|
Name |
Accession |
Description |
Interval |
E-value |
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
142-596 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 745.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPHKGMTTVDDFFQGTKAA 221
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQV 301
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 302 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 381
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 382 SKSAADLISQARKKGNVVFGEPITASLGTDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 461
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 462 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPD 540
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 541 AVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 596
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
142-591 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 734.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPHKGMTTVDDFFQGTKAA 221
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKdKGVNSFMVYMAYKDLYQV 301
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 302 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 381
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 382 SKSAADLISQARKKGNVVFGEPITASLGTDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 461
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 462 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDA 541
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1953317075 542 VKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAG 591
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
141-600 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 562.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 141 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPHKGMTTVDDFFQGTKA 220
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 221 ALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIkDKGVNSFMVYMAYKDLYQ 300
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 301 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKV 380
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 381 MSKSAADLISQARKKGNVVFGEPITASLGTDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 457
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 458 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVI 536
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953317075 537 WDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 600
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
139-610 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 544.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 139 SDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPHKGMTTVDDFFQGT 218
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 219 KAALAGGTTMIIDHVVPePEASLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDL 298
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 299 YQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVT 378
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 379 KVMSKSAADLISQARKKGNVVFGEPITASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGSAH 458
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 459 CTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWD 538
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953317075 539 PDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 610
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
143-595 |
1.45e-124 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 377.51 E-value: 1.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 143 LIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAAL 222
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 223 AGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLiKDKGVNSFMVYMAYKDLYQVS 302
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 303 NTE-LYEIFTCLGELGAIAQVHAENGDIIAQeqtRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVM 381
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 382 SKSAADLISQARKKGNVVFGE--P----ITAS-LGTDGTHYwsknwakaaafVTSPPLSpdptTPDYINSL---LASGDL 451
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR----TEEDREALwegLADGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 452 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 531
Cdd:COG0044 300 DVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953317075 532 SDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 595
Cdd:COG0044 376 ADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
142-598 |
4.96e-113 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 349.00 E-value: 4.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPH-KGMTTVDDFFQGTKA 220
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 221 ALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQNLIKDkGVNSFMVYMAYKDLy 299
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 300 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTK 379
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 380 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGTDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 452
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 453 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIS 527
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953317075 528 VGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 598
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
142-594 |
3.41e-64 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 219.47 E-value: 3.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDhvVP---EPEASLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLIK--DKGV---NSFMVYM 293
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 294 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNC 373
Cdd:cd01315 152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 374 PLYVTKVMSKSAADLISQARKKGNVVFGEpitaslgtDGTHYWS-------KNwakAAAFVTSPPLSpDPTTPDYINSLL 446
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 447 ASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRI 526
Cdd:cd01315 300 ENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRI 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953317075 527 SVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 594
Cdd:cd01315 380 AVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
188-568 |
1.31e-58 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 201.08 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 188 KMVIPGGIDVHTHFQMPhKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDIt 267
