|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-454 |
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: 735.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 84
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQL 164
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 165 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 244
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 245 SKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTF 324
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 325 NTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 404
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907099265 405 VKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSG 454
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
5-459 |
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: 676.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 84
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQL 164
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 165 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 244
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 245 SKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTF 324
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 325 NTAQK-AVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 403
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907099265 404 SVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 459
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
4-463 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 583.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKA 83
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 84 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQ 163
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 164 LTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKV 243
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 244 MSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCT 323
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 324 FNTAQKA-VGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDP 402
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907099265 403 DSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 463
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-463 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 552.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 2 SDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGT 81
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 82 KAALAGGTTMIIDHVVPEPGtSLLAAFDQWREWADsKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDR 161
Cdd:PLN02942 84 AAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 162 FQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVT 241
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 242 KVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAH 321
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 322 CTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWD 401
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907099265 402 PDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 463
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-459 |
5.50e-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: 371.35 E-value: 5.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 6 LIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAAL 85
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 86 AGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQL 164
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 165 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEeqqRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 244
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 245 SKSAAEVIAQARKKGTVVYGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQV 316
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 317 TGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 396
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907099265 397 LVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 459
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
5-459 |
1.18e-120 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 364.40 E-value: 1.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKA 83
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 84 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRF 162
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 163 QLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTK 242
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 243 VMSKSAAEVIAQARKKGTVVYGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQ 315
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 316 VTGSAHCTFN---TAQKAVGKDN--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIS 390
Cdd:PRK13404 313 VFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907099265 391 VGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 459
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
5-457 |
5.34e-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: 216.00 E-value: 5.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 84
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVKdhGVNSFLVYMAFKD 160
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNlDQLRPLDEAGVV--GFKCFLCPSGVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 161 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 240
Cdd:cd01315 156 FPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 241 TKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNSLLSCGD 313
Cdd:cd01315 236 VHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 314 LQVTGSAH--CTfnTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISV 391
Cdd:cd01315 304 IDMVVSDHspCT--PELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAV 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907099265 392 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 457
Cdd:cd01315 382 GYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
53-431 |
5.40e-61 |
|
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: 204.93 E-value: 5.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 53 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 132
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 133 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDSQIYEVLSVIRDIGAIAQVHAEngdiiaeeqqrildlgitgpeg 210
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 211 hvlsrpeeveaeavnRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 290
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 291 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 370
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907099265 371 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSP 431
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-448 |
1.39e-52 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 185.68 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 1 MSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 80
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 81 TKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKgiqEEMEALVkDHGVNSFLVYMA 157
Cdd:PRK06189 78 SAALAAGGCTTYFD--MPlnsIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL---EHLRELA-EAGVIGFKAFMS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 158 FK--DRFQLTDSQ-IYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQT 234
