|
Name |
Accession |
Description |
Interval |
E-value |
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
6-445 |
0e+00 |
|
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: 572.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVdtSATAADLTGVRTVQlADDEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAI--GPDIANTEAEEVID-AGGLVVMPGLIDTHVHINEPGRTEWEGFETGTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHEAGVSGFKCFLLHSGVDEFP 165
Cdd:cd01315 78 AAAAGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGVDEFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 166 PLDAEELKPVMREIGSFDGLLIVHAEDAHTIDH----APAAAGGTYEKFLNSRPREAENLAIEKVIELSRRTGCRVHILH 241
Cdd:cd01315 158 AVDDEQLEEAMKELAKTGSVLAVHAENPEITEAlqeqAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 242 VSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPD 321
Cdd:cd01315 238 LSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 322 LKALDTGDFGVAWGGISSLQLGLSAVWTGARE-RGFALADVVRWMSQATARHAGL-ARKGSIAVGHDADLCVFAPDDSYV 399
Cdd:cd01315 318 LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNkRGLSLEDIARLMCENPAKLFGLsHQKGRIAVGYDADFVVWDPEEEFT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1906352648 400 VDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI--DIEAA--PQGRLLT 445
Cdd:cd01315 398 VDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVyqDGEVVgePLGQLLL 447
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
6-444 |
0e+00 |
|
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: 551.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVdtsaTAADLTGVRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAI----GPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHEAGVSGFKCFLLHSGVDEFP 165
Cdd:TIGR03178 77 AAAAGGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLSPSGDDEFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 166 PLDAEELKPVMREIGSFDGLLIVHAEDAHTIDH----APAAAGGTYEKFLNSRPREAENLAIEKVIELSRRTGCRVHILH 241
Cdd:TIGR03178 157 HVDDWQLYKGMRELARLGQLLLVHAENPAITSAlgeeAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 242 VSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPD 321
Cdd:TIGR03178 237 LSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 322 LKAldTGDFGVAWGGISSLQLGLSAVWT-GARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYVV 400
Cdd:TIGR03178 317 LKR--AGDFFKAWGGIAGLQSTLDVMFDeAVQKRGLPLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPDESYTL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1906352648 401 DAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKID----IEAAPQGRLL 444
Cdd:TIGR03178 395 TPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYddeqFIGAPKGQLL 442
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-446 |
5.68e-166 |
|
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: 474.19 E-value: 5.68e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 8 VIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADltGVRTVQlADDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAA 87
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPE--AAEVID-ATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 88 AAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPG---NLADLRPLHEAGVSGFKCFLLHSGVDef 164
Cdd:COG0044 78 AAGGVTTVVDMP-NTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlgeNLAELGALAEAGAVAFKVFMGSDDGN-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 165 PPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAAGGT-YEKFLNSRPREAENLAIEKVIELSRRTGCRVHILHVS 243
Cdd:COG0044 155 PVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTsPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 244 SADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDLK 323
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 324 AldtGDFGVAWGGISSLQLGLSAVWT-GARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYVVDA 402
Cdd:COG0044 315 E---LPFAEAPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDAEWTVTA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1906352648 403 ASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI----DIEAAPQGRLLTR 446
Cdd:COG0044 392 EDLHSKSKNTPFEGRELTGRVVATIVRGRVVyedgEVVGEPRGRFLRR 439
|
|
| PLN02795 |
PLN02795 |
allantoinase |
8-444 |
2.27e-154 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 447.30 E-value: 2.27e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 8 VIRAARMVTPDGETAGAVGIRDGEIVAVdTSATAADLTGVRtVQLAD--DEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:PLN02795 47 VLYSKRVVTPAGVIPGAVEVEGGRIVSV-TKEEEAPKSQKK-PHVLDygNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLAD---LRPLHEAGVSGFKCFLLHSGVD 162
Cdd:PLN02795 125 AAAAGGITTLVDMPLNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNasvLEELLDAGALGLKSFMCPSGIN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 163 EFPPLDAEELKPVMREIGSFDGLLIVHAE--DAHTIDHAPAAAGGTYEKFLNSRPREAENLAIEKVIELSRRT------- 233
Cdd:PLN02795 205 DFPMTTATHIKAALPVLAKYGRPLLVHAEvvSPVESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTrpggvae 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 234 GCRVHILHVSSA-DVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVV 312
Cdd:PLN02795 285 GAHVHIVHLSDAeSSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 313 TDHSPSTPDLKALDTGDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVF 392
Cdd:PLN02795 365 SDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTLEQLARWWSERPAKLAGLDSKGAIAPGKDADIVVW 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906352648 393 APDDSYVVDAAS-LHHKN-AVTPYHGRTLAGVVRQTWLRGEKIDIE----AAPQGRLL 444
Cdd:PLN02795 445 DPEAEFVLDESYpIYHKHkSLSPYLGTKLSGKVIATFVRGNLVFLEgkhaKQACGSPI 502
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
5-450 |
4.02e-141 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 411.79 E-value: 4.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 5 LDVVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADltgvRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASAT 84
Cdd:PRK06189 3 YDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA----REIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHEAGVSGFKCFLLHSGVDEF 164
Cdd:PRK06189 79 AALAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVIGFKAFMSNSGTDEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 165 PPLDAEELKPVMREIGSFDGLLIVHAE-DAHT--IDHAPAAAGGTYEK-FLNSRPREAENLAIEKVIELSRRTGCRVHIL 240
Cdd:PRK06189 159 RSSDDLTLYEGMKEIAALGKILALHAEsDALTrhLTTQARQQGKTDVRdYLESRPVVAELEAVQRALLYAQETGCPLHFV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 241 HVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTP 320
Cdd:PRK06189 239 HISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 321 DLKALDtgDFGVAWGGISSLQLGLSAVWT-GARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYV 399
Cdd:PRK06189 319 ELKEGD--DFFLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDETYT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1906352648 400 VDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI----DIEAAPQGRLLTREGAR 450
Cdd:PRK06189 397 LTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVyqdgEVFPPPRGQLLRPSVVK 451
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
6-444 |
2.93e-106 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 322.58 E-value: 2.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVdtsatAADLTGVRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:PRK08044 4 DLIIKNGTVILENEARVVDIAVKGGKIAAI-----GQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHEAGVSGFKCFLLHSG----V 161
