|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-449 |
0e+00 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 945.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAA 80
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDND 160
Cdd:PRK08044 81 AKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 161 FRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHV 240
Cdd:PRK08044 161 FRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 241 CHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCP 320
Cdd:PRK08044 241 CHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 321 PEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLT 400
Cdd:PRK08044 321 PEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16128496 401 NDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
Cdd:PRK08044 401 NEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-449 |
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: 764.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQD-LGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIGPDiLGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 83 GGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDrgidNDFR 162
Cdd:TIGR03178 81 GGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLSPSGD----DEFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 163 DVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCH 242
Cdd:TIGR03178 157 HVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 243 VSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPE 322
Cdd:TIGR03178 237 LSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 323 MK-AGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTN 401
Cdd:TIGR03178 317 LKrAGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPDESYTLTP 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128496 402 DDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQgFPVAPKGQFIL 449
Cdd:TIGR03178 397 DDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQ-FIGAPKGQLLL 443
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-449 |
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: 707.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAA 81
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIanTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 82 KGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDrgidNDF 161
Cdd:cd01315 81 AGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGV----DEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 162 RDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVC 241
Cdd:cd01315 157 PAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 242 HVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPP 321
Cdd:cd01315 237 HLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 322 EMKA---GNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQ-QKGRIAPGKDADFVFIQPNSSY 397
Cdd:cd01315 317 ELKLlgkGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLShQKGRIAVGYDADFVVWDPEEEF 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16128496 398 VLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFpVAPKGQFIL 449
Cdd:cd01315 397 TVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVV-GEPLGQLLL 447
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-451 |
0e+00 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 515.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRA 79
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEIsSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 80 AAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDrgidN 159
Cdd:PRK06189 81 LAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVIGFKAFMSNSGT----D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 160 DFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLH 239
Cdd:PRK06189 157 EFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 240 VCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPC 319
Cdd:PRK06189 237 FVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 320 PPEMKAG-NIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYV 398
Cdd:PRK06189 317 PPELKEGdDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDETYT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16128496 399 LTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVaPKGQFILKH 451
Cdd:PRK06189 397 LTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPP-PRGQLLRPS 448
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-448 |
5.70e-180 |
|
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: 510.02 E-value: 5.70e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 6 IIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKG 83
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLaaPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 84 GITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLV---SYNIDRLHELDEVGVVGFKCFVATCGDRGIDND 160
Cdd:COG0044 81 GVTTVVDMP-NTNPVTDTPEALEFKLARAEEKALVDVGPHGALTkglGENLAELGALAEAGAVAFKVFMGSDDGNPVLDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 161 frdvndWQFFKGAQKLGELGQPVLVHCENALICDELgeeAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHV 240
Cdd:COG0044 160 ------GLLRRALEYAAEFGALVAVHAEDPDLIRGG---VMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 241 CHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCP 320
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 321 PEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLT 400
Cdd:COG0044 311 LEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDAEWTVT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128496 401 NDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQgFPVAPKGQFI 448
Cdd:COG0044 391 AEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGE-VVGEPRGRFL 437
|
|
| PLN02795 |
PLN02795 |
allantoinase |
25-450 |
6.33e-115 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 346.76 E-value: 6.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 25 VKGGKIAAIGQDLGDAK-----EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPAT 99
Cdd:PLN02795 66 VEGGRIVSVTKEEEAPKsqkkpHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPLNSFPST 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 100 VDRASIELKFDAAKGKLTIDAAQLGGLVS---YNIDRLHELDEVGVVGFKCFVATCGdrgiDNDFRDVNDWQFFKGAQKL 176
Cdd:PLN02795 146 TSVETLELKIEAAKGKLYVDVGFWGGLVPenaHNASVLEELLDAGALGLKSFMCPSG----INDFPMTTATHIKAALPVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 177 GELGQPVLVHCEnalICDELGEEAKREGRVTAHD-YVASRPVFTEVEAIRRVLYLAK-------VAGCRLHVCHVS-SPE 247
Cdd:PLN02795 222 AKYGRPLLVHAE---VVSPVESDSRLDADPRSYStYLKSRPPSWEQEAIRQLLEVAKdtrpggvAEGAHVHIVHLSdAES 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 248 GVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMK--- 324
Cdd:PLN02795 299 SLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKlle 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 325 AGNIMKAWGGIAGLQSCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDL 404
Cdd:PLN02795 379 EGNFLRAWGGISSLQFVLPATW-TAGRAYGLTLEQLARWWSERPAKLAGLDSKGAIAPGKDADIVVWDPEAEFVLDESYP 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128496 405 EY--RHKVSPYVGRTIGARITKTILRGDVIYdIEQGFPVAPKGQFILK 450
Cdd:PLN02795 458 IYhkHKSLSPYLGTKLSGKVIATFVRGNLVF-LEGKHAKQACGSPILA 504
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-448 |
2.52e-101 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 309.66 E-value: 2.52e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAA 81
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLdgSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 82 KGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGlVSYNIDRLHELDEVGVVGF-KCFVA-TCGDRGIDN 159
Cdd:PRK02382 83 AGGVTTVVDQP-NTDPPTVDGESFDEKAELAARKSIVDFGINGG-VTGNWDPLESLWERGVFALgEIFMAdSTGGMGIDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 160 D-FRDVndwqffkgAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDyvASRPVFTEVEAIRRVLYLAKVAGCRL 238
Cdd:PRK02382 161 ElFEEA--------LAEAARLGVLATVHAEDEDLFDELAKLLKGDADADAWS--AYRPAAAEAAAVERALEVASETGARI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 239 HVCHVSSPEGVEEVTRARqegqdVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSP 318
Cdd:PRK02382 231 HIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 319 CPPEMKAGNIMKAWGGIAGLQSCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYV 398
Cdd:PRK02382 306 HTREEKDADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAARE 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16128496 399 LTNDDLEYRHKVSPYVGRTiGARITKTILRGDVIYDiEQGFPVAP-KGQFI 448
Cdd:PRK02382 385 IRGDDLHSKAGWTPFEGME-GVFPELTMVRGTVVWD-GDDINAKRgRGEFL 433
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-434 |
5.96e-100 |
|
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: 306.07 E-value: 5.96e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLeaPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMpLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEV---GVVGFKCFVATcgdrgi 157
Cdd:cd01314 81 AAGGTTTIIDF-AIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELvkkGISSFKVFMAY------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 158 dNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCR 237
Cdd:cd01314 154 -KGLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 238 LHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE---EIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVS 314
Cdd:cd01314 233 LYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdwFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 315 DHSPCPPEMKA---GNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVF 390
Cdd:cd01314 313 DHCPFNFAQKArgkDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLyPRKGTIAVGSDADLVI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 16128496 391 IQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:cd01314 393 WDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVE 436
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-448 |
2.35e-99 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 305.17 E-value: 2.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 3 FDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDakEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANLGD--EVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMPLnQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEV---GVVGFKCFVAtcgdrgI 157
Cdd:PRK08323 79 ACGGTTTIIDFAL-QPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELveeGITSFKLFMA------Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 158 DNDFRdVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCR 237
Cdd:PRK08323 152 KGALM-LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 238 LHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTL--AK--CSPPIRDLENQKGMWEKLFNGEIDCLV 313
Cdd:PRK08323 231 LYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegAKyvMSPPLRDKEHQDALWRGLQDGDLQVVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 314 SDHspCP-----PEMKA-GNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQ-QKGRIAPGKDA 386