Cdd:PRK06189 152 NSgtDEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 235 NCPLYVTKVMSKSAAEVIAQARKKGtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNSLLS 310
Cdd:PRK06189 232 GCPLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWRGLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 311 CGDLQVTGSAH--CTFNTAQkavgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGR 388
Cdd:PRK06189 303 AGEIDMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 389 ISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 448
Cdd:PRK06189 378 LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-460 |
5.03e-52 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 184.09 E-value: 5.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 1 MSDrLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 80
Cdd:PRK02382 1 MRD-ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 81 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT-EWhkgiqEEMEALVkDHGVNSF-LVYMA- 157
Cdd:PRK02382 78 SRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgNW-----DPLESLW-ERGVFALgEIFMAd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 158 -------FKDRFQltdsqiyEVLSVIRDIGAIAQVHAENGDIIaEEQQRILDlGITGPEGHVLSRPEEVEAEAVNRSITI 230
Cdd:PRK02382 152 stggmgiDEELFE-------EALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 231 ANQTNCPLYVTKVmskSAAEVIAQARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLL 309
Cdd:PRK02382 223 ASETGARIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 310 ScGDLQVTGSAHCTFNTAQKAVG-KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGR 388
Cdd:PRK02382 293 D-GTIDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGR 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907099265 389 ISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 460
Cdd:PRK02382 366 IAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
5-458 |
7.18e-50 |
|
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: 177.96 E-value: 7.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 84
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVkdHGVNSFLVYMAFKD 160
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNlDDLRELDEAGV--VGFKAFLSPSGDDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 161 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 240
Cdd:TIGR03178 155 FPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 241 TKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLSCGDLQV 316
Cdd:TIGR03178 235 VHLSSAEAVELITEAKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNGLIDC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 317 TGSAHCTFNTAQKAvgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 396
Cdd:TIGR03178 306 VVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907099265 397 LVIWDPDSVKTISakthNSALEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 458
Cdd:TIGR03178 383 FVFVDPDESYTLT----PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
21-444 |
6.79e-47 |
|
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: 169.16 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 21 ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVP 98
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 99 EPGTSllAAFDQWREWADSKSCCDYSLHVDITEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDSQIYE 171
Cdd:TIGR00857 83 PIDTP--ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 172 VLSVIRDIGAIAQVHAENGDIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEV 251
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 252 IAQARKkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFN 325
Cdd:TIGR00857 229 IVKAKS-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 326 TAQKAVgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSV 405
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907099265 406 KTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 444
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
53-438 |
1.06e-35 |
|
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: 137.08 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 53 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 132
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 133 hkgiQEEMEALVKdHGVNSFLVYMAfkdrfQLTDS--QIYEVLSVI-RDIGAIAQVHAENGDIIAEEQQRILDLGItgpe 209
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMG-----DSTGDllDDEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 210 gHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 287
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 288 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 364
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907099265 365 enQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQG 438
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-432 |
1.06e-32 |
|
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: 128.89 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 42 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 121
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 122 DYSLHVD-------------ITEWHKGIQ-EEMEALvKDHGVNSFlvymaFKDRFQLTDSQI-YEVLSVIRDIGAIAQVH 186
Cdd:cd01317 66 ELLKNRAkdvgivrvlpigaLTKGLKGEElTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 187 AENGDIIAEEQqrILDLGITGPEGhVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGtvvygEP 266
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 267 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 340
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 341 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYN 420
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 1907099265 421 IFEGMECRGSPL 432
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-441 |
1.23e-32 |
|
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: 128.00 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 52 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 119
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 120 CC---DYSLHVDITEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDiiAEE 196
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 197 QQRILDLGITGPEGHVLSRPEEVeaeAVNRSITIANQTNCPLYVTkvmskSAAEVIAQARKKGTVvygepitasLGTDGS 276
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 277 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 356
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 357 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSvktisakthnsaleYNIFEGMECRGSPLVVIS 436
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 1907099265 437 QGKIV 441
Cdd:pfam01979 330 KGKIV 334
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
4-444 |
1.63e-31 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 126.46 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTK 82
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 83 AALAGGTTMiidhVVPEPGT----SLLAAFDQWREWADSKSCCDysLHV--DITEWHKGIQE-EMEALvKDHGVnsflvy 155
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNTkpviDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGV------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 156 MAFK-DRFQLTDSQI-YEVLSVIRDIG-AIAQvHAE----------NGDIIAEEqqrildLGITGpeghvlsRPEEVEAE 222
