|
Name |
Accession |
Description |
Interval |
E-value |
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
2-384 |
0e+00 |
|
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: 661.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 2 WTLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAKGEVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPEVQ 81
Cdd:cd01308 1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 82 LSQLTRAGITTVVGCLGTDSISRSMEELLVKANALEEEGLTCFVYSGGYQA-DRMIFDTLRKDLVLIDKVIGAGEIAISD 160
Cdd:cd01308 81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVpTRTITGSIRKDLLLIDKVIGVGEIAISD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 161 HRSAQPQKSELEHLAAEARVGGMLGDKAGVVHIHLGEGKRGLSPILKIIEETEIPISQFMPTHINRKETLLEQGVEFLKA 240
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 241 GGTIDLTAGCDDF---EPHLQVPFVLKALYEQGLLNDRVTVTSDGNGSLPQFNEAGILVGMGIGSVHVLWRDIREAVLRY 317
Cdd:cd01308 241 GGTIDLTSSIDPQfrkEGEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 698317205 318 GIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSDDLMIEQVWAKGRVMIRNRKPVVLGVYE 384
Cdd:cd01308 321 DIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
2-384 |
1.53e-161 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 459.25 E-value: 1.53e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 2 WTLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPP-YAKGE-VYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPE 79
Cdd:TIGR01975 1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKdFVPNCvVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 80 VQLSQLTRAGITTVVGCLGTDSISRSMEELLVKANALEEEGLTCFVYSGGYQAD-RMIFDTLRKDLVLIDKVIGAGEIAI 158
Cdd:TIGR01975 81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPsRTITGSVESDLLLIDKVIGVGEIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 159 SDHRSAQPQKSELEHLAAEARVGGMLGDKAGVVHIHLGEGKRGLSPILKIIEETEIPISQFMPTHINRKETLLEQGVEFL 238
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 239 KAGGTIDLTAGCDdfEPHLQVPFV-----LKALYEQGLLNDRVTVTSDGNGSLPQFNEAGILVGMGIGSVHVLWRDIREA 313
Cdd:TIGR01975 241 KKGGTIDLTSSID--PQFRKEGEVapaegIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 314 VLRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSDDLMIEQVWAKGRVMIRNRKPVVLGVYE 384
Cdd:TIGR01975 319 VKDGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-374 |
4.04e-31 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 122.38 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLF---APEPLQERDLLLVGNRIAALGDDLSLPPYAKGEVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSR--- 76
Cdd:COG1228 10 LLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAggg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 77 -TPEVQLSQLT--------RAGITTVVGCLGT-----DSISRSMEELLVKANAL-EEEGLTCFvysGGY------QADRM 135
Cdd:COG1228 90 iTPTVDLVNPAdkrlrralAAGVTTVRDLPGGplglrDAIIAGESKLLPGPRVLaAGPALSLT---GGAhargpeEARAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 136 IFDTLRKDLVLIDKVIGAGEIAISDHrsaqpqksELEHLAAEARVGGMLgdkagvVHIHLGegkrGLSPIL-------KI 208
Cdd:COG1228 167 LRELLAEGADYIKVFAEGGAPDFSLE--------ELRAILEAAHALGLP------VAAHAH----QADDIRlaveagvDS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 209 IEeteipisqfmptHINRketLLEQGVEFLKAGGTIDLTAGCDDFEPHLQVPFVLKALYEQGLLNDRVTvtsdgngSLPQ 288
Cdd:COG1228 229 IE------------HGTY---LDDEVADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALA-------NARR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 289 FNEAGILVGMG----IGSVHV--LWRDIREAVlRYGIPLDTALRTITSNPARILQLKNK-GMIREGFDGDLVALSDDLM- 360
Cdd:COG1228 287 LHDAGVPVALGtdagVGVPPGrsLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDPLe 365
|
410 420
....*....|....*....|.