Cdd:cd01302 1 LLVLPGFIDIHVHLRDP-GGTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 268 hWNDSVKQEVQNLIkDKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqtrmlemgitgp 345
Cdd:cd01302 79 -GPGDVTDELKKLF-DAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 346 eghvlsrpeeleaeavfRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGTDgTHYWSKNWAKaaa 425
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 426 FVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDENQF 505
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953317075 506 VAVTSTNAAKIFNLYPrKGRISVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAP 568
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
142-595 |
4.81e-52 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 186.43 E-value: 4.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLT-EAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNL--IKDKGVNSFMVYMAY--- 295
Cdd:TIGR03178 79 AAGGITTYIDMPLNSIPATTTrASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSPsgd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 296 KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPL 375
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 376 YVTKVMSKSAADLISQARKKGnvvfgepITASLGTdGTHYWSKNWAK----AAAFVTSPPLSPDPTTPDYINSLLAsGDL 451
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEG-------LDVTVET-CPHYLTLTAEEvpdgGTLAKCAPPIRDLANQEGLWEALLN-GLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 452 QLSGSAHCTFSTAQKAigKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 531
Cdd:TIGR03178 304 DCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953317075 532 SDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 595
Cdd:TIGR03178 381 ADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
142-585 |
3.04e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 184.52 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLIK--DKGVNSFMVYMAYK-- 296
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 297 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPL 375
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 376 YVTKVMSKSAADLISQARKKGnvvfgepITASLGTdGTHY--WSKN--WAKAAAFVTSPPLSPDPTTPDYINSLLAsGDL 451
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLRSRSQKEELWRGLLA-GEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 452 QLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVG 529
Cdd:PRK06189 307 DMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 530 SDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLH 585
Cdd:PRK06189 382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
142-595 |
1.31e-49 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 179.85 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQNL--IKDKGVNSF-MVYMA--YK 296
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLesLWERGVFALgEIFMAdsTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 297 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQTRMLEmGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLY 376
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 377 VTKVMSKSAADLISqarkkgnvvfGEPITaslgTDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSlLASGDL 451
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGIT----CEVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWER-LNDGTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 452 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSD 531
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953317075 532 SDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 595
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
158-581 |
1.21e-46 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 170.70 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALAGGTTMIIDHVVPEP 237
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 238 EASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNteLYEIFTCLGELG 317
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGRMFTDDGSEVQDILS--MRRALEYAAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 318 AIAQVHAENGDIIAQEQTRMLEMgitGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKgn 397
Cdd:TIGR00857 161 VPIALHAEDPDLIYGGVMHEGPS---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQ-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 398 vvfGEPITAS------LGTDGTHYWSKNWAKaaafvTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKD 471
Cdd:TIGR00857 236 ---GIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEK---TK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 472 NFTAIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDLVIWDPDAVKIVSAKSHQ 551
Cdd:TIGR00857 304 EFAAAPPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFY 381
|
410 420 430
....*....|....*....|....*....|
gi 1953317075 552 SAAEYNIFEGLELRGAPLVVICQGKIMLED 581
Cdd:TIGR00857 382 SKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
187-575 |
1.31e-34 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 135.15 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 187 GKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDI 266
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 267 ThwndsvKQEVQNLIKDKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQTRMLEMGItg 344
Cdd:cd01318 79 T------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 345 pegHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGTdgthyws 417
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 418 knWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAVAT 497
Cdd:cd01318 217 --LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LVNK 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953317075 498 GKMDENQFVAVTSTNAAKIFNLyPRKGRISVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQG 575
Cdd:cd01318 285 GILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
142-547 |
2.92e-34 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 136.14 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLTEA-YEKWREWADGKSCCDYALHVDITHWNDSVKQEvqnlIKDKGVNSFMVYMAY----- 295
Cdd:PRK08044 81 AKGGITTMIEMPLNQLPATVDRAsIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHE----LDEVGVVGFKCFVATcgdrg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 296 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNC 373
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 374 PLYVTKVMSKSAADLISQARKKGNVVFGEPITaslgtdgtHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 449
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 450 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRISVG 529
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
|
410
....*....|....*...