Cdd:PRK09357 146 VAFSdDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslteggvmNEGEVSAR------LGLPG-------IPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 223 AVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafv 290
Cdd:PRK09357 212 MIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 291 tsPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVA 370
Cdd:PRK09357 278 --PPLRTEEDREALIEGLKD-GTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907099265 371 VTSTNAAKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 444
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-419 |
3.93e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 123.04 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 1 MSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 80
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 81 TKAALAGGTTMIIDHvvpePGTSLLAAFDqwREWADSK-SCCDYSLHVDITEWHKGIQEEMEAL--VKDHGVNSFLVYMA 157
Cdd:PRK08044 77 TRAAAKGGITTMIEM----PLNQLPATVD--RASIELKfDAAKGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 158 F-KDR-----FQ-LTDSQIYEVLSVIRDIGAIAQVHAENG---DIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRS 227
Cdd:PRK08044 151 TcGDRgidndFRdVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 228 ITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPD 303
Cdd:PRK08044 228 LYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 304 FLNSLLScGDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLy 383
Cdd:PRK08044 300 MWEKLFN-GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL- 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907099265 384 PRKGRISVGSDADLVIWDPDSvktiSAKTHNSALEY 419
Cdd:PRK08044 375 QQKGRIAPGKDADFVFIQPNS----SYVLKNEDLEY 406
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-445 |
1.18e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 118.62 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 1 MSDRLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQ 79
Cdd:PRK07575 1 MMMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 80 GTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewhkgiQEEMEALVKDHGVNSFLVYMAFK 159
Cdd:PRK07575 79 ASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 160 DRFQLTDSQiyEVLSVI--RDIGAIAqVHAENGDIIAEEQQRILdlGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCP 237
Cdd:PRK07575 153 HGPLLVDEE--AALERIfaEGTRLIA-VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 238 LYVTKVMSKSAAEVIAQArkKGTVVYGEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQV 316
Cdd:PRK07575 228 LHILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 317 TGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 396
Cdd:PRK07575 300 IATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDAD 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907099265 397 LVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDG 445
Cdd:PRK07575 375 LVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
5-455 |
1.34e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 112.71 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 84
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewHKGIQE--EMEALVKDHGVNsflVYM--AFKD 160
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 161 RFQLTDSQIYEVLSVIRDIGAiaqVHAENGDIIAEEQqrilDLGITG-PEGHVLSRPEEVEAEAVNRSITIANQTNCPLY 239
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 240 VTKVMSKSAAEVIAQARKKGTV--------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSC 311
Cdd:PRK09060 232 VLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 312 GDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISV 391
Cdd:PRK09060 297 GVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907099265 392 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 455
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
10-459 |
1.10e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.56 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 10 GKIVNDDQSFYADIYMEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGT 89
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 90 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvditewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLT 165
Cdd:PRK01211 79 TFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 166 DSQIYEVlSVIRDIGAIAQVHAENGDIIAEEQQRILDLgitgpEGHVLSRPEEVEAEAVNRSITIANQtncplyvTKVMS 245
Cdd:PRK01211 147 DIEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 246 -KSAAEVIAQARKKGT----VVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSA 320
Cdd:PRK01211 214 hVSSIDVIGRFLREVTphhlLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 321 HCTFNTAQKAvgkdNFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDADLVIW 400
Cdd:PRK01211 276 HAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAF 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907099265 401 DPDSVKTISAKTHNSALEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 459
Cdd:PRK01211 349 DFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
10-457 |
2.39e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 108.32 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 10 GKIVNDDQSFYADIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGT 89
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 90 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTDSQI 169
Cdd:PRK04250 80 TLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVDYACA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 170 YEVLSvirdigaiaqVHAENGDIIAEEqqrildlgitgPEghvlsRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAA 249
Cdd:PRK04250 158 PGIVS----------VHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 250 EVIAQARKKGTVVYGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTA 327
Cdd:PRK04250 212 KLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 328 QKAVGKdnftlipEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrISVGSDADLVIWDPDSVKT 407
Cdd:PRK04250 280 DKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWT 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907099265 408 ISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 457
Cdd:PRK04250 350 IKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PLN02795 |
PLN02795 |
allantoinase |
2-460 |
3.88e-24 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 106.01 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 2 SDRLLIKGGKIVNDdqsfyadIYMEDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFF 78
Cdd:PLN02795 50 SKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 79 QGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDITEWHKGIQE------EMEALVkDHGV 149
Cdd:PLN02795 121 TGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 150 ---NSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLgiTGPEGHVLSRPEEVEAEAVNR 226
Cdd:PLN02795 192 lglKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 227 SITIANQTN-------CPLYVTKVM-SKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA--------FV 290
Cdd:PLN02795 270 LLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 291 TSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQFVA 370
Cdd:PLN02795 338 CAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLAR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 371 VTSTNAAKVFNLyPRKGRISVGSDADLVIWDP------DSVKTISAKTHN-SAleyniFEGMECRGSPLVVISQGKIVLE 443
Cdd:PLN02795 416 WWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHKHKSlSP-----YLGTKLSGKVIATFVRGNLVFL 489
|
490
....*....|....*..