gi 698317205 361 -------IEQVWAKGRVMIRN 374
Cdd:COG1228 366 diayledVRAVMKDGRVVDRS 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-353 |
5.61e-18 |
|
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: 85.14 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTpevqls 83
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA--EVIDATGLLVLPGLIDLHVHLREPGLEHKEDIET------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 84 qLTRA----GITTVVgCL-----GTDSISRsMEELLVKAN-------------------------ALEEEGLTCFVYSGG 129
Cdd:COG0044 73 -GTRAaaagGVTTVV-DMpntnpVTDTPEA-LEFKLARAEekalvdvgphgaltkglgenlaelgALAEAGAVAFKVFMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 130 YQADRMIFD--TLRK-----------------DLVLIDK-VIGAGEIAISDHRSAQPQKSELEHLaaeARVgGMLGDKAG 189
Cdd:COG0044 150 SDDGNPVLDdgLLRRaleyaaefgalvavhaeDPDLIRGgVMNEGKTSPRLGLKGRPAEAEEEAV---ARD-IALAEETG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 190 vVHIHLgegkrglspilkiieeteipisqfmpTHINRKEtlleqGVEFL---KAGGtIDLTAG------------CDDFE 254
Cdd:COG0044 226 -ARLHI--------------------------VHVSTAE-----AVELIreaKARG-LPVTAEvcphhltltdedLERYG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 255 PHLQV--PfvLK------ALYEqGLLNDRV-TVTSDGNgslPQ--------FNEA--GIlvgmgIG---SVHVLWrdiRE 312
Cdd:COG0044 273 TNFKVnpP--LRteedreALWE-GLADGTIdVIATDHA---PHtleekelpFAEApnGI-----PGletALPLLL---TE 338
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 698317205 313 AVLRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLV 353
Cdd:COG0044 339 LVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLV 379
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-374 |
3.17e-14 |
|
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: 73.71 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEP----LQERDLLLVGNRIAALGDDLSLPPYAKG-EVYDLHGHYLVPGFIDAHVHICG----GGGEAGP 73
Cdd:COG0402 2 LLIRGAWVLTMDPaggvLEDGAVLVEDGRIAAVGPGAELPARYPAaEVIDAGGKLVLPGLVNTHTHLPQtllrGLADDLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 74 -------------SSRTPE-VQLS------QLTRAGITTVVgclgtD--SISRSMEELLVKanALEEEGLTCFVYSGGYq 131
Cdd:COG0402 82 lldwleeyiwpleARLDPEdVYAGallalaEMLRSGTTTVA-----DfyYVHPESADALAE--AAAEAGIRAVLGRGLM- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 132 aDRMIFDTLRKDLV--------LIDKVIGAG----EIAISDHRsaqPQKSELEHLAAEARvggmLGDKAGV-VHIHLGEg 198
Cdd:COG0402 154 -DRGFPDGLREDADegladserLIERWHGAAdgriRVALAPHA---PYTVSPELLRAAAA----LARELGLpLHTHLAE- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 199 krglspilkiieeteipisqfmpthiNRKEtlleqgVEFLKAGGtidltaGCDDFEphlqvpfvlkALYEQGLLNDRVT- 277
Cdd:COG0402 225 --------------------------TRDE------VEWVLELY------GKRPVE----------YLDELGLLGPRTLl 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 278 -----VTSD----------------------GNG--SLPQFNEAGILVGMG--IGSVHV---LWRDIREAVL-------- 315
Cdd:COG0402 257 ahcvhLTDEeiallaetgasvahcptsnlklGSGiaPVPRLLAAGVRVGLGtdGAASNNsldMFEEMRLAALlqrlrggd 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 316 RYGIPLDTALRTITSNPARILQLKNK-GMIREGFDGDLVAL--------------------SDDLMIEQVWAKGRVMIRN 374
Cdd:COG0402 337 PTALSAREALEMATLGGARALGLDDEiGSLEPGKRADLVVLdldaphlaplhdplsalvyaADGRDVRTVWVAGRVVVRD 416
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-399 |