Cdd:PRK08323 311 TDH--CPfcfeqKKQLGrGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYpRKGTIAVGADA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128496 387 DFVFIQPNSSYVLTNDDLeyRHKV--SPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFI 448
Cdd:PRK08323 389 DIVIWDPNATKTISASTL--HSNVdyNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFL 450
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
5-448 |
3.85e-90 |
|
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: 281.20 E-value: 3.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLG--DAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIppDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMPLnQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHE----LDEVGVVGFKCFVATcgdrg 156
Cdd:TIGR02033 81 AAGGTTTIIDFVV-PEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEhipeVKEEGINSFKVFMAY----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 157 idNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
Cdd:TIGR02033 155 --KNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 237 RLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE---EIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLV 313
Cdd:TIGR02033 233 PLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDkpgFEGAKYVCSPPLREPEDQDALWSALSSGALQTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 314 SDHspCP------PEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQ-QKGRIAPGKDA 386
Cdd:TIGR02033 313 SDH--CTfnfaqkKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYpRKGTIAVGSDA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128496 387 DFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFI 448
Cdd:TIGR02033 391 DIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFV 452
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
48-429 |
2.22e-88 |
|
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: 273.44 E-value: 2.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 48 GLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAqLGGLV 127
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMP-NTKPPTTTAEALYEKLRLAAAKSVVDYG-LYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 128 SYNIDrLHELDEVGVVGFKCFVATC-GDRGID-NDFRDVndwqffkgaqkLGELGQPVLVHCENALICDELGEEAKREgr 205
Cdd:cd01318 79 TGSED-LEELDKAPPAGYKIFMGDStGDLLDDeETLERI-----------FAEGSVLVTFHAEDEDRLRENRKELKGE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 206 vtaHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEvtrARQEGQDVTCESCPHYFVLDTDQFEEIGTLA 285
Cdd:cd01318 145 ---SAHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKL---IKKAKPGVTVEVTPHHLFLDVEDYDRLGTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 286 KCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDeAVQKRGMSLPMFGKLMA 365
Cdd:cd01318 219 KVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLT-LVNKGILSLSRVVRLTS 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128496 366 TNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRG 429
Cdd:cd01318 298 HNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
49-425 |
9.43e-88 |
|
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: 271.19 E-value: 9.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 49 LVVSPGMVDAHTHISEPG-RSHWEGYETGTRAAAKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLV 127
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTG-PPPIDLPAIELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 128 S-YNIDRLHELDEVGVVGFKCFVATCGdrgidNDFRDVNDWQFFKGAQKLGELGQPVLVHCEnalicdelgeeakregrv 206
Cdd:cd01302 80 PgDVTDELKKLFDAGINSLKVFMNYYF-----GELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 207 tahdyvasrpvfteveairRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAK 286
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 287 CSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMK--AGNIMKAWGGIAGLQSCMDVMFdEAVQKRGMSLPMFGKLM 364
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKesGKDIWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVEIL 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128496 365 ATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKT 425
Cdd:cd01302 277 SENPARIFGLYPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
21-433 |
1.43e-87 |
|
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: 273.16 E-value: 1.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 21 VDIAVKGGKIAAIGQ-DLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPAT 99
Cdd:TIGR00857 6 VDILVEGGRIKKIGKlRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 100 vDRASIELKFDAAKGKLTIDAAQLGGLVSYNIdrlheLDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGEL 179
Cdd:TIGR00857 86 -TPETLEWKLQRLKKVSLVDVHLYGGVTQGNQ-----GKELTEAYELKEAGAVGRMFTDDGSEVQDILSMRRALEYAAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 180 GQPVLVHCENAlicDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEG 259
Cdd:TIGR00857 160 GVPIALHAEDP---DLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 260 QDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQ 339
Cdd:TIGR00857 237 IKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 340 SCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIG 419
Cdd:TIGR00857 317 TALPLLLQLLVKGL-ISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLK 395
|
410
....*....|....
gi 16128496 420 ARITKTILRGDVIY 433
Cdd:TIGR00857 396 GKPIATILRGKVVY 409
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-432 |
8.90e-83 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 261.78 E-value: 8.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGqDLG--DAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTR 78
Cdd:PRK09060 3 QTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSgaSAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 79 AAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEV-GVVGFKCFV-ATCGDRG 156
Cdd:PRK09060 82 AAVLGGVTAVFEMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELERLpGCAGIKVFMgSSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 157 IDND--FRDVndwqfFKGAQKLgelgqpVLVHCEnalicDELGEEAKREGRVTAHdyVASRPVFTEVE----AIRRVLYL 230
Cdd:PRK09060 161 VEDDegLRRI-----LRNGRRR------AAFHSE-----DEYRLRERKGLRVEGD--PSSHPVWRDEEaallATRRLVRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 231 AKVAGCRLHVCHVSSPEGVEEVTRARqegqDV-TCESCPHYFVLD-TDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGE 308
Cdd:PRK09060 223 ARETGRRIHVLHVSTAEEIDFLADHK----DVaTVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 309 IDCLVSDHSPCPPEMKAgnimKAW----GGIAGLQSCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLQQKGRIAPGK 384
Cdd:PRK09060 299 VDVLGSDHAPHTLEEKA----KPYpaspSGMTGVQTLVPIMLDHVNAGR-LSLERFVDLTSAGPARIFGIAGKGRIAVGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128496 385 DADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVI 432
Cdd:PRK09060 374 DADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-433 |
9.26e-83 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 261.28 E-value: 9.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVI-LENEARVVDIAVKGGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
Cdd:PRK09357 3 ILIKNGRVIdPKGLDEVADVLIDDGKIAAIGENIEaEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 83 GGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLG----GLVSYNIDRLHELDEVGVVGFkcfvatcGDRGID 158
Cdd:PRK09357 83 GGFTTVVAMP-NTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGaitkGLAGEELTEFGALKEAGVVAF-------SDDGIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 159 ndfrdVNDWQFFKGA-QKLGELGQPVLVHCENalicDELGEEAK-REGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
Cdd:PRK09357 155 -----VQDARLMRRAlEYAKALDLLIAQHCED----PSLTEGGVmNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 237 RLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDH 316
Cdd:PRK09357 226 RVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 317 SPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQkGRIAPGKDADFVFIQPNSS 396
Cdd:PRK09357 306 APHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVIFDPEAE 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 16128496 397 YVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
Cdd:PRK09357 385 WTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-448 |
1.39e-81 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 259.63 E-value: 1.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEP---GRSHWEGYETGT 77
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 78 RAAAKGGITTMIEMPLNQLPATVdRASIELKFDAAKGKLTIDAAQlgGLVSYNIDR------LHELDEVGVVGFKCFVA- 150
Cdd:PRK13404 82 VSAAFGGTTTVIPFAAQHRGQSL-REAVEDYHRRAAGKAVIDYAF--HLIVADPTEevlteeLPALIAQGYTSFKVFMTy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 151 ---TCGDRGIdNDFRDVndwqffkgAQKLGELgqpVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRV 227
Cdd:PRK13404 159 ddlKLDDRQI-LDVLAV--------ARRHGAM---VMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 228 LYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFV-----LDTDQFEeiGTLAKCSPPIRDLENQKGMWE 302
Cdd:PRK13404 227 IALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFltaedLDRPGME--GAKYICSPPPRDKANQEAIWN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 303 KLFNGEIDCLVSDHSPCPPEMKAG--------NIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL 374
Cdd:PRK13404 305 GLADGTFEVFSSDHAPFRFDDTDGklaaganpSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128496 375 Q-QKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIydIEQGFPVAP--KGQFI 448
Cdd:PRK13404 385 YpRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVV--VEDGELVAErgSGQFL 459
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-425 |
1.18e-73 |
|
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: 235.98 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 42 EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGK-----L 116
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMP-NTNPVIDNPAVVELLKNRAKDVgivrvL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 117 TIDAAQLGGLVSYNIDrLHELDEVGVVGFKcfvatcgdrgidNDFRDVNDWQFFKGAQKLGE-LGQPVLVHCENALICDE 195
Cdd:cd01317 82 PIGALTKGLKGEELTE-IGELLEAGAVGFS------------DDGKPIQDAELLRRALEYAAmLDLPIIVHPEDPSLAGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 196 L----GEEAKREGrvtahdyVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYF 271
Cdd:cd01317 149 GvmneGKVASRLG-------LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 272 VLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQ 351
Cdd:cd01317 222 LLDDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVK 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128496 352 KRGMSLPMFGKLMATNAADIFGLQQkGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKT 425
Cdd:cd01317 302 GGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-434 |
1.99e-69 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 226.86 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGTVILEN-EARVVDIAVKGGKIAAIGQDLGDAK--EVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGT 77
Cdd:PRK07575 1 MMMSLLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISATAvdTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 78 RAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDevGVVGFKCFV-ATCGDRG 156