gi 1907099265 444 DGtLHVTEGSGRYIPRK 460
Cdd:PLN02795 490 EG-KHAKQACGSPILAK 505
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
3-126 |
9.35e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 82.61 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 3 DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQG 80
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907099265 81 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLH 126
Cdd:PRK09236 78 SRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFY 123
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-410 |
1.64e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 66.14 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 1 MSDRLLIKGGKIVNDDQSFY---ADIYMEDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD------- 68
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgravefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 69 --QGMTSADDFFQGT----KAALAGGTTMIIDHvvpePGTSL----------LAAFDQWREWADSKSccdyslhVDITE- 131
Cdd:COG1228 86 agGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLAAGPA-------LSLTGg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 132 WHKGIQEEMEALV---KDHGVNSFLVYMAFKDRfQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIaeeqQRILDLGITGP 208
Cdd:COG1228 155 AHARGPEEARAALrelLAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 209 EgHVLSRPEeveaeavnrsitianqtncplyvtkvmsksaaEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNWAKAAA 288
Cdd:COG1228 230 E-HGTYLDD--------------------------------EVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKAR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 289 FVtspplspDPTTPDFLNSLLSCGDLQVTGSAHctfntaqkavgkdNFTLIPEGTNGTEERMsviwdkaVVTGKMDENQ- 367
Cdd:COG1228 275 KV-------REAALANARRLHDAGVPVALGTDA-------------GVGVPPGRSLHRELAL-------AVEAGLTPEEa 327
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907099265 368 FVAVTStNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISA 410
Cdd:COG1228 328 LRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
5-455 |
2.11e-10 |
|
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: 62.70 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVndDQS----FYADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF--- 77
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrps 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 78 -FQGTKAALAG------------GTTMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DITEWHK 134
Cdd:cd01297 76 sRQGVTTVVLGncgvspapanpdDLARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 135 GI---------QEEMEALVKDH------GVNSFLVYMafkDRFQLTDSQIYEVLSVIRDIGAIAQVHaengdiIAEEQQR 199
Cdd:cd01297 155 GLdareateeeLAKMRELLREAleagalGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTH------VRYEGDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 200 ILdlgitgpeghvlsrpeeveaEAVNRSITIANQTNCPLYVT--KVMSKS-------AAEVIAQARKKGTVVYGE--PIT 268
Cdd:cd01297 226 IL--------------------EALDELLRLGRETGRPVHIShlKSAGAPnwgkidrLLALIEAARAEGLQVTADvyPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 269 ASLGTDgshywsknwakAAAFVTSPPlspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEE 348
Cdd:cd01297 286 AGSEDD-----------VRRIMAHPV-------------VMGGSDGGALGKPHP-------------------RSYGDFT 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 349 RMSVIWdkAVVTGKMDENQFVAVTSTNAAKVFNLYPRkGRISVGSDADLVIWDPDSVK---TISAKTHNSaleynifEGM 425
Cdd:cd01297 323 RVLGHY--VRERKLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGI 392
|
490 500 510
....*....|....*....|....*....|
gi 1907099265 426 EcrgspLVVISqGKIVLEDGtLHVTEGSGR 455
Cdd:cd01297 393 E-----AVLVN-GVPVVRDG-AFTGARPGR 415
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
54-454 |
8.79e-10 |
|
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: 60.54 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 54 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT--E 131
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 132 WHKGIQeemealVKDHGVNS-FLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAqVHAENGDIIAeeqqrILDLgitgpeg 210
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 211 hvlsrpeeveAEAVNRSITIANqtncplyvtkVMSKSAAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 290
Cdd:cd01316 144 ----------ASLHNRSIHICH----------VSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 291 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 370
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 371 VTSTNAAKVFNLYPrkgrisvgsDADLVI-WDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 449
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 1907099265 450 TEGSG 454
Cdd:cd01316 340 PPGFG 344
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-447 |
9.57e-10 |
|
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: 60.68 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQS---FYADIYMEDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM------------- 66
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 67 --------PDQGMTSADDFFQGTKAALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKscc 121
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEET--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 122 dyslhvditewhKGIQEEMEALVKD-HGVNSFLVYMAFKDR--FQLTDSQIYEVLSVIRDIGAIAQVH-AENGDIIAEEQ 197
Cdd:cd01298 158 ------------EEALAEAERLIREwHGAADGRIRVALAPHapYTCSDELLREVAELAREYGVPLHIHlAETEDEVEESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 198 QR--------ILDLGITGPE---GH-VLSRPEEVEAEAvNRSITIAnqtNCPlyvTKVMsKSAAEV--IAQARKKGtvvy 263
Cdd:cd01298 226 EKygkrpveyLEELGLLGPDvvlAHcVWLTDEEIELLA-ETGTGVA---HNP---ASNM-KLASGIapVPEMLEAG---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 264 gepITASLGTDGShywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAVGKDNFTLIPEg 342
Cdd:cd01298 294 ---VNVGLGTDGA---------------------------------ASNNnLDMFEEMRLAALL-QKLAHGDPTALPAE- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 343 tngteermsviwdkavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNif 422
Cdd:cd01298 336 ------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS-- 388
|
490 500
....*....|....*....|....*..