3.21e-14 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 73.98 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLF--APEPLQERDLLLVGNRIAALGDDlslpPYAKGEVYDLHGHYLVPGFIDAHVHIcggggEagpSSR-TPE 79
Cdd:COG1001 7 LVIKNGRLVnvFTGEILEGDIAIAGGRIAGVGDY----IGEATEVIDAAGRYLVPGFIDGHVHI-----E---SSMvTPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 80 vqlsQLTRA----GITTVVgclgTDSIsrsmeELlvkANALEEEGLtcfvysggyqaDRMIfdTLRKDLVLidKVIgage 155
Cdd:COG1001 75 ----EFARAvlphGTTTVI----ADPH-----EI---ANVLGLEGV-----------RYML--EAAEGLPL--DIF---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 156 IAISdhrSAQPQKSELEH----LAAEArVGGMLGDKaGVvhIHLGEgkrglspilkiieeteipisqFM--PTHINRKET 229
Cdd:COG1001 120 VMLP---SCVPATPGLETagavLGAED-LAELLDHP-RV--IGLGE---------------------VMnfPGVLNGDPR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 230 LLEQGVEFLKAGGTID--------------LTAG-CDDFEPH--------LQ---------------VPFVLKALYEqgL 271
Cdd:COG1001 172 MLAKIAAALAAGKVIDghapglsgkdlnayAAAGiRSDHECTtaeealekLRrgmyvmiregsaakdLPALLPAVTE--L 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 272 LNDRVTVTSDGNgslpqfnEAGILVGMGigsvHVlwrD--IREAVlRYGIPLDTALRTITSNPARILQLKNKGMIREGFD 349
Cdd:COG1001 250 NSRRCALCTDDR-------HPDDLLEEG----HI---DhvVRRAI-ELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRR 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 698317205 350 GDLVALSD--DLMIEQVWAKGRVMIRNRKPVVLGVYETSLASHLQTVETPRL 399
Cdd:COG1001 315 ADIVLLDDleDFKVEKVYADGKLVAEDGKLLVDLPKYPYPPWARNTVKLRPL 366
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-371 |
7.41e-14 |
|
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: 72.15 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 52 YLVPGFIDAHVHICGGGGEAGPSSR-----TPEVQLSQLTRAGITTVVGCLGTDSISRsmeELLVKANALEEEGLTcFVY 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPefayeALRLGITTMLKSGTTTVLDMGATTSTGI---EALLEAAEELPLGLR-FLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 127 SGGYQADRMIFDTLRKDLVLIDKVI--------GAGEIAISDHRSAQPQKSELEHLAAEARVGGMLgdkagvVHIHLGEG 198
Cdd:pfam01979 77 PGCSLDTDGELEGRKALREKLKAGAefikgmadGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP------VAIHALET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 199 KRGLSPILKIIEETEI---PISQFMPTHINRK-ETLLEQGVEFLKAGGTIDLTAGCDDFEPHLQVP--------FVLKAL 266
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEhgtHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEHLKGAGVAHCPFSnsklrsgrIALRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 267 YEQGLlndRVTVTSDGNGSlpqfneagilvgmgiGSVHVLWRDIREAVL-----RYGIPLDTALRTITSNPARILQL-KN 340
Cdd:pfam01979 231 LEDGV---KVGLGTDGAGS---------------GNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLdDK 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 698317205 341 KGMIREGFDGDLVA-----------LSDDLMIEQVWAKGRVM 371
Cdd:pfam01979 293 VGSIEVGKDADLVVvdldplaaffgLKPDGNVKKVIVKGKIV 334
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-369 |
8.39e-14 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 72.05 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPE-PLQERDLLLVGNRIAALGDDLSLPpyakGEVYDLHGHYLVPGFIDAHVHicGGGGEAGPSSrTPEvQL 82
