGIIFLGPPSAA 157
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
111-385 |
5.37e-36 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 138.47 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 111 VQLIVEIAERTRVSAVWPGWGHASEN-PELPDALDekgiiFLGPPSAAMAALGDKIGSSLIAQAAGVPTlPWSgshvkvp 189
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVETaAELAEELG-----LPGPSPEAIRAMRDKVLMREALAAAGVPV-PGF------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 190 peschsipeelyrnACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEV----PGSPIFIMK 265
Cdd:COG0439 73 --------------ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGEVLVEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 266 VAsQSRHLEVQLLCDkHGNVaaLHsrdCSVQRRHQK---IIEEGPITIAA--PDTVKELEQAARQLAKCVQYV-GAATVE 339
Cdd:COG0439 139 FL-EGREYSVEGLVR-DGEV--VV---CSITRKHQKppyFVELGHEAPSPlpEELRAEIGELVARALRALGYRrGAFHTE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 670402573 340 YLYsMETGEYYFLELNPRLQVEH--PVTEWIAEINLPAAQVAVGMGIP 385
Cdd:COG0439 212 FLL-TPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
434-540 |
9.63e-29 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 112.20 E-value: 9.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 434 VRVTSEDPDDGFKPTSGRVEELNFKSKPNVWAYFSVKSGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEIQIRGeI 513
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*..
gi 670402573 514 RTNVDYTVDLLNATEYRENKIHTGWLD 540
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
91-393 |
5.37e-23 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 103.47 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 91 RIADQFIEVPGGTNNNNyANVQLIVEIAERTRVSAVWP---GWGHA-SEN-PELpdaldEKGIIFLGPPSAAMAALGDKI 165
Cdd:COG3919 46 RYVDEVVVVPDPGDDPE-AFVDALLELAERHGPDVLIPtgdEYVELlSRHrDEL-----EEHYRLPYPDADLLDRLLDKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 166 GSSLIAQAAGVPtlpwsgshvkvppeschsIPEELYrnacVSTTEEAVASCQVVGYPAMIKASWG--------GGGKGIR 237
Cdd:COG3919 120 RFYELAEELGVP------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGKKKVF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 238 KVHNDDEVRALFKQ---------VQGEVPGSpifimkvasQSRHLEVQLLCDKHGNVAALhsrdCSVQRRHQKIIEEGPI 308
Cdd:COG3919 178 YVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVAT----FTGRKLRHYPPAGGNS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 309 TIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSMETGEYYFLELNPRL--QVEHPVtewIAEINLPAAQVAVGMGIPL 386
Cdd:COG3919 245 AARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFwrSLYLAT---AAGVNFPYLLYDDAVGRPL 321
|
....*..
gi 670402573 387 YNIPEIR 393
Cdd:COG3919 322 EPVPAYR 328
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1607-1957 |
7.05e-18 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 89.70 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1607 GREIIVVANDVTFKAGSFGPREDAFFDAVTNLACERKLPLIYLAATAGARLGVAEEIKScfHVGwsdyespeRGFQYIYL 1686
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFA--GYG--------RIFYRNAR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1687 ttqdysrlSSSVIAhelQLkngetrwvvdTIVgkedglgcenlHGSGAIASAYSKAyketftLT------------FVTG 1754
Cdd:COG4799 151 --------SSGGIP---QI----------SVI-----------MGPCAAGGAYSPA------LSdfvimvkgtsqmFLGG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1755 ----RAVGigaylarlgmrciqrldqpiiltgfsalnkllGREVysSHMQLGGPKI-MATNGVVHQTVSDDLEGVSAILK 1829
Cdd:COG4799 193 ppvvKAAT--------------------------------GEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 1830 WLSYVPPYVGGPLPIMKPlDPPERPVTYL----PEN---ACDALAAICGIqdgegrwlggmFDRESFVETLEGWAKTVIT 1902
Cdd:COG4799 239 LLSYLPSNNLEDPPRAEP-APPARDPEELygivPEDprkPYDMREVIARL-----------VDGGSFFEFKPLYGPNIVT 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 670402573 1903 GRAKLGGIPVGVIAvetqtvmqvipADPGQLdsaervvpqAGqVWFPDSATKTAQ 1957
Cdd:COG4799 307 GFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAAR 340
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
202-395 |
2.46e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 79.27 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 RNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDk 281
Cdd:TIGR01369 686 KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 282 HGNV-----------AALHSRDCSVQRRHQKIieegpitiaAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmeTGEYY 350