gi 1953317075 530 SDSDLVIWDPDAVKIVSA 547
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKN 401
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
141-581 |
1.36e-33 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 133.78 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 141 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTK 219
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 220 AALAGGTTMIidHVVP--EPEASLTEAYEKWREWADGKSCCDyaLHV--DIThwndsVKQEVQNL-----IKDKGVNSFM 290
Cdd:PRK09357 79 AAAAGGFTTV--VAMPntKPVIDTPEVVEYVLDRAKEAGLVD--VLPvgAIT-----KGLAGEELtefgaLKEAGVVAFS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 291 vymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQTRMLEMGITGpeghvlsRPEELEAEAVFRA 364
Cdd:PRK09357 150 -----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVMIARD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 365 ITIASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITA------------SLGTDGTHYwsknwaKAAafvtsPPL 432
Cdd:PRK09357 217 VLLAEATGARVHICHVSTAGSVELIRWAKAL-----GIKVTAevtphhllltdeDLLTYDPNY------KVN-----PPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 433 SpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVT 509
Cdd:PRK09357 281 R----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKM 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953317075 510 STNAAKIFNLYPrkGRISVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLED 581
Cdd:PRK09357 354 TINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
179-569 |
1.21e-30 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 123.89 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 179 GVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALAGGTTmiidHVVPEPEAslteayekwREWADgkscc 258
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVID----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 259 dyalhvdithwNDSVKQEVQNLIKDKGVNSFMVYMAY-KDLYQVSNTELYEiftcLGELGAIA----------------- 320
Cdd:cd01317 61 -----------NPAVVELLKNRAKDVGIVRVLPIGALtKGLKGEELTEIGE----LLEAGAVGfsddgkpiqdaellrra 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 321 -----------QVHAENGDIIAQEQtrMLEMGITGPEGhVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLI 389
Cdd:cd01317 126 leyaamldlpiIVHPEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 390 SQARKKGnvvfgEPITAS------------LGTDGThywsknwakaaAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSA 457
Cdd:cd01317 203 RKAKAKG-----LPVTAEvtphhlllddeaLESYDT-----------NAKVNPPLR-SEEDREALIEALKDGTIDAIASD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 458 HCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRISVGSDSDLVIW 537
Cdd:cd01317 266 HAPHTDEEKDLP---FAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLF 340
|
410 420 430
....*....|....*....|....*....|..
gi 1953317075 538 DPDAVKIVSAKSHQSAAEYNIFEGLELRGAPL 569
Cdd:cd01317 341 DPDAEWIVDEETFRSKSKNTPFDGQKLKGRVL 372
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
139-584 |
9.34e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 122.86 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 139 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQG 217
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 218 TKAALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIkdkGVNSFMVYMaYKD 297
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 298 LYQVSNTELYEIFTCLGELgaIAqVHAENgdiiaqeQTRMLE-----MGITGPEGHVLSRPEELEAEAVFRAITIASQTN 372
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAED-------QARIRArraefAGISDPADHSQIQDEEAALLATRLALKLSKKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 373 CPLYVTKVMSKSAADLISQArkKGNVVFGE--PITASLGTDgthywskNWAKAAAFV-TSPPLSpDPTTPDYINSLLASG 449
Cdd:PRK07575 226 RRLHILHLSTAIEAELLRQD--KPSWVTAEvtPQHLLLNTD-------AYERIGTLAqMNPPLR-SPEDNEALWQALRDG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 450 DLQLSGSAHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRISVG 529
Cdd:PRK07575 296 VIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1953317075 530 SDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNL 584
Cdd:PRK07575 371 YDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
147-582 |
1.15e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 118.72 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 147 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTH---FQMPHKgmTTVDdffQGTKAALA 223
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 224 GGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVdITHWNDSVKQEVQNLIKDKgvnsFMVyMAYKDLYQVSN 303
Cdd:PRK04250 77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNF-LIAGNCEKAEEIKADFYKI----FMG-ASTGGIFSENF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 304 TELYEiftclgELGAIAQVHAENGDIIAQEqtrmlemgitgPEghvlsRPEELEAEAVFRAITIASQTNCPLYVTKVMSK 383
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 384 SAADLISQARKkgnvvfgEPITASLGTDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 463
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 464 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrISVGSDSDLVIWDPDAVK 543
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
|
410 420 430
....*....|....*....|....*....|....*....