gi 1907099265 423 egmeCRGSP--LVVISqGKIVLEDGTL 447
Cdd:cd01298 389 ----ANGGDvdTVIVN-GRVVMEDGEL 410
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
23-443 |
3.56e-08 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 55.86 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 23 IYMEDGLIKQIGENLivpGGVKTIEAHSRMVIPGGIDVHTRfqMPDQGMtSADDFFQGTKAALAGGttmiIDHVVPEPGT 102
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS--LKNDSL-SSKNLKSLENECLKGG----VGSIVLYPDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 103 SllaafdqwrewadsKSCCD-YSLhvditEWHKGIQEEMEalvkdhgVNSFLVYMAFKDRFQLTDsqiyevLSVIRDIGA 181
Cdd:PRK08417 71 T--------------PAIDNeIAL-----ELINSAQRELP-------MQIFPSIRALDEDGKLSN------IATLLKKGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 182 IAqVHAE---NGDI---IAEEQQR------------------ILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCP 237
Cdd:PRK08417 119 KA-LELSsdlDANLlkvIAQYAKMldvpifcrcedssfddsgVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 238 LYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHywSKNWAKAAAFvtSPPLSpDPTTPDFLNSLLSCGDLQVT 317
Cdd:PRK08417 198 VLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKEGKIDFL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 318 GSAHC-TFNTAQKAVgkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDAD 396
Cdd:PRK08417 273 TSLHSaKSNSKKDLA----FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEAD 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907099265 397 LVIWDPDSVKTISAKthnsaleYNIFEGMECRGSPLVVISQGKIVLE 443
Cdd:PRK08417 347 LVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-403 |
2.26e-07 |
|
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: 52.97 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTrfqmpdqgmtsaddffQGtkaa 84
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI----------------HG---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 85 lAGGttmiidhvvpepgtsllAAFDQWRewadsksccdyslhvditewHKGIQEEMEALVKdHGVNSFLVYMafkdrfqL 164
Cdd:cd00854 61 -GGG-----------------ADFMDGT--------------------AEALKTIAEALAK-HGTTSFLPTT-------V 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 165 TDS--QIYEVLSVIRD-----IGA-IAQVHAEnGDIIAEEQqrildlgiTG--PEGHVLS-RPEEVE-----AEAVNRSI 228
Cdd:cd00854 95 TAPpeEIAKALAAIAEaiaegQGAeILGIHLE-GPFISPEK--------KGahPPEYLRApDPEELKkwleaAGGLIKLV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 229 TIANQTncplyvtkvmsKSAAEVIAQARKKGtvvygepITASLG-TDGSHYWSKNWAKAAA-FVTS-----PPLS---PD 298
Cdd:cd00854 166 TLAPEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVTHlfnamSPLHhrePG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 299 PTTPDFLNSLLSCG---DLQvtgsaHC---TFNTAQKAVGKDNFTLI---------PEGT---NGTEERM---------- 350
Cdd:cd00854 228 VVGAALSDDDVYAEliaDGI-----HVhpaAVRLAYRAKGADKIVLVtdamaaaglPDGEyelGGQTVTVkdgvarladg 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907099265 351 ----SVI-WDKAVVT----GKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 403
Cdd:cd00854 303 tlagSTLtMDQAVRNmvkwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-208 |
3.32e-07 |
|
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: 52.91 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIV--NDDQSFYAD--IYMEDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSAD 75
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 76 DFFQ--------------------GTKAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDY 123
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 124 SLHVDITEWHKGIQEEMEALVKD-HGVNSFLVYMAFKDRF--QLTDSQIYEVLSVIRDIGAIAQVH-----AENGDIIAE 195
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADGRIRVALAPHApyTVSPELLRAAAALARELGLPLHTHlaetrDEVEWVLEL 235
|
250
....*....|....*..