Cdd:PRK08044 79 AAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGdrgiD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 162 DEFPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAAGG----TYEKFLNSRPREAENLAIEKVIELSRRTGCRV 237
Cdd:PRK08044 159 NDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKRegrvTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 238 HILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSP 317
Cdd:PRK08044 239 HVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 318 STPDLKAldtGDFGVAWGGISSLQLGLSAVW-TGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDD 396
Cdd:PRK08044 319 CPPEMKA---GNIMEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1906352648 397 SYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI-DIEA----APQGRLL 444
Cdd:PRK08044 396 SYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIyDIEQgfpvAPKGQFI 448
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
53-426 |
2.29e-81 |
|
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: 256.01 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 53 ADDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGG 132
Cdd:cd01317 7 AEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMP-NTNPVIDNPAVVELLKNRAKDVGIVRVLPIGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 133 AVPGN----LADLRPLHEAGVSGFkcfllhsGVDEFPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAAGGTYE 208
Cdd:cd01317 86 LTKGLkgeeLTEIGELLEAGAVGF-------SDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 209 KF-LNSRPREAENLAIEKVIELSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCC 287
Cdd:cd01317 159 RLgLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 288 PPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDLKALdtgDFGVAWGGISSLQLGLSAVWTGARERGFA-LADVVRWMS 366
Cdd:cd01317 239 PPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDL---PFAEAPPGIIGLETALPLLWTLLVKGGLLtLPDLIRALS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 367 QATARHAGLaRKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQT 426
Cdd:cd01317 316 TNPAKILGL-PPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
55-430 |
1.68e-78 |
|
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: 248.02 E-value: 1.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 55 DEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGaV 134
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMP-NTKPPTTTAEALYEKLRLAAAKSVVDYGLYFG-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 135 PGNlADLRPLHEAGVSGFKCFLLHSGVDEFPPLDAEElkpvmREIGSFDGLLIVHAEDAHTIDHAPAAAGGTYEKFLnSR 214
Cdd:cd01318 79 TGS-EDLEELDKAPPAGYKIFMGDSTGDLLDDEETLE-----RIFAEGSVLVTFHAEDEDRLRENRKELKGESAHPR-IR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 215 PREAENLAIEKVIELSRRTGCRVHILHVSSADvlaTLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGA 294
Cdd:cd01318 152 DAEAAAVATARALKLARRHGARLHICHVSTPE---ELKLIKKAKPGVTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRSRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 295 NREQLWEGLRDGVIDMVVTDHSPSTPDLKALDTGDfgvAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAG 374
Cdd:cd01318 229 DRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFG 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906352648 375 LARKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRG 430
Cdd:cd01318 306 IKNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
7-431 |
8.12e-76 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 243.18 E-value: 8.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGE-TAGAVGIRDGEIVAVdtsATAADLTGVRTVQlADDEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAI---GENIEAEGAEVID-ATGLVVAPGLVDLHVHLREPGQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVgFWGGAVPGN-----LADLRPLHEAGVSGFkcfllhsG 160
Cdd:PRK09357 79 AAAAGGFTTVVAMP-NTKPVIDTPEVVEYVLDRAKEAGLVDV-LPVGAITKGlageeLTEFGALKEAGVVAF-------S 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 161 VDEFPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAAGGTYEKF-LNSRPREAENLAIEKVIELSRRTGCRVHI 239
Cdd:PRK09357 150 DDGIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLgLPGIPAVAEEVMIARDVLLAEATGARVHI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 240 LHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPST 319
Cdd:PRK09357 230 CHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 320 PDLKAldtGDFGVAWGGISSLQLGLSAVWTGARERG-FALADVVRWMSQATARHAGLARkGSIAVGHDADLCVFAPDDSY 398
Cdd:PRK09357 310 REEKE---CEFEAAPFGITGLETALSLLYTTLVKTGlLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVIFDPEAEW 385
|
410 420 430
....*....|....*....|....*....|...
gi 1906352648 399 VVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGE 431
Cdd:PRK09357 386 TVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGK 418
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
9-421 |
8.85e-76 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 243.43 E-value: 8.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 9 IRAARMVTPDGET-AGAVGIRDGEIVAVDTSATAADLTgvrTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAA 87
Cdd:PRK07575 7 IRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVD---TVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 88 AAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHeaGVSGFKCFLLHSG----VDE 163
Cdd:PRK07575 84 AKGGVTSFLEMP-NTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTAN--PTCGIKIFMGSSHgpllVDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 164 fppldAEELKPVMREiGSFdgLLIVHAEDAHTIDHAPAAAGGTYEKFLNSRPR--EAENLAIEKVIELSRRTGCRVHILH 241
Cdd:PRK07575 161 -----EAALERIFAE-GTR--LIAVHAEDQARIRARRAEFAGISDPADHSQIQdeEAALLATRLALKLSKKYQRRLHILH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 242 VSSADVLATLataRRD-GVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTP 320
Cdd:PRK07575 233 LSTAIEAELL---RQDkPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 321 DLKALD-----TGDFGVAwggiSSLQLGLsavwTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPD 395
Cdd:PRK07575 310 EEKAQPypnspSGMPGVE----TSLPLML----TAAMRGKCTVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDLN 381
|
410 420
....*....|....*....|....*.
gi 1906352648 396 DSYVVDAASLHHKNAVTPYHGRTLAG 421
Cdd:PRK07575 382 TYRPVRREELLTKCGWSPFEGWNLTG 407
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-431 |
1.00e-72 |
|
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: 234.64 E-value: 1.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 20 ETAGAVGIRDGEIVAVDTSATAADLTgvrtVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMP 99
Cdd:TIGR00857 3 ETEVDILVEGGRIKKIGKLRIPPDAE----VIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 100 lNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGN----LADLRPLHEAGVSGFKCFllhsgVDEFPPLDAEELKPV 175
Cdd:TIGR00857 79 -NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNqgkeLTEAYELKEAGAVGRMFT-----DDGSEVQDILSMRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 176 MrEIGSFDGLLIV-HAEDAHTIDHAPAAAG-GTYEKFLNSRPREAENLAIEKVIELSRRTGCRVHILHVSSADVLATLAT 253
Cdd:TIGR00857 153 L-EYAAIAGVPIAlHAEDPDLIYGGVMHEGpSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 254 ARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDLKaldTGDFGVA 333
Cdd:TIGR00857 232 AKSQGIKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEK---TKEFAAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 334 WGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTP 413
Cdd:TIGR00857 309 PPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTP 388
|
410
....*....|....*...