gi 1953317075 544 IVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDG 582
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
142-592 |
5.15e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 111.55 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAA 221
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 222 LAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMvYMAYKDLYQV 301
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELERLPGCAGIKVFM-GSSTGDLLVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 302 SNTELYEIftclgeLGAI---AQVHAEngdiiaqEQTRMLEMGITGPEGHVLSRPEELEAEAVFRA----ITIASQTNCP 374
Cdd:PRK09060 163 DDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETGRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 375 LYVTKVMSKSAADLISQARKKGNV--------VFGEPITASLGTdgthYWSKNwakaaafvtsPPLSpDPTTPDYINSLL 446
Cdd:PRK09060 230 IHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 447 ASGDLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRI 526
Cdd:PRK09060 295 RQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRI 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 527 SVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLhVTQGAGR 592
Cdd:PRK09060 370 AVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
147-594 |
7.88e-26 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 111.79 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 147 GRIVNDDQSFYADIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALA 223
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 224 GGTTMIIDhvVP---EPEASLTEAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNLIKDK--------GVNSFMVY 292
Cdd:PLN02795 129 GGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPENAHNASVLEelldagalGLKSFMCP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 293 MAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQtrMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTN 372
Cdd:PLN02795 201 SGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 373 -------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITaslgtdgtHYWsknwAKAAA--------FVTSPPLSpDP 436
Cdd:PLN02795 279 pggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIR-DA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 437 TTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKI 516
Cdd:PLN02795 346 ANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 517 FNLyPRKGRISVGSDSDLVIWDPDAVKIVSAKS-----HQSAAEYNifeGLELRGAPLVVICQGKIMLEDGNlHVTQGAG 591
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAEFVLDESYpiyhkHKSLSPYL---GTKLSGKVIATFVRGNLVFLEGK-HAKQACG 499
|
...
gi 1953317075 592 RFI 594
Cdd:PLN02795 500 SPI 502
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
157-595 |
1.69e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 106.48 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 157 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 236
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 237 PEASLTEAYEKWREWADGKSCCDYALHVDITHWNdsvkqevqNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIfTCLGEL 316
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNN--------ALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 317 GAIAQVHAENGDIIAQEQTRMLEMgitgpEGHVLSRPEELEAEAVFRAITIASQtncplyvTKVMS-KSAADLISQarkk 395
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 396 gnvvFGEPITA---------SLGTDGThywsknwakaaafvTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQK 466
Cdd:PRK01211 224 ----FLREVTPhhlllnddmPLGSYGK--------------VNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 467 AigkdNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLVIWDPDAVKIVS 546
Cdd:PRK01211 285 Q----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKIN 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1953317075 547 AKSHQSAAEYNIFEGLELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 595
Cdd:PRK01211 358 DKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
189-578 |
6.21e-23 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 100.65 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 189 MVIPGGIDVHTHFQMPHKGMTTVDDFF------QGTKAALAGGTTMIIDHVVPEPEASLT--EAYEKWRE--WADGKSCC 258
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 259 ---DYALHVDITHWNDSVKQEvqNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQT 335
Cdd:pfam01979 81 ldtDGELEGRKALREKLKAGA--EFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKG---EVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 336 RMLEMGITGPEghVLSRPEELEAEAVFRAITIASQTNCPLYVTkvmskSAADLISQARKKGNVvfgepitasLGTDGTHY 415
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 416 WSKNWAKAAAfvtspplspdpttpdyinsLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERmsviwdkAV 495
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ-------FD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 496 ATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDavkivsakshqsaaEYNIFEGLELRGAPLVVICQG 575
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
...
gi 1953317075 576 KIM 578
Cdd:pfam01979 332 KIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
140-290 |
5.63e-21 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 96.48 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 140 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMP---HKGmttvdDFFQ 216
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPgltHKG-----DIAS 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953317075 217 GTKAALAGGTTMIID--HVVPepeASLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQNLIKDK--GVNSFM 290
Cdd:PRK09236 77 ESRAAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFM 149
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
138-547 |
9.70e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 70.37 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 138 QSDRLLIKGGRIVNDDQSFY---ADIYMEDGLIKQIGDN--LIVPGGVKTIEANGKMVIPGGIDVHTHFQMPHKGMT--- 209
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 210 -------TVDDFFQGTK---AALAGGTTMIIDH------VVPEPEASLTEAYEKWREWADGKS-CCDYALHvdiTHWNDS 272
Cdd:COG1228 86 agggitpTVDLVNPADKrlrRALAAGVTTVRDLpggplgLRDAIIAGESKLLPGPRVLAAGPAlSLTGGAH---ARGPEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 273 VKQEVQNLIKDkGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqeqtRMLEMGITGPEgHVLSR 352
Cdd:COG1228 163 ARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDIR----LAVEAGVDSIE-HGTYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 353 PEEleaeavfraitiasqtncplyvtkvmsksAADLIsqaRKKGNVVFGePiTASLGTDGTHYWSKNWAKAAAFVtsppl 432
Cdd:COG1228 236 DDE-----------------------------VADLL---AEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV----- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 433 spDPTTPDYINSLLASGdlqlsgsahCTFstaqkAIGKDNFTAIPEGTNGVEErmsvIWdKAVATGkMDENQ-FVAVTSt 511
Cdd:COG1228 277 --REAALANARRLHDAG---------VPV-----ALGTDAGVGVPPGRSLHRE----LA-LAVEAG-LTPEEaLRAATI- 333
|
410 420 430
....*....|....*....|....*....|....*.