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIGPGAEPD----AEVIDLGGGYLAPGFIDLHVH--GGGGVDFMDG-TPE-AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 83 SQLTRA----GITTVVGCLGTDSIsrsmEELLvkaNALEeegltcfvysggyqadrmifdtlrkdlvlidkvigageiAI 158
Cdd:COG1820 73 RTIARAharhGTTSFLPTTITAPP----EDLL---RALA---------------------------------------AI 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 159 SDHRSAQPqkselehlaaearVGGMLGdkagvvhIHLgEG------KRG---------LSP--ILKIIEETEIPISQF-- 219
Cdd:COG1820 107 AEAIEQGG-------------GAGILG-------IHL-EGpflspeKKGahppeyirpPDPeeLDRLLEAAGGLIKLVtl 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 220 ---MPTHINRKETLLEQGV---------------EFLKAG-------------------GTI-------DLTAG--CDDF 253
Cdd:COG1820 166 apeLPGALEFIRYLVEAGVvvslghtdatyeqarAAFEAGathvthlfnamsplhhrepGVVgaaldddDVYAEliADGI 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 254 epHLQvPFVLKALYEQ----------------GL------LNDR-VTVTsDG-----NGSLpqfneAgilvgmgiGSVHV 305
Cdd:COG1820 246 --HVH-PAAVRLALRAkgpdrlilvtdamaaaGLpdgeyeLGGLeVTVK-DGvarlaDGTL-----A--------GSTLT 308
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698317205 306 LWRDIREAVLRYGIPLDTALRTITSNPARILQL-KNKGMIREGFDGDLVALSDDLMIEQVWAKGR 369
Cdd:COG1820 309 MDDAVRNLVEWTGLPLEEAVRMASLNPARALGLdDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-378 |
4.73e-13 |
|
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: 70.02 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPE--PLQERDLLLVGNRIAALGDDLSLPpyAKgEVYDLHGHYLVPGFIDAHVHicggggEAGPSSRTPEv 80
Cdd:cd01297 2 LVIRNGTVVDGTgaPPFTADVGIRDGRIAAIGPILSTS--AR-EVIDAAGLVVAPGFIDVHTH------YDGQVFWDPD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 81 qLSQLTRAGITTVVgcLGTDSIS-------------RSMEELLVKA--------------NALEEEGL----TCFV---- 125
Cdd:cd01297 72 -LRPSSRQGVTTVV--LGNCGVSpapanpddlarliMLMEGLVALGeglpwgwatfaeylDALEARPPavnvAALVghaa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 126 ---YSGGYQADRMIFDTLRKDLVLIDKVIGAGEIAISDHRSAQP-QKSELEHLAAEARVggmLGDKAGVVHIHL-GEGKR 200
Cdd:cd01297 149 lrrAVMGLDAREATEEELAKMRELLREALEAGALGISTGLAYAPrLYAGTAELVALARV---AARYGGVYQTHVrYEGDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 201 GLSPILKIIE---ETEIPISQFM------PTHINRKETLLEqgVEFLKAGGtIDLTAGCddfephlqvpfvlkALYEQGL 271
Cdd:cd01297 226 ILEALDELLRlgrETGRPVHISHlksagaPNWGKIDRLLAL--IEAARAEG-LQVTADV--------------YPYGAGS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 272 LNDR--------VTVTSDGnGSLPQFNeagilVGMGIGSVHVLWRDIREavlRYGIPLDTALRTITSNPARILQLKNKGM 343
Cdd:cd01297 289 EDDVrrimahpvVMGGSDG-GALGKPH-----PRSYGDFTRVLGHYVRE---RKLLSLEEAVRKMTGLPARVFGLADRGR 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 698317205 344 IREGFDGDLV-----ALSDDLM----------IEQVWAKGRVMIRNRKPV 378
Cdd:cd01297 360 IAPGYRADIVvfdpdTLADRATftrpnqpaegIEAVLVNGVPVVRDGAFT 409
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-368 |
6.11e-13 |
|
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: 69.53 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHicGGGGEAGPSSRTP--EV 80
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEAD--EIIDLKGQYLVPGFIDIHIH--GGGGADFMDGTAEalKT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 81 QLSQLTRAGITTVVGCLgtdsISRSMEELL-----VKANALEEEGLTC--------FVYSG--GYQADRMIFDTlrkDLV 145