Cdd:TIGR01369 765 GEEVlipgimehieeAGVHSGDSTCVLPPQTL---------SAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK--DGEVY 833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 670402573 351 FLELNPRLQVEHPVTEWIAEINLPAAQVAVGMGIPLYNIPEIRRF 395
Cdd:TIGR01369 834 VIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGVGKEK 878
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
680-744 |
2.51e-13 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 66.67 E-value: 2.51e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670402573 680 LLADTPCKLLRFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIHFVM-PEGQAMKANDLIARL 744
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
82-357 |
4.12e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 66.83 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 82 DLKINAEHIRIADQFIEVPGGTNNNnYANVqlIVEIAERTRVSAVWPGwghaSEnPELP------DALDEKGIIFLGPPS 155
Cdd:PRK12767 32 DISELAPALYFADKFYVVPKVTDPN-YIDR--LLDICKKEKIDLLIPL----ID-PELPllaqnrDRFEEIGVKVLVSSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 156 AAMAALGDKIGSSLIAQAAGVPTlpwsgshvkvpPESChsipeelyrnaCVSTTEEAVASCQV--VGYPAMIKASWGGGG 233
Cdd:PRK12767 104 EVIEICNDKWLTYEFLKENGIPT-----------PKSY-----------LPESLEDFKAALAKgeLQFPLFVKPRDGSAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 234 KGIRKVHNDDEVRALFKQVQGevpgspIFIMKVASQSrhlE--VQLLCDKHGNVAALHSRdcsvqRRHQKIIEEGPITIA 311
Cdd:PRK12767 162 IGVFKVNDKEELEFLLEYVPN------LIIQEFIEGQ---EytVDVLCDLNGEVISIVPR-----KRIEVRAGETSKGVT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 670402573 312 APDtvKELEQAARQLAKCVQYVGAATVEYLYSmeTGEYYFLELNPR 357
Cdd:PRK12767 228 VKD--PELFKLAERLAEALGARGPLNIQCFVT--DGEPYLFEINPR 269
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
690-744 |
4.16e-10 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 57.61 E-value: 4.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 670402573 690 RFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIHFVM-PEGQAMKANDLIARL 744
Cdd:pfam00364 18 EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILvPEGDTVEVGDPLAKI 73
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
208-357 |
4.84e-10 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 65.18 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 208 TTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDE-VRALFKQVQGEvPGSPIFIMKVASQSRHLEVQLLCDKHGNV- 285
Cdd:PLN02735 725 SEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKlKTYLETAVEVD-PERPVLVDKYLSDATEIDVDALADSEGNVv 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 286 ----------AALHSRD--CSVqrrhqkiieegPITIAAPDTVKELEQAARQLAKCVQYVGAATVEYLYSMEtGEYYFLE 353
Cdd:PLN02735 804 iggimehieqAGVHSGDsaCSL-----------PTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPS-GEVYIIE 871
|
....
gi 670402573 354 LNPR 357
Cdd:PLN02735 872 ANPR 875
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
202-421 |
3.95e-09 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 61.82 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 RNACVSTTEEAVASCQVVGYPAMIKASW--GGGGKGIrkVHNDDEVRALFKQVQGEVPGSPIFImkvaSQS----RHLEV 275
Cdd:COG0458 131 KSGTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLI----DESllgaKEIEV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 276 QLLCDKHGNV-----------AALHSRDcSvqrrhqkiieegpITIAAP-----DTVKELEQAARQLAKCVQYVGAATVE 339
Cdd:COG0458 205 DVVRDGEDNViivgimehiepAGVHSGD-S-------------ICVAPPqtlsdKEYQRLRDATLKIARALGVVGLCNIQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 340 YLysMETGEYYFLELNPRLQ---------VEHPvtewIAEInlpAAQVAVGmgiplYNIPEIRRFYGMdhgggyhnWRTI 410
Cdd:COG0458 271 FA--VDDGRVYVIEVNPRASrsspfaskaTGYP----IAKI---AAKLALG-----YTLDELGNDTGF--------EPTL 328
|
250
....*....|....
gi 670402573 411 SAVATK---FDLDK 421
Cdd:COG0458 329 DYVVVKepvFPFEK 342
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
202-357 |
3.11e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 56.13 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 RNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKqvQGEVPGSPIFIMKVASqSRHLEVQLLCD- 280
Cdd:PRK12815 687 PGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFID-GKEYEVDAISDg 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 281 ---------KHGNVAALHSRDcsvqrrhqKIIEEGPITIaAPDTVKELEQAARQLAKCVQYVGAATVEYLysMETGEYYF 351
Cdd:PRK12815 764 edvtipgiiEHIEQAGVHSGD--------SIAVLPPQSL-SEEQQEKIRDYAIKIAKKLGFRGIMNIQFV--LANDEIYV 832
|
....*.