gi 1906352648 414 YHGRTLAGVVRQTWLRGE 431
Cdd:TIGR00857 389 FEGMSLKGKPIATILRGK 406
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-426 |
7.44e-72 |
|
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: 229.97 E-value: 7.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 57 VLLPGVVDAHVHVNDPGRTEWEG-FASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVP 135
Cdd:cd01302 2 LVLPGFIDIHVHLRDPGGTTYKEdFESGSRAAAAGGVTTVIDMP-NTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 136 GNLAD-LRPLHEAGVSGFKCFLLHSGVDEFPPLDAEeLKPVMREIGSFDGLLIVHAEdahtidhapaaaggtyekflnsr 214
Cdd:cd01302 81 GDVTDeLKKLFDAGINSLKVFMNYYFGELFDVDDGT-LMRTFLEIASRGGPVMVHAE----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 215 preaenlaieKVIELSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGA 294
Cdd:cd01302 137 ----------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRSKE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 295 NREQLWEGLRDGVIDMVVTDHSPSTPDLKALdTGDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAG 374
Cdd:cd01302 207 DREALWEGVKNGKIDTIASDHAPHSKEEKES-GKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFG 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1906352648 375 LARKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQT 426
Cdd:cd01302 286 LYPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
6-448 |
1.34e-70 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 230.31 E-value: 1.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADltgVRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASATR 85
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSS---SEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 86 AAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGaVPGNLADLRPLHEAGVSGF-KCFLLHSGVDEf 164
Cdd:PRK02382 80 SAAAGGVTTVVDQP-NTDPPTVDGESFDEKAELAARKSIVDFGINGG-VTGNWDPLESLWERGVFALgEIFMADSTGGM- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 165 pPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHA--PAAAGGTYEKFLNSRPREAENLAIEKVIELSRRTGCRVHILHV 242
Cdd:PRK02382 157 -GIDEELFEEALAEAARLGVLATVHAEDEDLFDELakLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 243 SSADvlaTLATARRDGvrVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDL 322
Cdd:PRK02382 236 STPE---GVDAARREG--ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 323 KALDTGDfgvAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYVVDA 402
Cdd:PRK02382 311 KDADIWD---APSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAAREIRG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1906352648 403 ASLHHKNAVTPYHGRTlaGVVRQ-TWLRGEKI----DIEAAP-QGRLLTREG 448
Cdd:PRK02382 388 DDLHSKAGWTPFEGME--GVFPElTMVRGTVVwdgdDINAKRgRGEFLRGRG 437
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-433 |
1.53e-70 |
|
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: 230.18 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGETAGAVGIRDGEIVAVdtSATAADLTGVRTVQlADDEVLLPGVVDAHVHVNDP--GRTEWEGFASAT 84
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAI--GPNLEAPGGVEVID-ATGKYVLPGGIDPHTHLELPfmGTVTADDFESGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVDMplnSIP-PTCDVV-ALDLKRKTAASQALVDVGF------WGGAVpgnLADLRPLHEAGVSGFKCFL 156
Cdd:cd01314 78 RAAAAGGTTTIIDF---AIPnKGQSLLeAVEKWRGKADGKSVIDYGFhmiitdWTDSV---IEELPELVKKGISSFKVFM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 157 LHSGVDEfppLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPA---AAGGT-YEKFLNSRPREAENLAIEKVIELSRR 232
Cdd:cd01314 152 AYKGLLM---VDDEELLDVLKRAKELGALVMVHAENGDVIAELQKkllAQGKTgPEYHALSRPPEVEAEATARAIRLAEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 233 TGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEI----PDGAtQFKCCPPIREGANREQLWEGLRDGVI 308
Cdd:cd01314 229 AGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYwkdwFEGA-KYVCSPPLRPKEDQEALWDGLSSGTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 309 DMVVTDHSPSTPDLKALDTGDFGVAWGGISSLQLGLSAVWTGARERG-FALADVVRWMSQATARHAGL-ARKGSIAVGHD 386
Cdd:cd01314 308 QTVGSDHCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGrITLEKFVELTSTNPAKIFGLyPRKGTIAVGSD 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1906352648 387 ADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI 433
Cdd:cd01314 388 ADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVV 434
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
5-449 |
3.18e-64 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 213.88 E-value: 3.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 5 LDVVIRAARMVTPDGETAGAVGIRDGEIVAV--DTSATAADLTGvrtvqladdEVLLPGVVDAHVHVNDP--GRTEWEGF 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIgaNLGDEVIDATG---------KYVMPGGIDPHTHMEMPfgGTVSSDDF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 81 ASATRAAAAGGVTTIVDMPLNsiPPTCDVV-ALDLKRKTAASQALVDVGF------WGGAVpgnLADLRPLHEAGVSGFK 153
Cdd:PRK08323 72 ETGTRAAACGGTTTIIDFALQ--PKGQSLReALEAWHGKAAGKAVIDYGFhmiitdWNEVV---LDEMPELVEEGITSFK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 154 CFLLHSGVDEfppLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPA---AAGGTYEKF--LnSRPREAENLAIEKVIE 228
Cdd:PRK08323 147 LFMAYKGALM---LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAkllAEGKTGPEYhaL-SRPPEVEGEATNRAIM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 229 LSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEI--PDG--ATQFKCCPPIREGANREQLWEGLR 304
Cdd:PRK08323 223 LAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYdgPDWfeGAKYVMSPPLRDKEHQDALWRGLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 305 DGVIDMVVTDHSP-STPDLKALDTGDFGVAWGGISSLQLGLSAVWTGARERG-FALADVVRWMSQATARHAGL-ARKGSI 381
Cdd:PRK08323 303 DGDLQVVATDHCPfCFEQKKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGrITLNRFVELTSTNPAKIFGLyPRKGTI 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906352648 382 AVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKIdieaAPQGRLLTREGA 449
Cdd:PRK08323 383 AVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVV----VEDGEFRGKAGH 446
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-433 |
5.93e-60 |
|
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: 202.62 E-value: 5.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADltGVRTVQlADDEVLLPGVVDAHVHVNDP--GRTEWEGFASAT 84
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPD--AVEVID-ATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVDMPLNsiPPTCDVV-ALDLKRKTAASQALVDVGF------WGGAVpgnLADLRP-LHEAGVSGFKCFL 156
Cdd:TIGR02033 78 KAAAAGGTTTIIDFVVP--EKGSSLTeALETWHEKAEGKSVIDYGFhmdithWNDSV---LEEHIPeVKEEGINSFKVFM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 157 LHSGVDEfppLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPA---AAGGTYEKFLN-SRPREAENLAIEKVIELSRR 232
Cdd:TIGR02033 153 AYKNLLM---VDDEELFEILKRLKELGALLQVHAENGDIIAELQArmlAQGITGPEYHAlSRPPELEAEAVARAITLAAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 233 TGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYL--TFAAEEIPDG-ATQFKCCPPIREGANREQLWEGLRDGVID 309