Cdd:cd00854 77 IAEALAKHGTTSFLPTT----VTAPPEEIAkalaaIAEAIAEGQGAEIlgihlegpFISPEkkGAHPPEYLRAP---DPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 146 LIDKVIGAGEIAIsdhRSA-----QPQKSELEHLAAEARVGGMLGD------------KAGVVHI-HLGEGKRGLS---- 203
Cdd:cd00854 150 ELKKWLEAAGGLI---KLVtlapeLDGALELIRYLVERGIIVSIGHsdatyeqavaafEAGATHVtHLFNAMSPLHhrep 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 204 -PILKIIEE----TEIpISQFMPTHinrkETLLEQGVEFLKAGGTIDLT-----AGCDD--FEphlqvpfvlkaLYEQgl 271
Cdd:cd00854 227 gVVGAALSDddvyAEL-IADGIHVH----PAAVRLAYRAKGADKIVLVTdamaaAGLPDgeYE-----------LGGQ-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 272 lndRVTVTSDG----NGSLpqfneAGILVGMGIGsvhvlwrdIREAVLRYGIPLDTALRTITSNPARILQL-KNKGMIRE 346
Cdd:cd00854 289 ---TVTVKDGVarlaDGTL-----AGSTLTMDQA--------VRNMVKWGGCPLEEAVRMASLNPAKLLGLdDRKGSLKP 352
|
410 420
....*....|....*....|..
gi 698317205 347 GFDGDLVALSDDLMIEQVWAKG 368
Cdd:cd00854 353 GKDADLVVLDDDLNVKATWING 374
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-335 |
9.95e-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: 65.05 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 57 FIDAHVHICGGGGEAGPSS---------------RTPEVQLSQLTRAGITTVVGCLGTDSISRSMEELLVKANALEEEGL 121
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 122 TCFVYSGGYQADRMIFDTLRKDLVL--IDKVIGAGEIAISDHRSAQPQKSELEHLAAEARVGGMLGdkaGVVHIHLGEGK 199
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLelLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLG---LPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 200 RGLSPILKIIeETEIPISQFMPTHINRKETLLEQGVEFLKAGGTIDLTAGCDDFEPHLQVPfVLKALYEQGllnDRVTVT 279
Cdd:cd01292 158 DPTRALEDLV-ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGEGAE-ALRRLLELG---IRVTLG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 698317205 280 SDGNGSLPQFNeagilvgmgigsvhvLWRDIREA--VLRYGIPLDTALRTITSNPARI 335
Cdd:cd01292 233 TDGPPHPLGTD---------------LLALLRLLlkVLRLGLSLEEALRLATINPARA 275
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-353 |
3.02e-11 |
|
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: 64.55 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHIcggggeAGPSSRTPEVQ- 81
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGV--EVIDATGKYVLPGGIDPHTHL------ELPFMGTVTADd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 82 LSQLTRA----GITTVV-----------------------GCLGTD-----SISRSMEELLVKANALEEEGLTCF----V 125
Cdd:cd01314 73 FESGTRAaaagGTTTIIdfaipnkgqslleavekwrgkadGKSVIDygfhmIITDWTDSVIEELPELVKKGISSFkvfmA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 126 YSGGYQA-DRMIFDTLRK---------------DLV--LIDKVIGAGEIAISDHRSAQPQKSELEHLAAEARVGGMLGDK 187
Cdd:cd01314 153 YKGLLMVdDEELLDVLKRakelgalvmvhaengDVIaeLQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 188 AGVVHIHLGEG--------KRGlspiLKIIEETeipisqfMPTHINRKETLLEQgveflkaggtidltagcDDFEPHLQV 259
Cdd:cd01314 233 LYIVHVSSKEAadeiararKKG----LPVYGET-------CPQYLLLDDSDYWK-----------------DWFEGAKYV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 260 ---PFVLKALYE---QGLLNDRVTVTSDGNGSlpqFNEAGILVGM--------GIGSV----HVLWrdiREAVLRYGIPL 321
Cdd:cd01314 285 cspPLRPKEDQEalwDGLSSGTLQTVGSDHCP---FNFAQKARGKddftkipnGVPGVetrmPLLW---SEGVAKGRITL 358
|
410 420 430
....*....|....*....|....*....|...