gi 670402573 352 LELNPR 357
Cdd:PRK12815 833 LEVNPR 838
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
194-393 |
1.13e-06 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 54.23 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 194 HSIPEELYRNACVSTTEEAVASCQVVGYPAMIKASW--GGGGKGIrkVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSR 271
Cdd:TIGR01369 136 KEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 272 HLEVQLLCDKHGNVAALhsrdCSVQRRHQKIIEEG-PITIAAPDTVKELE-----QAARQLAKCVQYVGAATVEYLYSME 345
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENFDPMGVHTGdSIVVAPSQTLTDKEyqmlrDASIKIIRELGIEGGCNVQFALNPD 289
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 670402573 346 TGEYYFLELNPRLQ---------VEHPvtewIAEInlpAAQVAVGmgiplYNIPEIR 393
Cdd:TIGR01369 290 SGRYYVIEVNPRVSrssalaskaTGYP----IAKV---AAKLAVG-----YTLDELK 334
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
108-247 |
1.65e-06 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 52.42 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 108 YANVQLIVEIAERTRVSAVWP----GWGhasENPELPDALDEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWsg 183
Cdd:COG1181 39 GIDVEDLPAALKELKPDVVFPalhgRGG---EDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPY-- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670402573 184 shvkvppeschsipeELYRNACVSTTEEAVAScqvVGYPAMIKASWGGGGKGIRKVHNDDEVRA 247
Cdd:COG1181 114 ---------------VVLRRGELADLEAIEEE---LGLPLFVKPAREGSSVGVSKVKNAEELAA 159
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
141-356 |
2.07e-05 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 48.78 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 141 DALDEKGIIFLGPPsAAMAALGDKIGSSLIAQAAGVPTlpwsgshvkvpPESchsipeelyrnACVSTTEEAVASCQVVG 220
Cdd:COG0189 75 RQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPV-----------PPT-----------LVTRDPDDLRAFLEELG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 221 YPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQgEVPGSPIFIMKVASQSRHLEVQLLC--DKHgnVAAlhsrdcsVQRR 298
Cdd:COG0189 132 GPVVLKPLDGSGGRGVFLVEDEDALESILEALT-ELGSEPVLVQEFIPEEDGRDIRVLVvgGEP--VAA-------IRRI 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670402573 299 HQKiiEEGPITIAAPDTV------KELEQAARQLAKCV--QYVGaatVEYLYSMetGEYYFLELNP 356
Cdd:COG0189 202 PAE--GEFRTNLARGGRAepveltDEERELALRAAPALglDFAG---VDLIEDD--DGPLVLEVNV 260
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
137-395 |
2.29e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 49.15 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 137 PELPDALdEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGShvkvPPESChsipeelyrnacvstteeavasc 216
Cdd:COG2232 87 PELLERL-ARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFE----PPPDP----------------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 217 qvvgYPAMIKASWGGGGKGIRKVHNDDEVRALFkQVQGEVPGSPifimkvASqsrhleVQLLCDKHGNVAALHSRdcsvq 296
Cdd:COG2232 139 ----GPWLVKPIGGAGGWHIRPADSEAPPAPGR-YFQRYVEGTP------AS------VLFLADGSDARVLGFNR----- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 297 rrhQKIIEE-----------GPITIaAPDTVKELEQAARQLAKCVQYVGAATVEYLysMETGEYYFLELNPRLQVEHPVT 365
Cdd:COG2232 197 ---QLIGPAgerpfryggniGPLAL-PPALAEEMRAIAEALVAALGLVGLNGVDFI--LDGDGPYVLEVNPRPQASLDLY 270
|
250 260 270
....*....|....*....|....*....|.
gi 670402573 366 EWIAEINLPAAQVAVGMG-IPLYNIPEIRRF 395
Cdd:COG2232 271 EDATGGNLFDAHLRACRGeLPEVPRPKPRRV 301
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
202-357 |
4.34e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.94 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 202 RNACVSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDk 281
Cdd:PRK05294 686 PNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 282 HGNV-----------AALHSRD--CSVqrrhqkiieeGPITIaAPDTVKELEQAARQLAKCVQYVGAATVEYLYSmeTGE 348
Cdd:PRK05294 765 GEDVliggimehieeAGVHSGDsaCSL----------PPQTL-SEEIIEEIREYTKKLALELNVVGLMNVQFAVK--DDE 831
|
....*....