gi 1953317075 512 NAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSA 547
Cdd:COG1228 334 NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
142-247 |
1.15e-12 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 70.31 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVIPGGIDVHTHFQM------------- 203
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 204 --------PHKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEAsLTEAYEK 247
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDA-VAEAAEE 135
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
191-591 |
2.79e-11 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 65.55 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 191 IPGGIDVHTHfqMPHKGMTTVDDFFQGTKAALAGGTTMIidHVVPEPEASL--TEAYEKWREWADGKSCCDYALHVDITH 268
Cdd:cd01316 5 LPGLIDVHVH--LREPGATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 269 WNDSVKQEVqnliKDKGVNSFMVymaykdlyqvsnteLYEIFTCLgELGAIAQV--HAE----NGDIIAQEQTRMLemgi 342
Cdd:cd01316 81 TNAATVGEL----ASEAVGLKFY--------------LNETFSTL-ILDKITAWasHFNawpsTKPIVTHAKSQTL---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 343 tgpeghvlsrpeeleaEAVfraITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLgtdgthYWSKNWAK 422
Cdd:cd01316 138 ----------------AAV---LLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 423 AAAFvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGK 499
Cdd:cd01316 193 RGQY----EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 500 MDENQFVAVTSTNAAKIFNLYPRkgrisvgSDSDLVIwDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVICQGKIML 579
Cdd:cd01316 261 LTIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
410
....*....|..
gi 1953317075 580 EDGNLHVTQGAG 591
Cdd:cd01316 333 IDGEIVAPPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
159-593 |
1.06e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 64.01 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 159 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVIPGGIDVHTHF---QMPHKgmttvDDFFQGTKAALAGGT 226
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 227 TMIIDHVVPEPEASLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQNLikdkGVNSFMVYMayKDLyqvsntE 305
Cdd:PRK00369 80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 306 LYEIFTCLGELGAIAQVHAEngdiiaqeqtrmLEMGITGPEGhvLSRPEELEAEAVFraitiasqtncplYVtkvmsKSA 385
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALY-------------YV-----KDY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 386 ADL-ISQARKKGNVVFGEPITASlgTDGT-HYWSKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 463
Cdd:PRK00369 191 QNVhITHASNPRTVRLAKELGFT--VDITpHHLLVNGEKDCLTKVNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 464 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLVI-----WD 538
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTViqfedWR 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1953317075 539 PdavkivsaKSHQSAAEYNIFEGLELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 593
Cdd:PRK00369 340 Y--------STKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
141-247 |
2.39e-09 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 59.84 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 141 RLLIKGGRIV--NDDQSFYAD--IYMEDGLIKQIGDNLIVP---GGVKTIEANGKMVIPGGIDVHTH-FQMPHKGMT--- 209
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLAddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953317075 210 -----------------TVDDFFQGTKAA----LAGGTTMIIDH--VVPEPEASLTEAYEK 247
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
142-230 |
3.19e-09 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 59.62 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQmphkGMTTVDDFFqg 217
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHYD----GQVFWDPDL-- 72
|
90
....*....|...