gi 1907099265 196 EQQRILD----LGITGP 208
Cdd:COG0402 236 YGKRPVEyldeLGLLGP 252
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
21-412 |
8.17e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 51.53 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 21 ADIYMEDGLIKQIGENLI-VPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTM--IIDHVV 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 98 P---EPGTslLAAFDQ---------WREWAD-SKSCCDYSLhvdiTEWhkgiQEEMEAlvkdhGVNSFlvymafkdrfql 164
Cdd:PRK07369 100 PpldNPAT--LARLQQqaqqippvqLHFWGAlTLGGQGKQL----TEL----AELAAA-----GVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 165 TDSQIYEVLSVIRDIGAIAQVH-------------AENGdiIAEEQQRILDLGITGpeghvlsRPEEVEAEAVNRSITIA 231
Cdd:PRK07369 153 TDGQPLENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 232 NQTNCPLYVTKVMSKSAAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPLsPDPTTPD 303
Cdd:PRK07369 224 AAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPL-GNPSDRQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 304 FLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLY 383
Cdd:PRK07369 291 ALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQE 367
|
410 420
....*....|....*....|....*....
gi 1907099265 384 PRkgRISVGSDADLVIWDPDSVKTISAKT 412
Cdd:PRK07369 368 PP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
369-403 |
8.22e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.25 E-value: 8.22e-07
10 20 30
....*....|....*....|....*....|....*
gi 1907099265 369 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 403
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-77 |
1.22e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.00 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT--------RFQMP------- 67
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVhvypgstpYGDEPdevgvrs 80
|
90
....*....|....*.
gi 1907099265 68 ------DQGMTSADDF 77
Cdd:PRK09237 81 gvttvvDAGSAGADNF 96
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-62 |
3.90e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.25 E-value: 3.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907099265 6 LIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENliVPGGVKTIEAHSRMVIPGGIDVHT 62
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
4-462 |
4.79e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 46.23 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTrfqmpdQGMTSADDFFQgt 81
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHA------HGQSVAAYRMQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 82 kaALAGGTTMIidhvVPEPGTSLLAAFdqWREWADSKSCCDYSLHVDiteWHKGIQEEMEALVKDHGVNSFLVYMaFKDR 161
Cdd:PRK09061 90 --AFDGVTTAL----ELEAGVLPVARW--YAEQAGEGRPLNYGASVG---WTPARIAVLTGPQAEGTIADFGKAL-GDPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 162 FQ---LTDSQIYEVLSVIR---DIGAIAqVHAENGDIIAEEQQRILDLG-ITGPEG-----HV--LSRPE-EVEAEAVNR 226
Cdd:PRK09061 158 WQeraATPAELAEILELLEqglDEGALG-IGIGAGYAPGTGHKEYLELArLAARAGvptytHVryLSNVDpRSSVDAYQE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 227 SITIANQTNCPLYVTKVMSKS------AAEVIAQARKKGTVV------YGEPITAsLGTD----------GSHYWSKNW- 283
Cdd:PRK09061 237 LIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVtteaypYGAGSTV-VGAAffdpgwlermGLGYGSLQWv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 284 ---------AKAAAFVTSPPLSP---------DPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEG--- 342
Cdd:PRK09061 316 etgerlltrEELAKLRANDPGGLvlihfldedNPRDRALLDRSVLFPGAAIASDAMPWTWSDGTVYEGDAWPLPEDAvsh 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 343 --TNGT---------EERMSVIWDKAVvtGKMdenqfvavtSTNAAKVFNLY----PRKGRISVGSDADLVIWDPDSVK- 406
Cdd:PRK09061 396 prSAGTfarflreyvRERKALSLLEAI--RKC---------TLMPAQILEDSvpamRRKGRLQAGADADIVVFDPETITd 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907099265 407 --TISAKTHNSaleynifEGMEcrgsplVVISQGKIVLEDGTLHVTEGSGRYIpRKPF 462
Cdd:PRK09061 465 raTFEDPNRPS-------EGVR------HVLVNGVPVVSNGELVRDARPGRPV-RRPV 508
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
369-424 |
6.59e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.60 E-value: 6.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907099265 369 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEG 424
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
4-101 |
8.68e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.05 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIVN-----DDQsfyADIYMEDGLIKQIGEnliVPGGV---KTIEAHSRMVIPGGIDVHTRFQMPdqGMTSAD 75
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110
....*....|....*....|....*....|.