Cdd:TIGR02033 230 ADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLvlDDTHYDKPGFeGAKYVCSPPLREPEDQDALWSALSSGALQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 310 MVVTDHSP-STPDLKALDTGDFGVAWGGISSLQLGLSAVWTGARERG-FALADVVRWMSQATARHAGL-ARKGSIAVGHD 386
Cdd:TIGR02033 310 TVGSDHCTfNFAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGrITLEKFVEVTSTNPAKIFNLyPRKGTIAVGSD 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1906352648 387 ADLCVFAPDDSYVVdAASLHHKNA-VTPYHGRTLAGVVRQTWLRGEKI 433
Cdd:TIGR02033 390 ADIVIWDPNRTTVI-SAETHHSNAdYNPFEGFKVRGAPVSVLSRGRVV 436
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-445 |
9.81e-58 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 196.29 E-value: 9.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 1 MSRDLDVVIRAARMVTPDGETAGAVGIRDGEIVAVD--TSATAA---DLTGVRtvqladdevLLPGVVDAHVHVNDPGRT 75
Cdd:PRK09060 1 MTQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGdlSGASAGeviDCRGLH---------VLPGVIDSQVHFREPGLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 76 EWEGFASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPL-HEAGVSGFKC 154
Cdd:PRK09060 72 HKEDLETGSRAAVLGGVTAVFEMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELeRLPGCAGIKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 155 FLLHSG----VDefpplDAEELKPVMREIGSfdgLLIVHAED-AHTIDHAPAAAGGTYEKFLNSRPREAENLAIEKVIEL 229
Cdd:PRK09060 151 FMGSSTgdllVE-----DDEGLRRILRNGRR---RAAFHSEDeYRLRERKGLRVEGDPSSHPVWRDEEAALLATRRLVRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 230 SRRTGCRVHILHVSSADVLATLATARRdgvRVTAETCPHYLTFAAEEIPDG-ATQFKCCPPIREGANREQLWEGLRDGVI 308
Cdd:PRK09060 223 ARETGRRIHVLHVSTAEEIDFLADHKD---VATVEVTPHHLTLAAPECYERlGTLAQMNPPIRDARHRDGLWRGVRQGVV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 309 DMVVTDHSPSTPDLKALD-----TGDFGVAwggiSSLQLGLSAVWTGArergFALADVVRWMSQATARHAGLARKGSIAV 383
Cdd:PRK09060 300 DVLGSDHAPHTLEEKAKPypaspSGMTGVQ----TLVPIMLDHVNAGR----LSLERFVDLTSAGPARIFGIAGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906352648 384 GHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI----DIEAAPQGRLLT 445
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVmwdgELVGPPTGEPVR 437
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-431 |
5.99e-56 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 191.62 E-value: 5.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 1 MSRdldVVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAAdltGVRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGF 80
Cdd:PRK09236 1 MKR---ILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAK---SADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 81 ASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGNLADLRPLHEAGVSGFKCFLLHS- 159
Cdd:PRK09236 75 ASESRAAVAGGITSFMEMP-NTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGVKVFMGASt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 160 G---VDefpplDAEELKPVMREIgsfDGLLIVHAEDAHTIDHAPAAAGGTYEKFLNS------RPREAENLAIEKVIELS 230
Cdd:PRK09236 154 GnmlVD-----NPETLERIFRDA---PTLIATHCEDTPTIKANLAKYKEKYGDDIPAemhpliRSAEACYKSSSLAVSLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 231 RRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDM 310
Cdd:PRK09236 226 KKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 311 VVTDHSPSTPDLKAldtGDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLC 390
Cdd:PRK09236 306 IATDHAPHTWEEKQ---GPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDIKERGFIREGYWADLV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1906352648 391 VFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGE 431
Cdd:PRK09236 383 LVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQ 423
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
6-433 |
2.63e-51 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 180.28 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVdtsatAADLTGVRTVQLADDEVLLPGVVDAHVHVNDP---GRTEWEGFAS 82
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIGIRGGRIAAL-----GEGLGPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 83 ATRAAAAGGVTTIVDMPL----NSIPPtcdvvALDLKRKTAASQALVDVGFW---GGAVPGNLA-DLRPLHEAGVSGFKC 154
Cdd:PRK13404 80 GTVSAAFGGTTTVIPFAAqhrgQSLRE-----AVEDYHRRAAGKAVIDYAFHlivADPTEEVLTeELPALIAQGYTSFKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 155 FLLHSGVDefppLDAEELKPVM---REIGSfdgLLIVHAEDAHTIDHAP---AAAGGTYEKF-LNSRPREAENLAIEKVI 227
Cdd:PRK13404 155 FMTYDDLK----LDDRQILDVLavaRRHGA---MVMVHAENHDMIAWLTkrlLAAGLTAPKYhAISRPMLAEREATHRAI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 228 ELSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIP----DGAtQFKCCPPIREGANREQLWEGL 303
Cdd:PRK13404 228 ALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDrpgmEGA-KYICSPPPRDKANQEAIWNGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 304 RDGVIDMVVTDHSP---STPDLKALDTGDFGVAW--GGISSLQLGLSAVWT-GARERGFALADVVRWMSQATARHAGLA- 376
Cdd:PRK13404 307 ADGTFEVFSSDHAPfrfDDTDGKLAAGANPSFKAiaNGIPGIETRLPLLFSeGVVKGRISLNRFVALTSTNPAKLYGLYp 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352648 377 RKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEKI 433
Cdd:PRK13404 387 RKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVV 443
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
23-444 |
8.81e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 158.01 E-value: 8.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 23 GAVGIRDGEIVAVdtsaTAADLTGVRTVQLADdEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNS 102
Cdd:PRK04250 15 GGIGIENGRISKI----SLRDLKGKEVIKVKG-GIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMP-NT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 103 IPPTCDVVALDLKRKTAASQALVDVGFwggavpgnladlrplheagvsgfkCFLLHSGVDEFPPLDAEELKPVMRE---- 178
Cdd:PRK04250 89 KPPIMDEKTYEKRMRIAEKKSYADYAL------------------------NFLIAGNCEKAEEIKADFYKIFMGAstgg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 179 --IGSFD-------GLLIVHAEDAHTIDHAPaaaggtyekflnSRPREAENLAIEKVIELSRRTGCRVHILHVSSADVLA 249
Cdd:PRK04250 145 ifSENFEvdyacapGIVSVHAEDPELIREFP------------ERPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 250 TLAtaRRDGVRVTAETCPHYLtFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDgvIDMVVTDHSPSTpdlkaLDTGD 329
Cdd:PRK04250 213 LIL--KSNLPWVSFEVTPHHL-FLTRKDYERNPLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHT-----LEDKE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 330 FGVAwgGISSLQLGLsAVWTGARERGF-ALADVVRWMSQATARHAGLARKGsIAVGHDADLCVFAPDDSYVVDAASLHHK 408
Cdd:PRK04250 283 AGAA--GIPGLETEV-PLLLDAANKGMiSLFDIVEKMHDNPARIFGIKNYG-IEEGNYANFAVFDMKKEWTIKAEELYTK 358
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1906352648 409 NAVTPYHGRTLAGVVRQTWLRGEKI----DIEAAPQGRLL 444
Cdd:PRK04250 359 AGWTPYEGFKLKGKVIMTILRGEVVmeddEIIGKPRGVRI 398
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
7-430 |
3.16e-41 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 151.75 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDG--ETAGAVGIRDGEIVAVDTSAtaADLTGVRTVQlADDEVLLPGVVDAHVHVNDPGRTEWEGFASAT 84