gi 1953317075 218 TKAALAGGTTMII 230
Cdd:cd01297 73 RPSSRQGVTTVVL 85
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
142-200 |
6.51e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.32 E-value: 6.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953317075 142 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
160-580 |
9.60e-09 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 57.79 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 160 IYMEDGLIKQIGDNLivpGGVKTIEANGKMVIPGGIDVHTHfqmPHKGMTTVDDFFQGTKAALAGGTTMIIdhVVPEPEA 239
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS---LKNDSLSSKNLKSLENECLKGGVGSIV--LYPDSTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 240 SLTEAYekwrewadgksccdyALHVDithwndsvkqevQNLIKDKGVNSFMVYMAYKDlyqvsNTELYEIFTcLGELGAI 319
Cdd:PRK08417 73 AIDNEI---------------ALELI------------NSAQRELPMQIFPSIRALDE-----DGKLSNIAT-LLKKGAK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 320 AqVHAE---NGDIIAQ--EQTRMLEM-------------------GITGPEGHVLSRPEELEAEAVFRAITIASQTNCPL 375
Cdd:PRK08417 120 A-LELSsdlDANLLKViaQYAKMLDVpifcrcedssfddsgvmndGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 376 YVTKVMSKSAADLISQARKKGNVVFGEPITASLGTDGTHywSKNWAKAAAFvtSPPLSpDPTTPDYINSLLASGDLQLSG 455
Cdd:PRK08417 199 LFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKEGKIDFLT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 456 SAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLV 535
Cdd:PRK08417 274 SLHSAKSNSKKDLA---FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLV 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1953317075 536 IWDPDAVKIVSAKshqsaaeYNIFEGLELRGAPLVVICQGKIMLE 580
Cdd:PRK08417 349 LFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
195-412 |
2.27e-08 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 55.80 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 195 IDVHTHFQMPHKGMT----------------TVDDFFQGTKAALAGGTTMIIDHVVPEPEASLTEAYEKWREWADGKSCC 258
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 259 DYALHVDITH----WNDSVKQEVQNLIKD---KGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIA 331
Cdd:cd01292 82 RVVLGLGIPGvpaaVDEDAEALLLELLRRgleLGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 332 QEQTRMLEMGITGPE---GHVLSRPEELEAEAVFRAITIASqtnCPLYVTKVMSKS-AADLISQARKKGNVVfgepitaS 407
Cdd:cd01292 161 RALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV---CPLSNYLLGRDGeGAEALRRLLELGIRV-------T 230
|
....*
gi 1953317075 408 LGTDG 412
Cdd:cd01292 231 LGTDG 235
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
142-200 |
4.36e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 55.66 E-value: 4.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953317075 142 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
141-200 |
1.14e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 54.62 E-value: 1.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953317075 141 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
142-200 |
1.28e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 54.81 E-value: 1.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953317075 142 LLIKGGRI------VNDDQsfyADIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
137-229 |
1.36e-07 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 54.70 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 137 DQSDRLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTHfqmphkGMTTVDDF 214
Cdd:PRK09061 16 MAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQSVAAYR 87
|
90
....*....|....*
gi 1953317075 215 FQgtkaALAGGTTMI 229
Cdd:PRK09061 88 MQ----AFDGVTTAL 98
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
143-200 |
2.39e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.56 E-value: 2.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953317075 143 LIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNliVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
142-231 |
3.02e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.57 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQmphKGMTTVDDFfqgTK 219
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIE---SSMVTPAEF---AR 78
|
90
....*....|...