Cdd:PRK07575 81 RACAKGGVTSFLEMP-NTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTAN--PTCGIKIFMgSSHGPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 157 IDNDfrDVNDWQFFKGAQklgelgqPVLVHCEnalicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVLYLAKV 233
Cdd:PRK07575 158 VDEE--AALERIFAEGTR-------LIAVHAE-----DQARIRARRAefaGISDPADHSQIQDEEAALLATRLALKLSKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 234 AGCRLHVCHVSSpeGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLV 313
Cdd:PRK07575 224 YQRRLHILHLST--AIEAELLRQDKPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 314 SDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQP 393
Cdd:PRK07575 302 TDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGK-CTVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16128496 394 NSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK07575 381 NTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFD 421
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-434 |
3.25e-61 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 205.49 E-value: 3.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSfDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTR 78
Cdd:PRK09236 1 MK-RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAksADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 79 AAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFV-ATCGDRGI 157
Cdd:PRK09236 80 AAVAGGITSFMEMP-NTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGVKVFMgASTGNMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 158 DND------FRDVndwqffkgaqklgelGQPVLVHCENALICDELGEEAKRE-GR-VTAHDYvasrPVFTEVEAI----R 225
Cdd:PRK09236 159 DNPetleriFRDA---------------PTLIATHCEDTPTIKANLAKYKEKyGDdIPAEMH----PLIRSAEACykssS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 226 RVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLF 305
Cdd:PRK09236 220 LAVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 306 NGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKD 385
Cdd:PRK09236 300 DDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDIKERGFIREGYW 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16128496 386 ADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK09236 379 ADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYH 427
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-448 |
7.59e-55 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 190.05 E-value: 7.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 2 SFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGT 77
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLkvPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 78 RAAAKGGITTMIE--MPLNQlpatvdraSIELKFDAAKGKLTIDAAQLG---GLVSYNIDRLHELD----EVGVVGFKCF 148
Cdd:PLN02942 84 AAALAGGTTMHIDfvIPVNG--------NLLAGYEAYEKKAEKSCMDYGfhmAITKWDDTVSRDMEtlvkEKGINSFKFF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 149 VATCGDRGidndfrdVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVL 228
Cdd:PLN02942 156 MAYKGSLM-------VTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 229 YLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF--EEIGTLAK--CSPPIRDLENQKGMWEKL 304
Cdd:PLN02942 229 RLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLwdPDFTIASKyvMSPPIRPAGHGKALQAAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 305 FNGEIDCLVSDHSPCPPEMKA---GNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRI 380
Cdd:PLN02942 309 SSGILQLVGTDHCPFNSTQKAfgkDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIyPRKGAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128496 381 APGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFI 448
Cdd:PLN02942 389 LAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYI 456
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
10-432 |
6.70e-51 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 177.27 E-value: 6.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 10 GTVILENeaRVVD--IAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITT 87
Cdd:PRK04250 4 GKFLLKG--RIVEggIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 88 MIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAqLGGLVSYNIDrlhELDEVGVVGFKCF-VATCGDRGIDNdfrdvnd 166
Cdd:PRK04250 82 VFDMP-NTKPPIMDEKTYEKRMRIAEKKSYADYA-LNFLIAGNCE---KAEEIKADFYKIFmGASTGGIFSEN------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 167 wqfFKGAQKlgELGQPVLVHCENALICDELGEeakregrvtahdyvasRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSP 246
Cdd:PRK04250 150 ---FEVDYA--CAPGIVSVHAEDPELIREFPE----------------RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 247 EGVEEVTRARQEGqdVTCESCPHYFVLDTDQFEEiGTLAKCSPPIRDLENQKGMWEKLFNgeIDCLVSDHSPCPPEMK-A 325
Cdd:PRK04250 209 DGLKLILKSNLPW--VSFEVTPHHLFLTRKDYER-NPLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLEDKeA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 326 GNimkawGGIAGLQSCMDVMFDEAvqKRGM-SLPMFGKLMATNAADIFGLQQKGrIAPGKDADFVFIQPNSSYVLTNDDL 404
Cdd:PRK04250 284 GA-----AGIPGLETEVPLLLDAA--NKGMiSLFDIVEKMHDNPARIFGIKNYG-IEEGNYANFAVFDMKKEWTIKAEEL 355
|
410 420
....*....|....*....|....*...
gi 16128496 405 EYRHKVSPYVGRTIGARITKTILRGDVI 432
Cdd:PRK04250 356 YTKAGWTPYEGFKLKGKVIMTILRGEVV 383
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
7-434 |
2.94e-45 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 162.92 E-value: 2.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 7 IKNGTVI--LENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
Cdd:PRK07627 5 IKGGRLIdpAAGTDRQADLYVAAGKIAAIGQAPAGfnADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 83 GGITTMI-----EMPLNQlPATVDRasieLKFDAAK---------GKLTIdaaqlgGLVSYNIDRLHELDEVGVVGFkcf 148
Cdd:PRK07627 85 GGVTSLVcppdtDPVLDE-PGLVEM----LKFRARNlnqahvyplGALTV------GLKGEVLTEMVELTEAGCVGF--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 149 vaTCGDRGIdndfrdVNDWQFFKGAQKLGELGQPVLVHCENALICDelgeeakreGRVTAHDYVASR------PVFTEVE 222
Cdd:PRK07627 151 --SQANVPV------VDTQVLLRALQYASTFGFTVWLRPLDAFLGR---------GGVAASGAVASRlglsgvPVAAETI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 223 AIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCE-SCPHYFVLDTDqfeeIGTL-AKC--SPPIRDLENQK 298
Cdd:PRK07627 214 ALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDvGVNHVHLIDVD----IGYFdSQFrlDPPLRSQRDRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 299 GMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAvQKRGMSLPMFGKLMATNAADIFGLqQKG 378
Cdd:PRK07627 290 AIRAALADGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLTLKWA-DEAKVPLARALARITSAPARVLGL-PAG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128496 379 RIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK07627 368 RLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFE 423
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
22-453 |
1.34e-43 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 158.10 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 22 DIAVKGGKIAAIGQDLGDAKEVmDASGLVVsPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATvD 101
Cdd:PRK01211 17 EIEVEDGKIKSIKKDAGNIGKK-ELKGAIL-PAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIK-D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 102 RASIELKFDAAKGKLTIDAaqlgGLVSYNIDRLHE-LDEVGvVGFKCFVA-TCGDRGIDNDFRDVndwqffkgaQKLGEL 179
Cdd:PRK01211 94 YNAFSDKLGRVAPKAYVDF----SLYSMETGNNALiLDERS-IGLKVYMGgTTNTNGTDIEGGEI---------KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 180 GQPVLVHCENALICDELGEEAKregrvTAHDYVASRPVFTEVEAIRRVLYLAKVAGcrlHVCHVSSPEGVEEVTRarqeg 259
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESK-----NLRDHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSIDVIGRFLR----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 260 qdvtcESCPHYFVLDTDQfeEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAgNIMKAWGGIAGLQ 339
Cdd:PRK01211 227 -----EVTPHHLLLNDDM--PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ-EFEYAKSGIIGVE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 340 SCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGrtIG 419
Cdd:PRK01211 299 TRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI-KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG--FD 374
|
410 420 430
....*....|....*....|....*....|....*
gi 16128496 420 ARITKT-ILRGDVIYDIEQGFPvAPKGQFILKHQQ 453
Cdd:PRK01211 375 AIFPSHvIMRGEVVIDNYELIS-ERTGKFVPKGGE 408
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
12-433 |
1.47e-42 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 155.58 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 12 VILENeARVVD----------IAVKGGKIAAIGQDLG-----DAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETG 76
Cdd:PRK09059 5 ILLAN-ARIIDpsrgldeigtVLIEDGVIVAAGKGAGnqgapEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 77 TRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTID----AAQLGGLVSYNIDRLHELDEVGVVGFkcfvaTC 152
Cdd:PRK09059 84 SRAAAAGGVTSIIMMP-DTDPVIDDVALVEFVKRTARDTAIVNihpaAAITKGLAGEEMTEFGLLRAAGAVAF-----TD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 153 GDRGIDNDfrdvndwQFFKGAQKLG-ELGQPVLVHCENAlicDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLA 231
Cdd:PRK09059 158 GRRSVANT-------QVMRRALTYArDFDAVIVHETRDP---DLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 232 KVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDC 311
Cdd:PRK09059 228 ALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 312 LVSDHSPCPPEMKAGNIMKAWGGIAGLQScmdvMFDEA---VQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADF 388
Cdd:PRK09059 308 IVSSHDPQDVDTKRLPFSEAAAGAIGLET----LLAAAlrlYHNGEVPLLRLIEALSTRPAEIFGL-PAGTLKPGAPADI 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16128496 389 VFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
Cdd:PRK09059 383 IVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
23-433 |
2.92e-33 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 129.05 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 23 IAVKGGKIAAIGQDLGDaKEVMDASGLVVSPGMVD--AHTHISEPGRSHWEGYETgtrAAAKGGITTMIEMPlNQLPATV 100
Cdd:PRK08417 1 IRIKDGKITEIGSDLKG-EEILDAKGKTLLPALVDlnVSLKNDSLSSKNLKSLEN---ECLKGGVGSIVLYP-DSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 101 DRASIELkfdaakgkltiDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDfRDVNDWQFFKGAQKLGELG 180
Cdd:PRK08417 76 NEIALEL-----------INSAQRELPMQIFPSIRALDEDGKLSNIATLLKKGAKALELS-SDLDANLLKVIAQYAKMLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 181 QPVLVHCENALICDElgeEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQ 260
Cdd:PRK08417 144 VPIFCRCEDSSFDDS---GVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 261 DVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQS 340
Cdd:PRK08417 221 KLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 341 CMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSSYVLtnDDleyrhKVSPYVGRTIGA 420
Cdd:PRK08417 301 YFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL-NSGEIEVGKEADLVLFDPNESTII--DD-----NFSLYSGDELYG 372
|
410
....*....|...