gi 670402573 349 YYFLELNPR 357
Cdd:PRK05294 832 VYVIEVNPR 840
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
206-392 |
8.11e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 48.04 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 206 VSTTEEAVASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDKHGNV 285
Cdd:PRK12815 149 VTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNC 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 286 AALhsrdCSVQRRHQKIIEEGPITIAAP------DTVKELEQAARQLAKCVQYVGAATVEYLYSMETGEYYFLELNPRLQ 359
Cdd:PRK12815 229 ITV----CNMENIDPVGIHTGDSIVVAPsqtltdDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVS 304
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 670402573 360 VE---------HPvtewIAEInlpAAQVAVGmgiplYNIPEI 392
Cdd:PRK12815 305 RSsalaskatgYP----IAKI---AAKLAVG-----YTLNEL 334
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
684-744 |
1.76e-04 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 41.62 E-value: 1.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670402573 684 TPCKLLRFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIH-FVMPEGQAMKANDLIARL 744
Cdd:cd06849 13 TEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAkILVEEGDTVPVGQVIAVI 74
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
172-356 |
3.31e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 172 QAAGVPTLPWsgshVKVPPESCHSIPEELYRNACvstteeavascQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFK- 250
Cdd:pfam07478 3 KAAGLPVVPF----VTFTRADWKLNPKEWCAQVE-----------EALGYPVFVKPARLGSSVGVSKVESREELQAAIEe 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 251 --QVQGEVpgspifIMKVASQSRHLEVQLLCDKHGNVAALHSR--DCSVQRRHQKIIEEGPITIAAPDTVKELEQAARQL 326
Cdd:pfam07478 68 afQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQEL 141
|
170 180 190
....*....|....*....|....*....|....
gi 670402573 327 A----KCVQYVGAATVEYLYSmETGEYYFLELNP 356
Cdd:pfam07478 142 AlkayKALGCRGLARVDFFLT-EDGEIVLNEVNT 174
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
214-359 |
6.35e-04 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 42.37 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 214 ASCQVVGYPAMIKASWGGGGKGIRKVHNDDEVRALFKQ--VQGEVPGspifimkvasqsRHLEVQLLCDKHGNVAALHSR 291
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEG------------EPLSVSLLSDGEKALPLSVNR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670402573 292 DcSVQRRHQKIIEEGPITIAAPDTVKELEQAARQLAKCVQ----YVGaatVEYLYSmeTGEYYFLELNPRLQ 359
Cdd:pfam02655 93 Q-YIDNGGSGFVYAGNVTPSRTELKEEIIELAEEVVECLPglrgYVG---VDLVLK--DNEPYVIEVNPRIT 158
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
150-250 |
8.72e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 43.95 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 150 FLGPP---SAAMA-ALG-DKIGSSLIAQAAGVPTLPWsgshvkvppeschsipeelyrnACVSTTEEAVASCQVVGYPAM 224
Cdd:PRK01372 80 LLGIPytgSGVLAsALAmDKLRTKLVWQAAGLPTPPW----------------------IVLTREEDLLAAIDKLGLPLV 137
|
90 100
....*....|....*....|....*.
gi 670402573 225 IKASWGGGGKGIRKVHNDDEVRALFK 250
Cdd:PRK01372 138 VKPAREGSSVGVSKVKEEDELQAALE 163
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
141-339 |
1.13e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 43.60 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 141 DALDEKGIIFlgPPSAAMAALGDKIGS-SLIAQAaGVPTLPWsgshvkvppeschsipeelyrnACVSTTEEAVASCQVV 219
Cdd:PRK06019 80 DALAARVPVP--PGPDALAIAQDRLTEkQFLDKL-GIPVAPF----------------------AVVDSAEDLEAALADL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 220 GYPAMIKASWGG-GGKGIRKVHNDDEVRALFKqvqgEVPGSPIFIMKVASQSRhlEVQLLC--DKHGNVAALhsrDCsVQ 296
Cdd:PRK06019 135 GLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWA----LLGSVPCILEEFVPFER--EVSVIVarGRDGEVVFY---PL-VE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 670402573 297 RRHQK-IIEEgpiTIAAPDTVKELEQAARQLAKCV----QYVGAATVE 339
Cdd:PRK06019 205 NVHRNgILRT---SIAPARISAELQAQAEEIASRIaeelDYVGVLAVE 249
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
152-356 |
1.63e-03 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 43.65 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 152 GPPSAAMAALG-DKIGSSLIAQAAGVPTLPWSgshvkvpPESCHSIPEElyRNACVSTTEEAVAscqvvgYPAMIKASWG 230
Cdd:PRK14573 556 TGPSLAFSAIAmDKVLTKRFASDVGVPVVPYQ-------PLTLAGWKRE--PELCLAHIVEAFS------FPMFVKTAHL 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670402573 231 GGGKGIRKVHNDDEVRAlfKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDKHGN--VAALHSRdC------SVQRRH--- 299
Cdd:PRK14573 621 GSSIGVFEVHNVEELRD--KISEAFLYDTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYgls 697
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 670402573 300 ----QKIIEEGPITIAAPDTVKELeqaARQLAKCVQYVGAATVEYLYSMEtGEYYFLELNP 356
Cdd:PRK14573 698 gkssAQIVFDLDLSKESQEQVLEL---AERIYRLLQGKGSCRIDFFLDEE-GNFWLSEMNP 754
|
|
| |