gi 1953317075 220 AALAGGTT-MIID 231
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
159-538 |
5.29e-07 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 52.33 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 159 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH-FQ------------MPHKGMTTVDDffqgtkaalAGG 225
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHvYQggtrygdrpdmiGVKSGVTTVVD---------AGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 226 T-TMIID---HVVPEPEASLTEAYekwrewadgksccdyalhVDITHWNdsvkqevqnlikdkgvnsfmvymaykdlyQV 301
Cdd:cd01307 72 AgADNIDgfrYTVIERSATRVYAF------------------LNISRVG-----------------------------LV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 302 SNTELYEIFTClgELGAIAQVHAENGDIIAQEQTRMlEMGITGPEGhvlSRPEELEAEavfraitIASQTNCPLYvtkVM 381
Cdd:cd01307 105 AQDELPDPDNI--DEDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKK-------IAKEADLPLM---VH 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 382 SKSAADLISQA---RKKGNVVfgepitaslgtdgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSG 455
Cdd:cd01307 169 IGSPPPILDEVvplLRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HG 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 456 SAHCTFSTAQKAIGKD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRISV 528
Cdd:cd01307 227 TASFSFRVARAAIAAGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAV 304
|
410
....*....|
gi 1953317075 529 GSDSDLVIWD 538
Cdd:cd01307 305 GYDADLTVFD 314
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
140-238 |
1.49e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 51.16 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 140 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTH--------------- 200
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1953317075 201 ---FQMPHKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 238
Cdd:PRK08204 81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
158-253 |
3.22e-06 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 49.94 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH------FQMPH-----------------KGMTTVDDF 214
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWPnnsggtlleaiiaweerKLLLTAEDV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953317075 215 FQ----GTKAALAGGTTMIIDHVVPEPEASLT------EAYEKWREWAD 253
Cdd:cd01293 95 KEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
158-230 |
6.19e-06 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 49.25 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkgmttvddffQGTKAALAGG 225
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 1953317075 226 TTMII 230
Cdd:cd00375 152 ITTMI 156
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
118-226 |
1.22e-05 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 48.35 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 118 GVEIRSATGKEVLQNLGPKDQSDR----LLIKGGRIVNDDQSFYADIYMEDGLIKQIG------------DNLIVPGGVK 181
Cdd:PRK13985 39 GEELKFGGGKTLREGMSQSNNPSKeeldLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1953317075 182 TIEANGKMVIPGGIDVHTHFQMPHKGMTTvddFFQGTKAALAGGT 226
Cdd:PRK13985 119 ALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIGGGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
142-203 |
1.36e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 48.26 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953317075 142 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQM 203
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
158-566 |
1.48e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 48.06 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQGTKAALAGGTTMI------- 229
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 230 --IDHvvPEPEASL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQNLIKdKGVNSFMVYMAYKDLYQ 300
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELAA-AGVVGFTDGQPLENLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 301 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQTRMLEMGITGpeghvlsRPEELEAEAVFRAITIASQTNCPLY 376
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 377 VTKVMSKSAADLISQARKKGnvvfgEPITAS-------LGTDGTHYWSKNWAKAaafvtsPPLSpdptTPDYINSLLA-- 447
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITASttwmhllLDTEALASYDPNLRLD------PPLG----NPSDRQALIEgv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 448 -SGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRI 526
Cdd:PRK07369 297 rTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SL 371
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1953317075 527 SVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRG 566
Cdd:PRK07369 372 APGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
158-229 |
1.90e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkgmttvddffQGTKAALAGG 225
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
....*
gi 1953317075 226 -TTMI 229
Cdd:PRK13308 156 iTTML 160
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
506-540 |
2.00e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.40 E-value: 2.00e-05
10 20 30
....*....|....*....|....*....|....*
gi 1953317075 506 VAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPD 540
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
142-201 |
2.22e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 47.49 E-value: 2.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 142 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 201
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
506-561 |
2.23e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 2.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953317075 506 VAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEG 561
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
142-218 |
2.36e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 47.19 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQMP-HKGM---TTVDDF 214
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80
|
....