Cdd:PRK07627 3 IHIKGGRLIDPAAgtDRQADLYVAAGKIAAIGQAP--AGFNADKTID-ASGLIVCPGLVDLSARLREPGYEYKATLESEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVdmplnsIPPTCDVVaLD-------LK-RKTAASQALV------DVGFWGGAvpgnLADLRPLHEAGVS 150
Cdd:PRK07627 80 AAAVAGGVTSLV------CPPDTDPV-LDepglvemLKfRARNLNQAHVyplgalTVGLKGEV----LTEMVELTEAGCV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 151 GFKcfllHSGVdefPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAAGGTYEKF-LNSRPREAENLAIEKVIEL 229
Cdd:PRK07627 149 GFS----QANV---PVVDTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLgLSGVPVAAETIALHTIFEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 230 SRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVID 309
Cdd:PRK07627 222 MRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTID 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 310 MVVTDHSPSTPDLKALdtgDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLArKGSIAVGHDADL 389
Cdd:PRK07627 302 AICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLP-AGRLAEGAPADL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1906352648 390 CVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRG 430
Cdd:PRK07627 378 CVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAG 418
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
7-430 |
2.32e-38 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 145.37 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADltGVRTVQlADDEVLLPGVVDAHVHVNDP--GRTEWEGFASAT 84
Cdd:PLN02942 7 ILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPD--DVRVID-ATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVDMplnSIPPTCDVVALDLKRKTAASQALVDVGF------WGGAVPGNLADLrpLHEAGVSGFKCFLLH 158
Cdd:PLN02942 84 AAALAGGTTMHIDF---VIPVNGNLLAGYEAYEKKAEKSCMDYGFhmaitkWDDTVSRDMETL--VKEKGINSFKFFMAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 159 SGVdefPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHAPAAA---GGT-YEKFLNSRPREAENLAIEKVIELSRRTG 234
Cdd:PLN02942 159 KGS---LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMielGITgPEGHALSRPPLLEGEATARAIRLAKFVN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 235 CRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDG----ATQFKCCPPIREGANREQLWEGLRDGVIDM 310
Cdd:PLN02942 236 TPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPdftiASKYVMSPPIRPAGHGKALQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 311 VVTDHSPSTPDLKALDTGDFGVAWGGISSLQLGLSAVWTGARERG-FALADVVRWMSQATARHAGL-ARKGSIAVGHDAD 388
Cdd:PLN02942 316 VGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGqISPTDYVRVTSTECAKIFNIyPRKGAILAGSDAD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1906352648 389 LCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRG 430
Cdd:PLN02942 396 IIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQG 437
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
7-431 |
3.49e-38 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 143.64 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTP--DGETAGAVGIRDGEIVAVDTSATAADLTGVRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFASAT 84
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 85 RAAAAGGVTTIVDMPLNSipPTCDVVAL-DLKRKTAASQALVDV--------GFWGGavpgNLADLRPLHEAGVSGFKCF 155
Cdd:PRK09059 85 RAAAAGGVTSIIMMPDTD--PVIDDVALvEFVKRTARDTAIVNIhpaaaitkGLAGE----EMTEFGLLRAAGAVAFTDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 156 llHSGVDefpplDAEELKPVMREIGSFDGLLIVHAEDAHTIdhapaAAGGTYEKFLNSR------PREAENLAIEKVIEL 229
Cdd:PRK09059 159 --RRSVA-----NTQVMRRALTYARDFDAVIVHETRDPDLG-----GNGVMNEGLFASWlglsgiPREAEVIPLERDLRL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 230 SRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVID 309
Cdd:PRK09059 227 AALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 310 MVVTDHSPSTPDLKALdtgDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATARHAGLaRKGSIAVGHDADL 389
Cdd:PRK09059 307 IIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGL-PAGTLKPGAPADI 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1906352648 390 CVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGE 431
Cdd:PRK09059 383 IVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGK 424
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
23-416 |
1.19e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 141.92 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 23 GAVGIRDGEIVAVDTSATaadltGVRTVQLadDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNS 102
Cdd:PRK01211 16 LEIEVEDGKIKSIKKDAG-----NIGKKEL--KGAILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMP-NN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 103 IPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGN--LADLRPLheagvsGFKCFLLHSGVDEFPPLDAEELKpvmrEIG 180
Cdd:PRK01211 88 NIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNalILDERSI------GLKVYMGGTTNTNGTDIEGGEIK----KIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 181 SFDGLLIVHAEDAHTIDHAPAAAGGTYEKFLnSRPREAENLAIEKVIELSRRTgcrVHILHVSSADVLAtlatarrdgvR 260
Cdd:PRK01211 158 EANIPVFFHAELSECLRKHQFESKNLRDHDL-ARPIECEIKAVKYVKNLDLKT---KIIAHVSSIDVIG----------R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 261 VTAETCPHYLtFAAEEIPDGaTQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDLKAldtgDFGVAWGGISSL 340
Cdd:PRK01211 224 FLREVTPHHL-LLNDDMPLG-SYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYAKSGIIGV 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906352648 341 QLGLSAVWTGARERGFALADVVRWMSQATARHAGLaRKGSIAVGHDADLCVFAPDDSYVVDAASLHHKNAVTPYHG 416
Cdd:PRK01211 298 ETRVPLFLALVKKKILPLDVLYKTAIERPASLFGI-KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG 372
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
7-428 |
2.75e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 132.80 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGET--AGAVGIRDGEIVAVDT--SATAADltgvRTVQLADDEVLLPGVVDAHVHVNDPGRTEWEGFAS 82
Cdd:PRK07369 4 ELLQQVRVLDPVSNTdrIADVLIEDGKIQAIEPhiDPIPPD----TQIIDASGLILGPGLVDLYSHSGEPGFEERETLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 83 ATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPGN----LADLRPLHEAGVSGF------ 152
Cdd:PRK07369 80 LAAAAAAGGFTRVAILP-DTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGqgkqLTELAELAAAGVVGFtdgqpl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 153 -KCFLLHSGVDEFPPLDaeelKPVMreigsfdglliVHAEDAhtidhAPAAAGGTYEKF------LNSRPREAENLAIEK 225
Cdd:PRK07369 159 eNLALLRRLLEYLKPLG----KPVA-----------LWPCDR-----SLAGNGVMREGLlalrlgLPGDPASAETTALAA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 226 VIELSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRD 305
Cdd:PRK07369 219 LLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 306 GVIDMVVTDHSPSTPDLKaldTGDFGVAWGGISSLQLGLSAVWTGARERGfALADVVRW--MSQATARHAGLARKgSIAV 383
Cdd:PRK07369 299 GVIDAIAIDHAPYTYEEK---TVAFAEAPPGAIGLELALPLLWQNLVETG-ELSALQLWqaLSTNPARCLGQEPP-SLAP 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1906352648 384 GHDADLCVFAPDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWL 428