gi 698317205 322 DTALRTITSNPARILQL-KNKGMIREGFDGDLV 353
Cdd:cd01314 359 EKFVELTSTNPAKIFGLyPRKGTIAVGSDADLV 391
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-353 |
1.10e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 62.75 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSlpPYAKGEVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPevqlS 83
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLD--GSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTG----S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 84 QLTRA-GITTVVGCLGTDSISRSMEELLVKANALEEEGLTCFVYSGGYQADrmiFDTLRkdlVLIDKVIGA-GEIAISDH 161
Cdd:PRK02382 79 RSAAAgGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGN---WDPLE---SLWERGVFAlGEIFMADS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 162 RSAQPQKSEL--EHLAAEARVGgmlgdkaGVVHIHL----------GEGKRGLSP------------------ILKIIEE 211
Cdd:PRK02382 153 TGGMGIDEELfeEALAEAARLG-------VLATVHAededlfdelaKLLKGDADAdawsayrpaaaeaaaverALEVASE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 212 TEIPIsqfmptHINRKETLleQGVEFLKAGG-TIDLTA-----GCDDFE---------PHLQVPFVLKALYEQglLNDRV 276
Cdd:PRK02382 226 TGARI------HIAHISTP--EGVDAARREGiTCEVTPhhlflSRRDWErlgtfgkmnPPLRSEKRREALWER--LNDGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 277 --TVTSDGNGSLPQFNEAGILVG-MGIGSVHVLWRDIREAVLRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLV 353
Cdd:PRK02382 296 idVVASDHAPHTREEKDADIWDApSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLV 375
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
47-372 |
1.40e-10 |
|
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: 62.63 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 47 DLHGHYLVPGFIDAHVHIcggggeagPSSRTPEVQLSQLT-RAGITTVVgclgTDSisrsmEELlvkANALEEEGLTCFV 125
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHI--------ESSMLTPSEFAKAVlPHGTTTVI----ADP-----HEI---ANVAGVDGIEFML 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 126 YsggyQADRMIFD---TLR--------------------KDLVLIDKVIGAGEIAisDHRSAQPQKSELEHLAAEARVGG 182
Cdd:cd01295 61 E----DAKKTPLDifwMLPscvpatpfetsgaeltaediKELLEHPEVVGLGEVM--DFPGVIEGDDEMLAKIQAAKKAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 183 MLGDkaGvvhiHLgegkRGLSPilkiiEETEIPISQFMPT---HINRKETL--LEQGVEFLKAGGTIdltagCDDFEphl 257
Cdd:cd01295 135 KPVD--G----HA----PGLSG-----EELNAYMAAGISTdheAMTGEEALekLRLGMYVMLREGSI-----AKNLE--- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 258 qvpFVLKALYEQGLlnDRVTVTSDGngSLPQFneagILVGMGIGSVhvlwrdIREAVlRYGIPLDTALRTITSNPARILQ 337
Cdd:cd01295 192 ---ALLPAITEKNF--RRFMFCTDD--VHPDD----LLSEGHLDYI------VRRAI-EAGIPPEDAIQMATINPAECYG 253
|
330 340 350
....*....|....*....|....*....|....*..