gi 1907099265 76 DFFQGTKAALAGGTTMII-----DHVVPEPG 101
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPG 104
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
5-62 |
1.44e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.41 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907099265 5 LLIKGGKI------VNDDQsfyADIYMEDGlikQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 62
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-91 |
2.35e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.63 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 4 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvkTIEAHSRMVIPGGIDVHT----RFQMP--------DQGM 71
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100
....*....|....*....|
gi 1907099265 72 TSADdffqgTKAALAGGTTM 91
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV 95
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
371-411 |
3.25e-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: 43.15 E-value: 3.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907099265 371 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPD-SVKTISAK 411
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
344-404 |
3.51e-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: 43.02 E-value: 3.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907099265 344 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 404
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
7-89 |
3.73e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 43.35 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 7 IKGGKIVNDDQSFYADiyMEDGlikqIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSaddFFQGTKAALA 86
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 1907099265 87 GGT 89
Cdd:PRK13985 158 GGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-66 |
4.62e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 42.87 E-value: 4.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907099265 5 LLIKGGKIVNDD--QSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQM 66
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-100 |
6.90e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.30 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 3 DRLLIKGGKIVNDDQSF----YADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVH-------TRFQMPD--- 68
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvLRGIGADwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907099265 69 -----------QGMTSADDFFQGTKA----ALAGGTTMIID--HVVPEP 100
Cdd:PRK08204 81 qtyfreihgnlGPMFRPEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
21-93 |
1.64e-03 |
|
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: 41.16 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 21 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 88
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQ-----------IEEALASG 151
|
....*
gi 1907099265 89 TTMII 93
Cdd:cd00375 152 ITTMI 156
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-62 |
2.36e-03 |
|
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: 40.31 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907099265 21 ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 62
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHI 56
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
318-401 |
2.44e-03 |
|
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: 40.39 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 318 GSAHCTFNTAQKAVGKDnftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKG 387
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIG 300
|
90
....*....|....
gi 1907099265 388 RISVGSDADLVIWD 401
Cdd:cd01307 301 TLAVGYDADLTVFD 314
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
371-455 |
2.58e-03 |
|
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: 40.47 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 371 VTSTNAAKVFNLyPRKGRISVGSDADLVIW--DPDSVKTISAKTHNSALEYnifegmecrgsPLVVISQGKIVLEDGTLh 448
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDPSDYEKVEKAFSR-----------AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 1907099265 449 VTEGSGR 455
Cdd:cd01304 502 VAEPWGR 508
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-403 |
2.79e-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: 39.99 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 27 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 85
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 86 AGGTTmiidHVVPEPGTSLLAAfdqwREWADSKSccdyslhvditewhKGIQEEMEALVKDHGVNSFLVYMAFK--DRFQ 163
Cdd:cd01309 81 AGGVT----TVQVLPGSANLIG----GQGVVIKT--------------DGGTIEDMFIKAPAGLKMALGENPKRvyGGKG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 164 LTDSQIYEVLSVIRDIGAIAQvhaengdiiaeEQQRILDLGITGPEGHVLSRPE-EVEAEAVNRSITIanqtncplyvtK 242
Cdd:cd01309 139 KEPATRMGVAALLRDAFIKAQ-----------EYGRKYDLGKNAKKDPPERDLKlEALLPVLKGEIPV-----------R 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 243 VMSKSAAE---VIAQARKkgtvvYGEPITASLGTDGsHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLlscgdlqvtgs 319
Cdd:cd01309 197 IHAHRADDiltAIRIAKE-----FGIKITIEHGAEG-YKLADELAKHGIPVIYGPTLTLPKKVEEVNDA----------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 320 ahcTFNTAQ-KAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTStNAAKVFNLYPRKGRISVGSDADLV 398
Cdd:cd01309 260 ---IDTNAYlLKKGGVAFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLV 335
|
....*
gi 1907099265 399 IWDPD 403
Cdd:cd01309 336 VWNGD 340
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
5-94 |
3.33e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.08 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 5 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGEnlIVPGGVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDFfqgTK 82
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI---ESSMVTPAEF---AR 78
|
90
....*....|...
gi 1907099265 83 AALAGGTT-MIID 94
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
21-92 |
3.61e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 21 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 88
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALASG 155
|
....*
gi 1907099265 89 -TTMI 92
Cdd:PRK13308 156 iTTML 160
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
376-461 |
3.81e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 40.16 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907099265 376 AAKVFNLYPRkGRISVGSDADLVIWDPDSVKtiSAKTHNSALEYNifEGMECrgsplVVISqGKIVLEDGTlHVTEGSGR 455
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-----VIVN-GVVVVEDGK-PTGARPGR 520
|
....*.
gi 1907099265 456 YIPRKP 461
Cdd:COG3653 521 VLRGGG 526
|
|
| |