Cdd:PRK07369 374 GQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQTWV 418
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
57-441 |
2.21e-30 |
|
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: 120.25 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 57 VLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWGGAVPG 136
Cdd:cd01316 3 IRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMP-NTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 137 NLADLRPLHEAGVsGFKCFLLhsgvDEFPPLDAEELKPVMREIGSFDGL--LIVHAEDAhtidhapaaaggtyekflnsr 214
Cdd:cd01316 82 NAATVGELASEAV-GLKFYLN----ETFSTLILDKITAWASHFNAWPSTkpIVTHAKSQ--------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 215 preaeNLAieKVIELSRRTGCRVHILHVSSADVLATLATARRDGVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREga 294
Cdd:cd01316 136 -----TLA--AVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFLPTRE-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 295 NREQLWEGLrdGVIDMVVTDHSPSTPDLKALDT---GDFGVAwggiSSLQLGLSAVWTGArergFALADVVRWMSQATAR 371
Cdd:cd01316 207 DQEALWENL--DYIDCFATDHAPHTLAEKTGNKpppGFPGVE----TSLPLLLTAVHEGR----LTIEDIVDRLHTNPKR 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906352648 372 HAGLARKGSIAVghDADLcvfapDDSYVVDAASLHHKNAVTPYHGRTLAGVVRQTWLRGEK--IDIEAAPQG 441
Cdd:cd01316 277 IFNLPPQSDTYV--EVDL-----DEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETafIDGEIVAPP 341
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
27-433 |
2.45e-28 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 115.57 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 27 IRDGEIVAVDTsataaDLTGvRTVQLADDEVLLPGVVDAHVHVNDPGRTEwEGFASATRAAAAGGVTTIVDMPlNSIPPT 106
Cdd:PRK08417 3 IKDGKITEIGS-----DLKG-EEILDAKGKTLLPALVDLNVSLKNDSLSS-KNLKSLENECLKGGVGSIVLYP-DSTPAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 107 CDVVALDLKrKTAASQALVDVgfwggaVP--------GNLADLRPLHEAGVSGfkcflLHSGVDefppLDAEELKPVMRE 178
Cdd:PRK08417 75 DNEIALELI-NSAQRELPMQI------FPsiraldedGKLSNIATLLKKGAKA-----LELSSD----LDANLLKVIAQY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 179 IGSFDGLLIVHAEDAHTIDHAPAAAGGT-YEKFLNSRPREAENLAIEKVIELSRRTGCRVHILHVSSADVLATLATARRD 257
Cdd:PRK08417 139 AKMLDVPIFCRCEDSSFDDSGVMNDGELsFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 258 GVRVTAETCPHYLTFAAEEIPDGATQFKCCPPIREGANREQLWEGLRDGVIDMVVTDHSPSTPDLK--ALDTGDFgvawg 335
Cdd:PRK08417 219 GEKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKdlAFDEAAF----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 336 GISSLQLGLSAVWTG-ARERGFALADVVRWMSQATARHAGLaRKGSIAVGHDADLCVFAPDDSYVVDaaslhhkNAVTPY 414
Cdd:PRK08417 294 GIDSICEYFSLCYTYlVKEGIITWSELSRFTSYNPAQFLGL-NSGEIEVGKEADLVLFDPNESTIID-------DNFSLY 365
|
410
....*....|....*....
gi 1906352648 415 HGRTLAGVVRQTWLRGEKI 433
Cdd:PRK08417 366 SGDELYGKIEAVIIKGKLY 384
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
52-430 |
1.08e-21 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 96.37 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 52 LADDEVLLPGVVDAHVHVNDPGRTEWEGFASATRAAAAGGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQALVDVGFWG 131
Cdd:PRK00369 39 LPQGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMP-NTIPPLNTPEAITEKLAELEYYSRVDYFVYS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 132 GaVPgnlADLRPLHEAGVSGFKCFllhsgvdefpPLDAEELKpVMREIGSFDGLLIVHAEdahtidHAPAAAGGTYEKfl 211
Cdd:PRK00369 118 G-VT---KDPEKVDKLPIAGYKIF----------PEDLEREE-TFRVLLKSRKLKILHPE------VPLALKSNRKLR-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 212 nsRPREAENLAIEKVIELSrrtgcRVHILHVSSadvLATLATARRDGvrVTAETCPHYLTFAAEeipdGATQFKCCPPIR 291
Cdd:PRK00369 175 --RNCWYEIAALYYVKDYQ-----NVHITHASN---PRTVRLAKELG--FTVDITPHHLLVNGE----KDCLTKVNPPIR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 292 EGANREQLWEGLRDgvIDMVVTDHSPSTPDLKALdtgDFGVAWGGISSLQLGLSAVWTGARERGFALADVVRWMSQATAR 371
Cdd:PRK00369 239 DINERLWLLQALSE--VDAIASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPAR 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906352648 372 HAGLArKGSIAVGHDADLCVFAPDDSYVvdaASLHHKNAVTPYHGRTLAGVVRQTWLRG 430
Cdd:PRK00369 314 ILGIP-YGEIKEGYRANFTVIQFEDWRY---STKYSKVIETPLDGFELKASVYATIVQG 368
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-395 |
1.05e-16 |
|
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: 81.01 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 57 VLLPGVVDAHVHVND--------PGRTEWEGFASATRAAAAGGVTTIVDMPLNsippTCDVVALDLKrktAASQALVDVG 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgipvPPEFAYEALRLGITTMLKSGTTTVLDMGAT----TSTGIEALLE---AAEELPLGLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 129 FWGGAVP----GNLADLRPLHEAGVSG--FKCFLLHSGVD------EFPPLDAEELKPVMREIGSFDGLLIVHA-EDAHT 195
Cdd:pfam01979 74 FLGPGCSldtdGELEGRKALREKLKAGaeFIKGMADGVVFvglaphGAPTFSDDELKAALEEAKKYGLPVAIHAlETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 196 IDHAPAAAGGTYEkflnsRPREAENLaiEKVIELSRRTGCRVHILHVSSADVLATLATARRDGVRvtaeTCPhyltfAAE 275
Cdd:pfam01979 154 VEDAIAAFGGGIE-----HGTHLEVA--ESGGLLDIIKLILAHGVHLSPTEANLLAEHLKGAGVA----HCP-----FSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 276 EIPdgatqfkccppireGANREQLWEGLRDGVIDMVVTDHSPSTPDLKALDTGDFGVAwggisslqlglsavWTGARERG 355
Cdd:pfam01979 218 SKL--------------RSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALE--------------LQFDPEGG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1906352648 356 FALADVVRWMSQATARHAGLA-RKGSIAVGHDADLCVFAPD 395
Cdd:pfam01979 270 LSPLEALRMATINPAKALGLDdKVGSIEVGKDADLVVVDLD 310
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
6-396 |
1.39e-16 |
|
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: 81.19 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVtpDGETA----GAVGIRDGEIVAVdtsATAADLTGVRTVQlADDEVLLPGVVDAHVHvnDPGRTEWEGFA 81
Cdd:cd01297 1 DLVIRNGTVV--DGTGAppftADVGIRDGRIAAI---GPILSTSAREVID-AAGLVVAPGFIDVHTH--YDGQVFWDPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 82 SATRAAaagGVTTIVDMPLNSIPPTCDVVALDLKRKT-AASQALVDVGFWGGAVPGNLADL-----RPLHEAGVSGFKCF 155
Cdd:cd01297 73 RPSSRQ---GVTTVVLGNCGVSPAPANPDDLARLIMLmEGLVALGEGLPWGWATFAEYLDAlearpPAVNVAALVGHAAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 156 -LLHSGVDEFPPLDAEELKpvMRE----------IGSFDGLLIVHAEDAHT-----IDHAPAAAGGTYEKFLNSRPREAE 219
Cdd:cd01297 150 rRAVMGLDAREATEEELAK--MREllrealeagaLGISTGLAYAPRLYAGTaelvaLARVAARYGGVYQTHVRYEGDSIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 220 NlAIEKVIELSRRTGCRVHILHVSSAD---------VLATLATARRDGVRVTAETCPHyltfaaeeipdgatqfkccppi 290
Cdd:cd01297 228 E-ALDELLRLGRETGRPVHISHLKSAGapnwgkidrLLALIEAARAEGLQVTADVYPY---------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 291 reGANREQLWEGLRDGVIDMVVTDHSPS-TPDLKALdtGDFGvawggissLQLGlsaVWtgARERG-FALADVVRWMSQA 368
Cdd:cd01297 285 --GAGSEDDVRRIMAHPVVMGGSDGGALgKPHPRSY--GDFT--------RVLG---HY--VRERKlLSLEEAVRKMTGL 347
|
410 420
....*....|....*....|....*...