gi 16128496 421 RITKTILRGDVIY 433
Cdd:PRK08417 373 KIEAVIIKGKLYL 385
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
4-441 |
6.02e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 125.64 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKnGTVILENEARVVDIavkgGKIAAIGQDLGDAKEVMD-ASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
Cdd:PRK00369 2 ILWIK-GKAYLGKEIKEICI----NFDRRIKEIKSRCKPDLDlPQGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 83 GGITTMIEMPlNQLPATVDRASIELKfdaakgkltIDAAQLGGLVSYNI-----DRLHELDEVGVVGFKCFVatcgdrgi 157
Cdd:PRK00369 77 GGVTLVADMP-NTIPPLNTPEAITEK---------LAELEYYSRVDYFVysgvtKDPEKVDKLPIAGYKIFP-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 158 dndfRDVNDWQFFKGAQKLGELgqpVLVHCENALicdelgeeAKREGRVTAhdyvasRPVFTEVEAIRRVLYLAKVagcr 237
Cdd:PRK00369 139 ----EDLEREETFRVLLKSRKL---KILHPEVPL--------ALKSNRKLR------RNCWYEIAALYYVKDYQNV---- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 238 lHVCHVSSPEGVEEvtrARQEG--QDVTcescPHYFVLDTdqfeEIGTLAKCSPPIRDLENQKGMWEKLFngEIDCLVSD 315
Cdd:PRK00369 194 -HITHASNPRTVRL---AKELGftVDIT----PHHLLVNG----EKDCLTKVNPPIRDINERLWLLQALS--EVDAIASD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 316 HSPCPPEMKAGNIMKAWGGIAGLQSCmdVMFDEAVQKRG-MSLPMFGKLMATNAADIFGLQQkGRIAPGKDADFVFIQPN 394
Cdd:PRK00369 260 HAPHSSFEKLQPYEVCPPGIAALSFT--PPFIYTLVSKGiLSIDRAVELISTNPARILGIPY-GEIKEGYRANFTVIQFE 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16128496 395 ssyvltndDLEYRHKVS-----PYVGRTIGARITKTILRGDVIYDIEQGFPV 441
Cdd:PRK00369 337 --------DWRYSTKYSkvietPLDGFELKASVYATIVQGKLAYLEGEVFPV 380
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
53-445 |
1.06e-27 |
|
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: 112.93 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 53 PGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNId 132
Cdd:cd01316 6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMP-NTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATSTNA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 133 rlHELDEVG--VVGFKCFVATCGDRGIDNDfrdVNDWQffkgaqklgelgqpvlVHCENalicdelgeeakregrvtahd 210
Cdd:cd01316 84 --ATVGELAseAVGLKFYLNETFSTLILDK---ITAWA----------------SHFNA--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 211 YVASRPVFTEVEA--IRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCS 288
Cdd:cd01316 122 WPSTKPIVTHAKSqtLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 289 PPIRdlENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimKAWGGIAGLQSCMDVMFdEAVQKRGMSLPMFGKLMATNA 368
Cdd:cd01316 202 LPTR--EDQEALWENL--DYIDCFATDHAPHTLAEKTGN--KPPPGFPGVETSLPLLL-TAVHEGRLTIEDIVDRLHTNP 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128496 369 ADIFGLqqkgriaPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKG 445
Cdd:cd01316 275 KRIFNL-------PPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
19-425 |
6.93e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 112.00 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 19 RVVDIAVKGGKIAAIGQDLGD---AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTM-----IE 90
Cdd:PRK07369 20 RIADVLIEDGKIQAIEPHIDPippDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVailpdTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 91 MPLNQlPATVDR--------ASIELKFDAAkgkLTIDAA--QLgglvsyniDRLHELDEVGVVGFkcfvatCGDRGIDNd 160
Cdd:PRK07369 100 PPLDN-PATLARlqqqaqqiPPVQLHFWGA---LTLGGQgkQL--------TELAELAAAGVVGF------TDGQPLEN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 161 frdvndWQFFKGA-QKLGELGQPVLVHCENALICdelGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLH 239
Cdd:PRK07369 161 ------LALLRRLlEYLKPLGKPVALWPCDRSLA---GNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 240 VCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPC 319
Cdd:PRK07369 232 LMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 320 PPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGlQQKGRIAPGKDADFVFIQPNSSYVL 399
Cdd:PRK07369 312 TYEEKTVAFAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLG-QEPPSLAPGQPAELILFDPQKTWTV 390
|
410 420
....*....|....*....|....*.
gi 16128496 400 TNDDLEYRHKVSPYVGRTIGARITKT 425
Cdd:PRK07369 391 SAQTLHSLSRNTPWLGQTLKGRVLQT 416
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-394 |
4.43e-24 |
|
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: 103.53 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVI--LENEARVVDIAVKGGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHisEPGRSHWEGyetGTRAA 80
Cdd:cd01297 1 DLVIRNGTVVdgTGAPPFTADVGIRDGRIAAIGPILStSAREVIDAAGLVVAPGFIDVHTH--YDGQVFWDP---DLRPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMPLNQLPATVDRASIELKFDAAKGkltIDAAQLGGLVSYN-----IDRL----HELDEVGVVGFKCF-VA 150
Cdd:cd01297 76 SRQGVTTVVLGNCGVSPAPANPDDLARLIMLMEG---LVALGEGLPWGWAtfaeyLDALearpPAVNVAALVGHAALrRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 151 TCGDRG----------IDNDFRDvndwqffkgAQKLGELG-------QPVLVHCENALIcdELGEEAKREGRV--TAHDY 211
Cdd:cd01297 153 VMGLDAreateeelakMRELLRE---------ALEAGALGistglayAPRLYAGTAELV--ALARVAARYGGVyqTHVRY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 212 VASRPvfteVEAIRRVLYLAKVAGCRLHVCHVSS---------PEGVEEVTRARQEGQDVTCESCPHyfvldtdqfeEIG 282
Cdd:cd01297 222 EGDSI----LEALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADVYPY----------GAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 283 TLAKCSPPIRDlenqkgmweKLFNGEIDCLVSDHSPCppemkagnimKAWGGIAglqscmDVMFDEAVQKRGMSLPMFGK 362
Cdd:cd01297 288 SEDDVRRIMAH---------PVVMGGSDGGALGKPHP----------RSYGDFT------RVLGHYVRERKLLSLEEAVR 342
|
410 420 430
....*....|....*....|....*....|..
gi 16128496 363 LMATNAADIFGLQQKGRIAPGKDADFVFIQPN 394
Cdd:cd01297 343 KMTGLPARVFGLADRGRIAPGYRADIVVFDPD 374
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
2-269 |
1.10e-18 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 88.21 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 2 SFDLIIKNGTVIlENEAR---VVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGrshwegyetGTR 78
Cdd:PRK09061 18 PYDLVIRNGRVV-DPETGldaVRDVGIKGGKIAAVGTAAIEGDRTIDATGLVVAPGFIDLHAHGQSVA---------AYR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 79 AAAKGGITTMIEMPLNQLP--ATVDRASIE---LKFDAAKGKLTID-AAQLGGLVSYNIDRLHELdevgvvgfkcfvatc 152
Cdd:PRK09061 88 MQAFDGVTTALELEAGVLPvaRWYAEQAGEgrpLNYGASVGWTPARiAVLTGPQAEGTIADFGKA--------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 153 gdrgidndFRDvNDWQF-------FKGAQKL-------GELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVF 218
Cdd:PRK09061 153 --------LGD-PRWQEraatpaeLAEILELleqgldeGALGIGIGAGYAPGTGHKEYLELARLAARAGVPTYTHVRYLS 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128496 219 -----TEVEAIRRVLYLAKVAGCRLHVCHVSS------PEGVEEVTRARQEGQDVTCESCPH 269
Cdd:PRK09061 224 nvdprSSVDAYQELIAAAAETGAHMHICHVNStslrdiDRCLALVEKAQAQGLDVTTEAYPY 285
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-89 |
4.22e-18 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 85.60 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILE--NEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHIsepgrshwegYETGTR- 78
Cdd:COG3964 1 DLLIKGGRVIDPanGIDGVMDIAIKDGKIAAVAKDIdaAEAKKVIDASGLYVTPGLIDLHTHV----------FPGGTDy 70
|
90
....*....|....*..