gi 1953317075 215 FQGT 218
Cdd:PRK06380 81 LMKT 84
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
144-200 |
2.78e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 47.41 E-value: 2.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 144 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
141-199 |
2.84e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 47.10 E-value: 2.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953317075 141 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVIPGGIDVHT 199
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
141-581 |
7.60e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.82 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 141 RLLIKGGRIVN-----DDQsfyADIYMEDGLIKQIGDnliVPGGV---KTIEANGKMVIPGGIDVHTHFQMP-HKGMTTV 211
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgYEYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 212 DDFFQgtkAALAGGTTMII-----DHVVPEPEasLTEAYeKWREWADGKSccdyalHV-DITHWNDSVKQEVQnlikdkg 285
Cdd:PRK07627 76 ESEMA---AAVAGGVTSLVcppdtDPVLDEPG--LVEML-KFRARNLNQA------HVyPLGALTVGLKGEVL------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 286 vnsfmvymaykdlyqvsnTELYEiftcLGELGAIAQVHAENGDIIAQEQTRMLEMGIT-------------------GPE 346
Cdd:PRK07627 137 ------------------TEMVE----LTEAGCVGFSQANVPVVDTQVLLRALQYASTfgftvwlrpldaflgrggvAAS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 347 GHVLSR------PEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITASLGTDGTH------ 414
Cdd:PRK07627 195 GAVASRlglsgvPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdi 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 415 -YWSKNwakaaaFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWDK 493
Cdd:PRK07627 270 gYFDSQ------FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLKW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 494 AVATgKMDENQFVAVTSTNAAKIFNLypRKGRISVGSDSDLVIWDPDAVKIVSAKSHQSAAEYNIFEGLELRGAPLVVIC 573
Cdd:PRK07627 340 ADEA-KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLV 416
|
....*...
gi 1953317075 574 QGKIMLED 581
Cdd:PRK07627 417 AGQVAFER 424
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
158-253 |
8.53e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.31 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQ--------MPHKGMTTVDDFFQGTK---------- 219
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDktfwgdpwYPNEPGPSLRERIANERrrraasghpa 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1953317075 220 ---------AALAGGTTMIIDHVVPEPEASLT------EAYEKWREWAD 253
Cdd:PRK05985 97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
142-201 |
8.97e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 45.31 E-value: 8.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953317075 142 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVIPGGIDVHTHF 201
Cdd:PRK07203 2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
158-230 |
2.21e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 44.32 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkgmttvddffQGTKAALAGG 225
Cdd:PRK13206 89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 1953317075 226 TTMII 230
Cdd:PRK13206 158 ITTLI 162
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
158-229 |
2.33e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 44.40 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 158 ADIYMEDGLIKQIG--------DN--LIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkgmttvddffQGTKAALAGG-T 226
Cdd:PRK13207 85 ADIGIKDGRIVAIGkagnpdiqDGvdIIIGPGTEVIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 1953317075 227 TMI 229
Cdd:PRK13207 154 TMI 156
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
160-201 |
3.50e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 43.40 E-value: 3.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953317075 160 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTHF 201
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
164-200 |
3.62e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 3.62e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1953317075 164 DGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
508-587 |
9.96e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 41.99 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 508 VTSTNAAKIFNLYPrKGRISVGSDSDLVIWDPDavkivsakshqsaaeYNIFEglelrgaplvVICQGKIMLEDGNLHVT 587
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD---------------LDINS----------VIAKGQIMVRNGKLLVK 383
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
142-230 |
1.52e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 41.56 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 142 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPhkGMTTVDDFFQ 216
Cdd:PRK09059 5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90
....*....|....
gi 1953317075 217 GTKAALAGGTTMII 230
Cdd:PRK09059 83 ASRAAAAGGVTSII 96
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
493-540 |
2.34e-03 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 2.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1953317075 493 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRISVGSDSDLVIWDPD 540
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGD 340
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
158-200 |
3.39e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 40.35 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1953317075 158 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 200
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
141-201 |
7.72e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 39.45 E-value: 7.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953317075 141 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTHF 201
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PLN02303 |
PLN02303 |
urease |
156-229 |
8.92e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 39.35 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953317075 156 FYADIYMEDGLIKQIG------------DNLIVpgGVKT--IEANGKMVIPGGIDVHTHFQMPHkgmttvddffQGTKAA 221
Cdd:PLN02303 350 YKADIGIKDGLIVGIGkagnpdvmdgvtSNMIV--GVNTevIAGEGMIVTAGGIDCHVHFICPQ----------LATEAI 417
|
....*...
gi 1953317075 222 LAGGTTMI 229
Cdd:PLN02303 418 ASGITTLV 425
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
159-201 |
9.42e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.21 E-value: 9.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1953317075 159 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 201
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| |