gi 1906352648 369 TARHAGLARKGSIAVGHDADLCVFAPDD 396
Cdd:cd01297 348 PARVFGLADRGRIAPGYRADIVVFDPDT 375
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
6-434 |
2.64e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.98 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDGETA---GAVGIRDGEIVAVDTSATAADLTGVRTVQLADdEVLLPGVVDAHVHVNDPGRTEWEGFAS 82
Cdd:COG1228 9 TLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATG-KTVLPGLIDAHTHLGLGGGRAVEFEAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 83 ATRAAAA---------------GGVTTIVDMPLNSIPPTCDVVA-----LDLKRKTAASQAL-VDVGFWGGAVPGNLADL 141
Cdd:COG1228 88 GGITPTVdlvnpadkrlrralaAGVTTVRDLPGGPLGLRDAIIAgesklLPGPRVLAAGPALsLTGGAHARGPEEARAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 142 RPLHEAGVSGFKCFllhsGVDEFPPLDAEELKPVMREIGSFDGLLIVHAEDAHTIDHApAAAGGtyekflnsrpreaenl 221
Cdd:COG1228 168 RELLAEGADYIKVF----AEGGAPDFSLEELRAILEAAHALGLPVAAHAHQADDIRLA-VEAGV---------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 222 aieKVIElsrrtgcrvHILHVsSADVLATLatARRDGVRVTAeTCPHYLTFAAEEIPDGATQFKccppiregANREQLWE 301
Cdd:COG1228 227 ---DSIE---------HGTYL-DDEVADLL--AEAGTVVLVP-TLSLFLALLEGAAAPVAAKAR--------KVREAALA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 302 GLRdgvidmvvtdhspstpdlKALDTG-------DFGVAWGGISSLQLGLSAvwtgARERGFALADVVRWMSQATARHAG 374
Cdd:COG1228 283 NAR------------------RLHDAGvpvalgtDAGVGVPPGRSLHRELAL----AVEAGLTPEEALRAATINAAKALG 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352648 375 LARK-GSIAVGHDADLCvfapddsyVVDAASLHHKNAVTPyhgrtlagvVRQTWLRGEKID 434
Cdd:COG1228 341 LDDDvGSLEPGKLADLV--------LLDGDPLEDIAYLED---------VRAVMKDGRVVD 384
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
63-346 |
2.21e-09 |
|
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: 58.11 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 63 VDAHVHVNDPGRTEWEGFASATRAAAA------------------GGVTTIVDMPlNSIPPTCDVVALDLKRKTAASQAL 124
Cdd:cd01292 2 IDTHVHLDGSALRGTRLNLELKEAEELspedlyedtlraleallaGGVTTVVDMG-STPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 125 VDVGFWGGA-----------VPGNLADLRPLHEAGVSGFKCFLLhsgvDEFPPLDAEELKPVMREIGSFDGLLIVHAEDA 193
Cdd:cd01292 81 IRVVLGLGIpgvpaavdedaEALLLELLRRGLELGAVGLKLAGP----YTATGLSDESLRRVLEEARKLGLPVVIHAGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 194 HTIDHapaaaggtyekflnsrpreaenlAIEKVIELSRRtGCRVHILHVsSADVLATLATARRDGVRVTAetCPHYLTFA 273
Cdd:cd01292 157 PDPTR-----------------------ALEDLVALLRL-GGRVVIGHV-SHLDPELLELLKEAGVSLEV--CPLSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906352648 274 AeeipdgatqfkccppiREGANREQLWEGLRDGVIDMVVTDHSPSTPDLKALDtgdfgVAWGGISSLQLGLSA 346
Cdd:cd01292 210 G----------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLA-----LLRLLLKVLRLGLSL 261
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
6-69 |
7.47e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.89 E-value: 7.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352648 6 DVVIRAARMVTPDGE--TAGAVGIRDGEIVAVDTSATAADLTGVRTVQL-ADDEVLLPGVVDAHVHV 69
Cdd:COG1574 9 DLLLTNGRIYTMDPAqpVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIdLGGKTVLPGFIDAHVHL 75
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
6-268 |
1.19e-07 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 53.93 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 6 DVVIRAARMVTPDG--ETAGAVGIRDGEIVAVDTSATAADltgvRTVQlADDEVLLPGVVDAHVHVNDPGRTEWEGFAsa 83
Cdd:PRK09061 20 DLVIRNGRVVDPETglDAVRDVGIKGGKIAAVGTAAIEGD----RTID-ATGLVVAPGFIDLHAHGQSVAAYRMQAFD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 84 traaaagGVTTIVDMPLNSIPptcdvVALDLKRKTAASQALvDVGFWGGAVPGNLADLRPLHEAG--VSGFKCFLLHSGV 161
Cdd:PRK09061 93 -------GVTTALELEAGVLP-----VARWYAEQAGEGRPL-NYGASVGWTPARIAVLTGPQAEGtiADFGKALGDPRWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 162 DEFPPldAEELKPVMREI--GSFDGLL---IVHAEDAHTiDHAP-------AAAGG----TYEKFLNSRPREAENLAIEK 225
Cdd:PRK09061 160 ERAAT--PAELAEILELLeqGLDEGALgigIGAGYAPGT-GHKEylelarlAARAGvptyTHVRYLSNVDPRSSVDAYQE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1906352648 226 VIELSRRTGCRVHILHVSSA------DVLATLATARRDGVRVTAETCPH 268
Cdd:PRK09061 237 LIAAAAETGAHMHICHVNSTslrdidRCLALVEKAQAQGLDVTTEAYPY 285
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
5-153 |
1.76e-07 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 5 LDVVIRAARMVTP-DGETAGAVGIRDGEIVAVDTSATAADLTGV---------RTVQLADDEVLLPGVVDAHVHVNDPGR 74
Cdd:PRK13308 68 LDFVLCNVTVIDPvLGIVKGDIGIRDGRIVGIGKAGNPDIMDGVdprlvvgpgTDVRPAEGLIATPGAIDVHVHFDSAQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 75 TEwegfasatrAAAAGGVTTIVDMPLNSIPPTCDVVALDLKRKTAASQAL-VDVGFWGGAVPGNLADLRPLHEAGVSGFK 153
Cdd:PRK13308 148 VD---------HALASGITTMLGGGLGPTVGIDSGGPFNTGRMLQAAEAWpVNFGFLGRGNSSKPAALIEQVEAGACGLK 218
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-69 |
2.02e-06 |
|
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: 49.83 E-value: 2.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906352648 6 DVVIRAARMVTPDGETA----GAVGIRDGEIVAVDTSATAADLTGVRTVQLADDEVLLPGVVDAHVHV 69
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHL 68
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-69 |
3.66e-05 |
|
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: 45.76 E-value: 3.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1906352648 24 AVGIRDGEIVAVDTSATAADLTG--VRTVQLaDDEVLLPGVVDAHVHV 69