gi 16128496 79 ------AAAKGGITTMI 89
Cdd:COG3964 71 gvdpdgVGVRSGVTTVV 87
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-388 |
1.25e-16 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 81.05 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVI--LENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHIsepgrshwegYETGT--- 77
Cdd:PRK09237 1 LLLRGGRVIdpANGIDGVIDIAIEDGKIAAVAGDIdgSQAKKVIDLSGLYVSPGWIDLHVHV----------YPGSTpyg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 78 ----RAAAKGGITTMiemplnqlpatVDRASI-ELKFDAAKgKLTIDAAQ----------LGGLVS----YNIDRLhELD 138
Cdd:PRK09237 71 depdEVGVRSGVTTV-----------VDAGSAgADNFDDFR-KLTIEASKtrvlaflnisRIGLLAqdelADLEDI-DAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 139 EVG---------VVGFKCFVATCGDRGidndfrdvNDWQFFKGAQKLGELGQ-PVLVHCENA-LICDELgEEAKREGRVT 207
Cdd:PRK09237 138 AVAeavkrnpdfIVGIKARMSSSVVGD--------NGIEPLELAKAIAAEANlPLMVHIGNPpPSLEEI-LELLRPGDIL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 208 AHDY--VASRPVfTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGqdvtcescphyFVLDTdqfeeIGTla 285
Cdd:PRK09237 209 THCFngKPNRIL-DEDGELRPSVLEALERGVRLDVGHGTASFSFKVAEAAIAAG-----------ILPDT-----IST-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 286 kcsppirdlenqkgmweklfngeidclvsdhspcppEMKAGNIMKawGGIAGLQSCMDVMFdeAVqkrGMSLPMFGKlMA 365
Cdd:PRK09237 270 ------------------------------------DIYCRNRIN--GPVYSLATVMSKFL--AL---GMPLEEVIA-AV 305
|
410 420
....*....|....*....|....
gi 16128496 366 T-NAADIFGLQQKGRIAPGKDADF 388
Cdd:PRK09237 306 TkNAADALRLPELGRLQVGSDADL 329
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-433 |
1.70e-16 |
|
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: 81.09 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARV---VDIAVKGGKIAAIGQDL----GDAKEVMDASGLVVSPGMVDAHTHISE-PGRSH------- 69
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALplpaYPADEVIDAKGKVVMPGLVNTHTHLAMtLLRGLaddlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 70 ---------WEGYET------GTRAA----AKGGITTMIEMpLNQLPATVDRASIELKFDAAKGKLTIDaaqLGGLVSYN 130
Cdd:cd01298 81 ewlkdliwpLERLLTeedvylGALLAlaemIRSGTTTFADM-YFFYPDAVAEAAEELGIRAVLGRGIMD---LGTEDVEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 131 idrlheldevgvvgfkcfvatcGDRGIDNDFRDVNDWQFFKGaqklgelgqpvlvhcenalicdelgeeakreGRVTAHd 210
Cdd:cd01298 157 ----------------------TEEALAEAERLIREWHGAAD-------------------------------GRIRVA- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 211 yVASRPVFT-EVEAIRRVLYLAKVAGCRLHvCHVSspEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF---------EE 280
Cdd:cd01298 183 -LAPHAPYTcSDELLREVAELAREYGVPLH-IHLA--ETEDEVEESLEKYGKRPVEYLEELGLLGPDVVlahcvwltdEE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 281 IGTLAkcsppirdlenqkgmweklfngEIDCLVSdHSPCPpemkagNiMKAWGGIAGLQSCMDV---------------- 344
Cdd:cd01298 259 IELLA----------------------ETGTGVA-HNPAS------N-MKLASGIAPVPEMLEAgvnvglgtdgaasnnn 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 345 --MFDEA-----VQKRG----MSLPMFGKL-MAT-NAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLeyrhkVS 411
Cdd:cd01298 309 ldMFEEMrlaalLQKLAhgdpTALPAEEALeMATiGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPVHDP-----IS 383
|
490 500
....*....|....*....|..
gi 16128496 412 PYVGRTIGARITKTILRGDVIY 433
Cdd:cd01298 384 HLVYSANGGDVDTVIVNGRVVM 405
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-434 |
9.92e-15 |
|
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: 75.63 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVV----DIAVKGGKIAAIG-----QDLGDAKEVMDASGLVVSPGMVDAHTHISE---------- 64
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVledgAVLVEDGRIAAVGpgaelPARYPAAEVIDAGGKLVLPGLVNTHTHLPQtllrgladdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 65 -----------PGRSHW--EGYETGTRAAA----KGGITTMIEMplnqlpATVDRASIELKFDAAKgkltidAAQLGGLV 127
Cdd:COG0402 81 plldwleeyiwPLEARLdpEDVYAGALLALaemlRSGTTTVADF------YYVHPESADALAEAAA------EAGIRAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 128 SYnidrlheldevgvvgfkcfvaTCGDRGIDNDfrdvndwqffkgaqkLGELGQPVLVHCEnALIcDELgeEAKREGRVT 207
Cdd:COG0402 149 GR---------------------GLMDRGFPDG---------------LREDADEGLADSE-RLI-ERW--HGAADGRIR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 208 AHdyVASRPVFT-EVEAIRRVLYLAKVAGCRLHVcHVSspEGVEEVTRARQE-GQDVTcescpHYF----VLD------- 274
Cdd:COG0402 189 VA--LAPHAPYTvSPELLRAAAALARELGLPLHT-HLA--ETRDEVEWVLELyGKRPV-----EYLdelgLLGprtllah 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 275 ----TDqfEEIGTLAK---------CS--------PPIRDLEnQKGMweKLfngeidCLVSDHSPCPP------EMKAGN 327
Cdd:COG0402 259 cvhlTD--EEIALLAEtgasvahcpTSnlklgsgiAPVPRLL-AAGV--RV------GLGTDGAASNNsldmfeEMRLAA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 328 IM-KAWGGIAglqSCMDVmfDEAVQkrgmslpmfgklMAT-NAADIFGLQQK-GRIAPGKDADFVFIQPNSSYVLTNDDL 404
Cdd:COG0402 328 LLqRLRGGDP---TALSA--REALE------------MATlGGARALGLDDEiGSLEPGKRADLVVLDLDAPHLAPLHDP 390
|
490 500 510
....*....|....*....|....*....|
gi 16128496 405 eyrhkVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:COG0402 391 -----LSALVYAADGRDVRTVWVAGRVVVR 415
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-62 |
2.16e-14 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 75.14 E-value: 2.16e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128496 3 FDLIIKNGTVI--LENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHI 62
Cdd:COG1001 5 ADLVIKNGRLVnvFTGEILEGDIAIAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-434 |
1.49e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.92 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVV---DIAVKGGKIAAIGQDLG----DAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETG 76
Cdd:COG1228 9 TLLITNATLVDGTGGGVIengTVLVEDGKIAAVGPAADlavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 77 T---------------RAAAKGGITTMIEMPlnqlpatvdRASIELKFDAAKGKLtidaAQLGGlvsyniDRLheldevg 141
Cdd:COG1228 89 GitptvdlvnpadkrlRRALAAGVTTVRDLP---------GGPLGLRDAIIAGES----KLLPG------PRV------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 142 vvgfkcFVAtcgDRGIDndfrdvndwqFFKGAQKLGElgqpvlVHCENALicdelgEEAKREGrvtAhDYV-----ASRP 216
Cdd:COG1228 143 ------LAA---GPALS----------LTGGAHARGP------EEARAAL------RELLAEG---A-DYIkvfaeGGAP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 217 VFTEvEAIRRVLYLAKVAGcrLHV-CHVSSPEGVEEVTRA-----------RQEGQDVTCESCPHYFVLDTDQFEEIGTL 284
Cdd:COG1228 188 DFSL-EELRAILEAAHALG--LPVaAHAHQADDIRLAVEAgvdsiehgtylDDEVADLLAEAGTVVLVPTLSLFLALLEG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 285 AKCSPPIRDLENQKGMWE---KLFNGEIDCLVsdHSPCPPEMKAG-------NIMKAWGgiaglqscMDVMfdEAVQkrg 354
Cdd:COG1228 265 AAAPVAAKARKVREAALAnarRLHDAGVPVAL--GTDAGVGVPPGrslhrelALAVEAG--------LTPE--EALR--- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 355 mslpmfgklMAT-NAADIFGLQQK-GRIAPGKDADFVfiqpnssyVLTNDDLEYRHKVspyvgrtigARITKTILRGDVI 432
Cdd:COG1228 330 ---------AATiNAAKALGLDDDvGSLEPGKLADLV--------LLDGDPLEDIAYL---------EDVRAVMKDGRVV 383
|
..
gi 16128496 433 YD 434
Cdd:COG1228 384 DR 385
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-432 |
2.47e-12 |
|
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: 67.91 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 50 VVSPGMVDAHTHIS--------EPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPAtvdrasIELKFDAAkgkltiDAA 121
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTG------IEALLEAA------EEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 122 QLGglvsynidrlheldeVGVVGFKCFVATcgdRGIDNDFRDVNDwQFFKGAQKLGELGqpvlvhcenalicdelgeeak 201
Cdd:pfam01979 69 PLG---------------LRFLGPGCSLDT---DGELEGRKALRE-KLKAGAEFIKGMA--------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 202 rEGRVTAHDYVASRPVFTEvEAIRRVLYLAKVAGCRLHVcHVSSPEGVEEVTRARqEGQDVTC----ESCPHYFVLDTDQ 277
Cdd:pfam01979 109 -DGVVFVGLAPHGAPTFSD-DELKAALEEAKKYGLPVAI-HALETKGEVEDAIAA-FGGGIEHgthlEVAESGGLLDIIK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 278 F----------EEIGTLAK-------CSPPIRDLENQKG---MWEKLFNGEIDCLVSDHSPcppemkAGNIMKAWGGIAg 337
Cdd:pfam01979 185 LilahgvhlspTEANLLAEhlkgagvAHCPFSNSKLRSGriaLRKALEDGVKVGLGTDGAG------SGNSLNMLEELR- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 338 lqscmDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVFIQPnssyvltnddleyrHKVSPYVGR 416
Cdd:pfam01979 258 -----LALELQFDPEGGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVVVDL--------------DPLAAFFGL 318
|
410
....*....|....*.
gi 16128496 417 TIGARITKTILRGDVI 432
Cdd:pfam01979 319 KPDGNVKKVIVKGKIV 334
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-395 |
2.88e-12 |
|
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: 67.67 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 23 IAVKGGKIAAIG------QDLGDAKEVMDASGLVVSPGMVDAHTHISEPG-RSH-----WEGYETGTRAAAKGGITTMIE 90
Cdd:cd01296 1 IAIRDGRIAAVGpaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGdRVDefaarLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 91 mplnqlpATVDRASIELKfdaAKGKLTIDAAQLGGLVS------YNIDR---------LHELDEVGVVGfkcFVAT-CGD 154
Cdd:cd01296 81 -------ATRAASEDELF---ASALRRLARMLRHGTTTvevksgYGLDLetelkmlrvIRRLKEEGPVD---LVSTfLGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 155 RGIDNDFRDvnDWQFFKgaqklgelgqpvlvhcenaLICDELGEEAKREGRVTAHDYVASRPVFTeVEAIRRVLYLAKVA 234
Cdd:cd01296 148 HAVPPEYKG--REEYID-------------------LVIEEVLPAVAEENLADFCDVFCEKGAFS-LEQSRRILEAAKEA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 235 G--CRLHVCHVSSPEGVEevtrarqEGQDVTCESCPHYFVLDTDQFE---EIGTLA-----------KCSPPIRDLenqk 298
Cdd:cd01296 206 GlpVKIHADELSNIGGAE-------LAAELGALSADHLEHTSDEGIAalaEAGTVAvllpgtafslrETYPPARKL---- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 299 gmwekLFNGEIDCLVSDHSP-CPPEmkagnimkawggiaglqSCMDVMFDEAVqkRGMSLPMFGKLMAT--NAADIFGLQ 375
Cdd:cd01296 275 -----IDAGVPVALGTDFNPgSSPT-----------------SSMPLVMHLAC--RLMRMTPEEALTAAtiNAAAALGLG 330
|
410 420
....*....|....*....|.
gi 16128496 376 QK-GRIAPGKDADFVFIQPNS 395
Cdd:cd01296 331 ETvGSLEVGKQADLVILDAPS 351
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
3-62 |
6.16e-12 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 66.97 E-value: 6.16e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128496 3 FDLIIKNGTviLENEARVVDIAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHI 62
Cdd:PRK07572 2 FDLIVRNAN--LPDGRTGIDIGIAGGRIAAVEPGLqAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-371 |
6.76e-12 |
|
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: 65.82 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 56 VDAHTHISEPGRSHW------------------EGYETGTRAAAKGGITTMIEMPLNqLPATVDRASIELKFDAAKGKLT 117
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGST-PPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 118 IDAAQLGGLVSYN-----------IDRLHELDEVGVVGFKCFVAtcgdrgidNDFRDVNDWQFFKGAQKLGELGQPVLVH 186
Cdd:cd01292 81 IRVVLGLGIPGVPaavdedaeallLELLRRGLELGAVGLKLAGP--------YTATGLSDESLRRVLEEARKLGLPVVIH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 187 CENALIcdelgeeakregrvtahdyvasrpvftEVEAIRRVLYLAKVaGCRLHVCHVSSPEgVEEVTRARQEGqdVTCES 266
Cdd:cd01292 153 AGELPD---------------------------PTRALEDLVALLRL-GGRVVIGHVSHLD-PELLELLKEAG--VSLEV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 267 CPHYFVLDTdqfeeigtlakcsppiRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWggiaglqscmdvmf 346
Cdd:cd01292 202 CPLSNYLLG----------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL-------------- 251
|
330 340
....*....|....*....|....*
gi 16128496 347 dEAVQKRGMSLPMFGKLMATNAADI 371
Cdd:cd01292 252 -LKVLRLGLSLEEALRLATINPARA 275
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-68 |
3.21e-11 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 65.21 E-value: 3.21e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128496 4 DLIIKNGTVI-LENEARVVD-IAVKGGKIAAIGQD------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRS 68
Cdd:COG1574 9 DLLLTNGRIYtMDPAQPVAEaVAVRDGRIVAVGSDaevralAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLA 81
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-88 |
5.70e-10 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 60.96 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHT-----HIS-EPGrSHWEgYETGT 77
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTdnlekHLApRPG-VDWP-ADAAL 80
|
90
....*....|....*
gi 16128496 78 RAA----AKGGITTM 88
Cdd:PRK15446 81 AAHdaqlAAAGITTV 95
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-100 |
2.74e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 58.57 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 6 IIKNGTVILENEARV-VDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTH------ISEPGrshWEGYETGTR 78
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHggggvdFMDGT---PEALRTIAR 77
|
90 100
....*....|....*....|..
gi 16128496 79 AAAKGGITTMiemplnqLPATV 100
Cdd:COG1820 78 AHARHGTTSF-------LPTTI 92
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-61 |
5.51e-09 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 58.09 E-value: 5.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128496 4 DLIIKNGTVILENEARVV---DIAVKGGKIAAIGQ--DLGDAKEVMDASGLVVSPGMVDAHTH 61
Cdd:PRK07228 2 TILIKNAGIVTMNAKREIvdgDVLIEDDRIAAVGDrlDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
5-62 |
6.15e-09 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 57.64 E-value: 6.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128496 5 LIIKNGTVILENEARVV----DIAVKGGKIAAIGQ--DLGDA---KEVMDASGLVVSPGMVDAHTHI 62
Cdd:PRK07203 2 LLIGNGTAITRDPAKPViedgAIAIEGNVIVEIGTtdELKAKypdAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-90 |
6.39e-09 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 57.46 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 1 MSFDLIIKNGtVILENEARVV---DIAVKGGKIAAIGQDlGDAKE--VMDASGLVVSPGMVDAHTHIsepgrsHWEGYET 75
Cdd:PRK12394 1 MKNDILITNG-HIIDPARNINeinNLRIINDIIVDADKY-PVASEtrIIHADGCIVTPGLIDYHAHV------FYDGTEG 72
|
90
....*....|....*...