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALKGpaTEVIDL-KGKTVLPGFIDSHSHL 47
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
8-69 |
5.24e-05 |
|
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: 45.27 E-value: 5.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906352648 8 VIRAARMVTPDGET---AGAVGIRDGEIVAVDTSATAADLTGVRTVQLADDeVLLPGVVDAHVHV 69
Cdd:cd01298 2 LIRNGTIVTTDPRRvleDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGK-VVMPGLVNTHTHL 65
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-68 |
5.51e-05 |
|
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: 45.26 E-value: 5.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906352648 7 VVIRAARMVTPDGETAGAVGIRDGEIVAVdtsATAADLTGVRTVQLADDEVLLPGVVDAHVH 68
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAI---GPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
6-66 |
5.94e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.17 E-value: 5.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906352648 6 DVVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAAdltgVRTVQLADDeVLLPGVVDAH 66
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASAL----PGAIDAEGD-YLLPGLVDLH 58
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
6-68 |
1.04e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 44.61 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906352648 6 DVVIRAARMVTPDGETA---GAVGIRDGEIVAVdtsATAADLTGVRTVQLADDEVLLPGVVDAHVH 68
Cdd:PRK07228 2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAV---GDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
7-97 |
1.08e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 44.07 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 7 VVIRAARMVTPDGETAGA--VGIRDGEIVAVDTSATAADltGVRTVQLADDEVLlPGVVDAHVHVNdPGRTEWegFASAT 84
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVidIAIEDGKIAAVAGDIDGSQ--AKKVIDLSGLYVS-PGWIDLHVHVY-PGSTPY--GDEPD 74
|
90
....*....|...
gi 1906352648 85 RAAAAGGVTTIVD 97
Cdd:PRK09237 75 EVGVRSGVTTVVD 87
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
5-153 |
3.37e-04 |
|
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: 43.09 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 5 LDVVIRAARMVTPDGETAGAVGIRDGEIVAVDTSATAADLTGVRT---------VQLADDEVLLPGVVDAHVHVNDPGRT 75
Cdd:cd00375 65 LDLVITNALIIDYTGIYKADIGIKDGRIVAIGKAGNPDIMDGVTPnmivgpsteVIAGEGKIVTAGGIDTHVHFICPQQI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906352648 76 EwegfasatrAAAAGGVTTIV----DMPLNSIPPTCDVVALDLKRKTAASQAL-VDVGFWGGAVPGNLADLRPLHEAGVS 150
Cdd:cd00375 145 E---------EALASGITTMIgggtGPAAGTKATTCTPGPWNIKRMLQAADGLpVNIGFLGKGNGSSPDALAEQIEAGAC 215
|
...
gi 1906352648 151 GFK 153
Cdd:cd00375 216 GLK 218
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-68 |
5.84e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 42.01 E-value: 5.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906352648 8 VIRAARMVTPDGE-TAGAVGIRDGEIVAVdtsaTAADLTGVRTVQLADDeVLLPGVVDAHVH 68
Cdd:COG1820 1 AITNARIFTGDGVlEDGALLIEDGRIAAI----GPGAEPDAEVIDLGGG-YLAPGFIDLHVH 57
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
24-68 |
9.20e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 41.44 E-value: 9.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1906352648 24 AVGIRDGEIVAVDTSATAADLTGVRTVQLADDEVLLPGVVDAHVH 68
Cdd:PRK09045 30 AVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLINAHTH 74
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
355-402 |
1.82e-03 |
|
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: 40.25 E-value: 1.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1906352648 355 GFALADVVRWMSQATARHAGLA-RKGSIAVGHDADLCVFapDDSYVVDA 402
Cdd:cd00854 323 GCPLEEAVRMASLNPAKLLGLDdRKGSLKPGKDADLVVL--DDDLNVKA 369
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
338-395 |
3.47e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 39.31 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906352648 338 SSLQLgLSAVWTGARERGFALADVVRWMSQATARHAGLA-RKGSIAVGHDADLCVFAPD 395
Cdd:COG1820 305 STLTM-DDAVRNLVEWTGLPLEEAVRMASLNPARALGLDdRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
5-68 |
5.96e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 38.85 E-value: 5.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906352648 5 LDVVIRAARMvtPDGETAGAVGIRDGEIVAVDTSATAAdltgVRTVQLADDEVLLPGVVDAHVH 68
Cdd:PRK07572 2 FDLIVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAE----AAEEIDAAGRLVSPPFVDPHFH 59
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
344-400 |
8.76e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 38.03 E-value: 8.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352648 344 LSAVWTGARERGFALADVVRWMSQATARHAGLARKGSIAVGHDADLCVFAPDDSYVV 400
Cdd:cd01306 261 LHAAFRLADLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDGVPV 317
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
7-69 |
9.14e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 38.44 E-value: 9.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906352648 7 VVIRAARMVTPDGET----AGAVGIRDGEIVAVDTSATAADLTGVRtvqlADDEVLLPGVVDAHVHV 69
Cdd:PRK08204 4 TLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIEAPDAEVVD----ARGMIVMPGLVDTHRHT 66
|
|
| |