gi 16128496 76 GTR---AAAKGGITTMIE 90
Cdd:PRK12394 73 GVRpdmYMPPNGVTTVVD 90
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-90 |
1.38e-08 |
|
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: 56.18 E-value: 1.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128496 22 DIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHIsepgrsHWEGYETGTRA---AAKGGITTMIE 90
Cdd:cd01307 1 DVAIENGKIAAVGAALaaPAATQIVDAGGCYVSPGWIDLHVHV------YQGGTRYGDRPdmiGVKSGVTTVVD 68
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
6-126 |
1.49e-08 |
|
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: 56.49 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 6 IIKNgTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHI-----SEPGRSHWEGYETGTR 78
Cdd:cd01293 1 LLRN-ARLADGGTALVDIAIEDGRIAAIGPALavPPDAEEVDAKGRLVLPAFVDPHIHLdktftGGRWPNNSGGTLLEAI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16128496 79 aaakggITTMIEMPLNQLPATVDRASIELKFDAAKGKLTI-------DAAQLGGL 126
Cdd:cd01293 80 ------IAWEERKLLLTAEDVKERAERALELAIAHGTTAIrthvdvdPAAGLKAL 128
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-61 |
2.85e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 55.58 E-value: 2.85e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARVV--DIAVKGGKIAAIGQDLGD-AKEVMDASGLVVSPGMVDAHTH 61
Cdd:PRK08393 3 ILIKNGYVIYGENLKVIraDVLIEGNKIVEVKRNINKpADTVIDASGSVVSPGFINAHTH 62
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
2-70 |
7.00e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 54.17 E-value: 7.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128496 2 SFDLIIKNgtVILENEARVvDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHisePGRSHW 70
Cdd:PRK05985 1 MTDLLFRN--VRPAGGAAV-DILIRDGRIAAIGPALAAppGAEVEDGGGALALPGLVDGHIH---LDKTFW 65
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-100 |
9.14e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 53.74 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARVVDIAVKGGKIAAIG--QDLGDAKEVMDASGLVVSPGMVDAHTHisepGR-------SHWEGYET 75
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGpeDELEEADEIIDLKGQYLVPGFIDIHIH----GGggadfmdGTAEALKT 76
|
90 100
....*....|....*....|....*
gi 16128496 76 GTRAAAKGGITTMiemplnqLPATV 100
Cdd:cd00854 77 IAEALAKHGTTSF-------LPTTV 94
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-89 |
9.24e-08 |
|
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: 54.26 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIG-------QD-------LGDAKEVMDASGLVVSPGMVDAHTHISEPgRSH 69
Cdd:cd00375 66 DLVITNALIIDYTGIYKADIGIKDGRIVAIGkagnpdiMDgvtpnmiVGPSTEVIAGEGKIVTAGGIDTHVHFICP-QQI 144
|
90 100
....*....|....*....|
gi 16128496 70 WEgyetgtraAAKGGITTMI 89
Cdd:cd00375 145 EE--------ALASGITTMI 156
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
6-84 |
1.59e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 53.47 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 6 IIKNGTVILENEA----RVVDIAVKGGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHIsepgrshWegyETGTRAA 80
Cdd:PRK08204 5 LIRGGTVLTMDPAigdlPRGDILIEGDRIAAVAPSIEaPDAEVVDARGMIVMPGLVDTHRHT-------W---QSVLRGI 74
|
....
gi 16128496 81 AKGG 84
Cdd:PRK08204 75 GADW 78
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
7-62 |
1.90e-07 |
|
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: 53.19 E-value: 1.90e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128496 7 IKNGTVI---LENEARVVDIAVKGGKIAAIGQDLGDAKeVMDASGLVVSPGMVDAHTHI 62
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVESSSGAKPAK-VIDASGKVVMAGGVDMHSHI 58
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-63 |
3.26e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 52.44 E-value: 3.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128496 4 DLIIKNGTVILENEARVVD--IAVKGGKIAAIGQDL-GDAKEVMDASGLVVSPGMVDAHTHIS 63
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKgsVVIEDGTITEVSESTpGDADTVIDAKGSVVMPGLVNTHTHAA 65
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
5-89 |
3.42e-07 |
|
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: 52.01 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL----GDAKEVMDASGLVVSPGMVDAHTHISEPGRShwEGYETGT--- 77
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLnlpgYENVTVVDLHGKILVPGFIDQHVHIIGGGGE--GGPSTRTpev 79
|
90
....*....|....
gi 16128496 78 --RAAAKGGITTMI 89
Cdd:cd01308 80 tlSDLTTAGVTTVV 93
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
2-146 |
3.47e-07 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 52.59 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 2 SFDLIIKNGTVILENEARVVDIAVKGGKIAAIG-------QD-------LGDAKEVMDASGLVVSPGMVDAHTHISEPgr 67
Cdd:PRK13985 64 ELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmQDgvknnlsVGPATEALAGEGLIVTAGGIDTHIHFISP-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 68 shwegyeTGTRAAAKGGITTMI---EMPLNQLPATV---DRASIELKFDAAKgKLTIDAAQLGGLVSYNIDRLHELDEVG 141
Cdd:PRK13985 142 -------QQIPTAFASGVTTMIgggTGPADGTNATTitpGRRNLKWMLRAAE-EYSMNLGFLGKGNSSNDASLADQIEAG 213
|
....*
gi 16128496 142 VVGFK 146
Cdd:PRK13985 214 AIGFK 218
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-62 |
8.64e-07 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 51.04 E-value: 8.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128496 1 MSfdLIIKNGTVILENEARVV---DIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHI 62
Cdd:PRK06380 1 MS--ILIKNAWIVTQNEKREIlqgNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHV 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
28-433 |
1.32e-06 |
|
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: 50.39 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 28 GKIAAIGQ--DLGDAKEVMDASGLVVSPGMVDAHTHI---SEPGRshWEGYETGT---------RA-------------A 80
Cdd:cd01309 2 GKIVAVGAeiTTPADAEVIDAKGKHVTPGLIDAHSHLgldEEGGV--RETSDANEetdpvtphvRAidginpddeafkrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 81 AKGGITTMIEMPLNQLP-----ATVDRASIELKFDAAKGKLTIDAAqLGglvsYNIDRLHEldevgvvGFKCFVATcgdR 155
Cdd:cd01309 80 RAGGVTTVQVLPGSANLiggqgVVIKTDGGTIEDMFIKAPAGLKMA-LG----ENPKRVYG-------GKGKEPAT---R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 156 -GIDNDFRDvndwQFFKgAQKLGELGQPVLVHCENALICD----ELGEEAKREGRVTAHDYVASrpvfteveAIRRVLYL 230
Cdd:cd01309 145 mGVAALLRD----AFIK-AQEYGRKYDLGKNAKKDPPERDlkleALLPVLKGEIPVRIHAHRAD--------DILTAIRI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 231 AKVAGCRLHVCHVSspEGVEEVTRARQEGQDVTcescphYFVLDTdqfeeigtlakcsPPIRDLENQKGMWEK---LFNG 307
Cdd:cd01309 212 AKEFGIKITIEHGA--EGYKLADELAKHGIPVI------YGPTLT-------------LPKKVEEVNDAIDTNaylLKKG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 308 EID-CLVSDHspcpPEMKAGNIMkawggiagLQSCMDVMFdeavqkrGMSLPMFGKLMATNAADIFGLQQK-GRIAPGKD 385
Cdd:cd01309 271 GVAfAISSDH----PVLNIRNLN--------LEAAKAVKY-------GLSYEEALKAITINPAKILGIEDRvGSLEPGKD 331
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16128496 386 ADFVfiqpnssyVLTNDDLEYrhkvspyvgrtiGARITKTILRGDVIY 433
Cdd:cd01309 332 ADLV--------VWNGDPLEP------------TSKPEQVYIDGRLVY 359
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
4-89 |
1.62e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 50.56 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVILENEARVVDIAVKGGKIAAIG-------QD-----LGDAKEVMDASGLVVSPGMVDAHTHISEPGRshwe 71
Cdd:PRK13207 68 DTVITNALILDHWGIVKADIGIKDGRIVAIGkagnpdiQDgvdiiIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQ---- 143
|
90
....*....|....*...
gi 16128496 72 gyetgTRAAAKGGITTMI 89
Cdd:PRK13207 144 -----IEEALASGVTTMI 156
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-68 |
1.73e-06 |
|
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: 50.00 E-value: 1.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16128496 22 DIAVKGGKIAAIGQD------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRS 68
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakalKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLS 53
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-89 |
4.05e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.93 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTVIlENEARVV--DIAVKGGKIAAIGQ------------DL--GDAKEVMDASGLVVSPGMVDAHTHISEPGR 67
Cdd:PRK13308 69 DFVLCNVTVI-DPVLGIVkgDIGIRDGRIVGIGKagnpdimdgvdpRLvvGPGTDVRPAEGLIATPGAIDVHVHFDSAQL 147
|
90 100
....*....|....*....|...
gi 16128496 68 S-HwegyetgtraAAKGGITTMI 89
Cdd:PRK13308 148 VdH----------ALASGITTML 160
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
5-79 |
6.13e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 48.31 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVIL-ENEARVVD----IAVKGGKIAAIG---QDLGDAKEVMDASGLVVSPGMVDAHTHIsepgrshwegYETG 76
Cdd:PRK08203 3 LWIKNPLAIVtMDAARREIadggLVVEGGRIVEVGpggALPQPADEVFDARGHVVTPGLVNTHHHF----------YQTL 72
|
...
gi 16128496 77 TRA 79
Cdd:PRK08203 73 TRA 75
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
307-394 |
3.29e-05 |
|
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: 45.73 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 307 GEIDCLVSDHSPcppemkagnimkawggiaglQSCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDA 386
Cdd:cd01306 246 GLLDILSSDYVP--------------------ASLLHAAF-RLADLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRA 304
|
....*...
gi 16128496 387 DFVFIQPN 394
Cdd:cd01306 305 DLILVDDM 312
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
4-62 |
3.58e-05 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 45.83 E-value: 3.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128496 4 DLIIKNGTVILE----NEARV--VDIAVKGGKIAAIGQ---DLGDakEVMDASGLVVSPGMVDAHTHI 62
Cdd:PRK12393 3 SLLIRNAAAIMTglpgDAARLggPDIRIRDGRIAAIGAltpLPGE--RVIDATDCVVYPGWVNTHHHL 68
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
42-433 |
6.41e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.21 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 42 EVMDASGLVVSPGMVDAHTHISEPG--------------------------------------RSHWEGYeTGTRAAAKG 83
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGlnlrelrlpdvlpnavvkgqagrtpkgrwlvgegwdeaQFAETRF-PYALADLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 84 GI------------------TTMIEMpLNQLPATVDRASIELKFDA----AKGKLTIDAAQLGGLVSynIDRLHELDEVG 141
Cdd:pfam07969 80 VApdgpvllralhthaavanSAALDL-AGITKATEDPPGGEIARDAngegLTGLLREGAYALPPLLA--REAEAAAVAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 142 VVGFKCFVATCGDRGIDNDFR--DVNDWQFFKGAQKLGELGQPV----LVHCENALICDELGEEAKREG--------RVT 207
Cdd:pfam07969 157 LAALPGFGITSVDGGGGNVHSldDYEPLRELTAAEKLKELLDAPerlgLPHSIYELRIGAMKLFADGVLgsrtaaltEPY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 208 AHDYVASRPVFTEvEAIRRVLYLAKVAGCRLHvCHVSSPEGVEEVTRA-----RQEGQD--VTCESCPHYFVLDTDQFEE 280
Cdd:pfam07969 237 FDAPGTGWPDFED-EALAELVAAARERGLDVA-IHAIGDATIDTALDAfeavaEKLGNQgrVRIEHAQGVVPYTYSQIER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 281 IGTLAKCSP------------PIRDLENQKGMW-----EKLFNGEIDCLVSDHSPCP----PEMKAGNIMKAWGGIAGLQ 339
Cdd:pfam07969 315 VAALGGAAGvqpvfdplwgdwLQDRLGAERARGltpvkELLNAGVKVALGSDAPVGPfdpwPRIGAAVMRQTAGGGEVLG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 340 SCMDVMFDEAVQkrgmslpmfgkLMATNAADIFGLQQ-KGRIAPGKDADFVfiqpnssyVLTNDDLeyrhKVSPYVGRTI 418
Cdd:pfam07969 395 PDEELSLEEALA-----------LYTSGPAKALGLEDrKGTLGVGKDADLV--------VLDDDPL----TVDPPAIADI 451
|
490
....*....|....*
gi 16128496 419 GARitKTILRGDVIY 433
Cdd:pfam07969 452 RVR--LTVVDGRVVY 464
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
342-392 |
8.78e-05 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 44.52 E-value: 8.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16128496 342 MDVMFDEAVQKrGMSlPMFGKLMAT-NAADIFGLQQKGRIAPGKDADFVFIQ 392
Cdd:cd01295 223 LDYIVRRAIEA-GIP-PEDAIQMATiNPAECYGLHDLGAIAPGRIADIVILD 272
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
4-89 |
1.25e-04 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 44.44 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIKNGTV--ILENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEgYETGTRA 79
Cdd:PRK10027 31 DYIIDNVSIldLINGGEISGPIVIKGRYIAGVGAEYADapALQRIDARGATAVPGFIDAHLHIESSMMTPVT-FETATLP 109
|
90
....*....|
gi 16128496 80 AakgGITTMI 89
Cdd:PRK10027 110 R---GLTTVI 116
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
333-389 |
2.83e-04 |
|
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: 42.95 E-value: 2.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128496 333 GGIAGLQSCMDVMFDEAVQKRGMSLPmFGKLMAT-NAADIFGL-QQKGRIAPGKDADFV 389
Cdd:cd00854 302 GTLAGSTLTMDQAVRNMVKWGGCPLE-EAVRMASlNPAKLLGLdDRKGSLKPGKDADLV 359
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
333-389 |
2.84e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 42.78 E-value: 2.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128496 333 GGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFV 389
Cdd:COG1820 300 GTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLdDRKGSIAPGKDADLV 357
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
4-89 |
9.82e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 41.62 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 4 DLIIkNGTVILENEARV-VDIAVKGGKIAAIGQ------------DL--GDAKEVMDASGLVVSPGMVDAHTHISEPGRS 68
Cdd:PRK13206 72 DTVI-TGAVILDHWGIVkADVGIRDGRIVAIGKagnpdimdgvhpDLviGPSTEIIAGNGRILTAGAIDCHVHFICPQIV 150
|
90 100
....*....|....*....|.
gi 16128496 69 HwegyetgtrAAAKGGITTMI 89
Cdd:PRK13206 151 D---------EALAAGITTLI 162
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
21-62 |
1.31e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.12 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 16128496 21 VDIAVKGGKIAAI---GQDLGDAKEVmDASGLVVSPGMVDAHTHI 62
Cdd:PRK07583 41 VDIEIADGKIAAIlpaGGAPDELPAV-DLKGRMVWPCFVDMHTHL 84
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
12-61 |
3.11e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 39.89 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 16128496 12 VILENEArvvdIAVKGGKIAAIG-----QDLGDAKEVMDASGLVVSPGMVDAHTH 61
Cdd:PRK09045 24 VVLEDHA----VAIRDGRIVAILpraeaRARYAAAETVELPDHVLIPGLINAHTH 74
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
8-107 |
4.29e-03 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 39.22 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 8 KNGTVILENEARVVDIAVKGGKIAAI---GQDLGDAKEVMDASGLVVSPGMVDAHTHISEPgrshwegYETGTRAAA--K 82
Cdd:PRK06846 19 YENGVIVQTETALCTLEIQDGKIVAIrpnKQVPDATLPTYDANGLLMLPAFREMHIHLDKT-------YYGGPWKACrpA 91
|
90 100 110
....*....|....*....|....*....|..
gi 16128496 83 GGITTMI-----EMPlNQLPATVDRAS--IEL 107
Cdd:PRK06846 92 KTIQDRIeleqkELP-ELLPTTQERAEklIEL 122
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
5-62 |
6.10e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 38.87 E-value: 6.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 5 LIIKNGTVI--LENEARVVDIAVKGGKIAAIGQDLgDAKEVMDASGLVVsPGMVDAHTHI 62
Cdd:PRK07213 2 LVYLNGNFLygEDFEPKKGNLVIEDGIIKGFTNEV-HEGNVIDAKGLVI-PPLINAHTHI 59
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
3-146 |
7.90e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 38.70 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 3 FDLIIKNGTVIlenEARV----VDIAVKGGKIAAIGQD--------------LGDAKEVMDASGLVVSPGMVDAHTHISE 64
Cdd:PRK13309 68 LDLVITNVTIV---DARLgvikADVGIRDGKIVGIGKSgnpstmdgvtqgmvVGVSTDAISGEHLILTAAGIDTHIHLIS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128496 65 PGRSHwegyetgtrAAAKGGITTMIEMPL------NQLPATVDRASIELKFDAAKGkLTIDAAQLGGLVSYNIDRLHELD 138
Cdd:PRK13309 145 PQQAY---------HALSNGVTTFFGGGIgptdgtNGTTVTPGPWNIRQMLRSIEG-LPVNVGILGKGNSYGRGPLLEQA 214
|
....*...
gi 16128496 139 EVGVVGFK 146
Cdd:PRK13309 215 IAGVAGYK 222
|
|
| |