gi 698317205 338 LKNKGMIREGFDGDLVALSD--DLMIEQVWAKGRVMI 372
Cdd:cd01295 254 LHDLGAIAPGRIADIVILDDleNFNITTVLAKGIAVV 290
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-378 |
1.53e-10 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 62.22 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEP---LQERDLLLVGNRIAALGDDLSLPPYAKGEVYDLHGHYLVPGFIDAHVHICG----GGGEAGP-- 73
Cdd:cd01298 1 ILIRNGTIVTTDPrrvLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMtllrGLADDLPlm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 74 -----------SSRTPE-------VQLSQLTRAGITTVVgclgtDSISRSMEELlvkANALEEEGLTCFV--------YS 127
Cdd:cd01298 81 ewlkdliwpleRLLTEEdvylgalLALAEMIRSGTTTFA-----DMYFFYPDAV---AEAAEELGIRAVLgrgimdlgTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 128 GGYQADRMIFDTLRkdlvLIDKVIGAGE----IAISDHrsaQPQKSELEHLAAEARvggmLGDKAGV-VHIHLGEGKRGL 202
Cdd:cd01298 153 DVEETEEALAEAER----LIREWHGAADgrirVALAPH---APYTCSDELLREVAE----LAREYGVpLHIHLAETEDEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 203 SPILKIIEETeiPisqfmpthinrketlleqgVEFLKAGGTID---LTAGCDDFEPHlqvpfvlkalyEQGLLNDR-VTV 278
Cdd:cd01298 222 EESLEKYGKR--P-------------------VEYLEELGLLGpdvVLAHCVWLTDE-----------EIELLAETgTGV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 279 ----TSD---GNG--SLPQFNEAGILVGMGIGSVHV-----LWRDIREAVL----RYG----IPLDTALRTITSNPARIL 336
Cdd:cd01298 270 ahnpASNmklASGiaPVPEMLEAGVNVGLGTDGAASnnnldMFEEMRLAALlqklAHGdptaLPAEEALEMATIGGAKAL 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698317205 337 QLKNKGMIREGFDGDLVAL---------SDDLM-----------IEQVWAKGRVMIRNRKPV 378
Cdd:cd01298 350 GLDEIGSLEVGKKADLILIdldgphllpVHDPIshlvysanggdVDTVIVNGRVVMEDGELL 411
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-357 |
3.33e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 61.34 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEPL--QERDLLLVGNRIAALGDDLslPPYAKGEVYDLHGHYLVPGFIDAHVHICGGGGEAG--PSSRTPe 79
Cdd:COG3964 3 LIKGGRVIDPANGidGVMDIAIKDGKIAAVAKDI--DAAEAKKVIDASGLYVTPGLIDLHTHVFPGGTDYGvdPDGVGV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 80 vqlsqltRAGITTVV--GCLGTDS--------ISRSMEELLVKANaLEEEGLTcfvySGGYQAD------RMIFDTLRKd 143
Cdd:COG3964 80 -------RSGVTTVVdaGSAGAANfdgfrkyvIDPSKTRVLAFLN-ISGIGLV----GGNELQDlddidpDATAAAAEA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 144 lvLIDKVIGAgEIAISDHRSAQPQKSELEhLAAEArvggmlGDKAGV-VHIHLGEGKRGLSPILKIIEETEIpisqfmPT 222
Cdd:COG3964 147 --NPDFIVGI-KVRASKGVVGDNGIEPLK-RAKEA------AKEAGLpLMVHIGNPPPPLDEVLDLLRPGDI------LT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 223 HI-NRKetlleqgveflkaGGTIDLTAGcddfEPHlqvPFVLKALyEQGLLNDrvtvTSDGNGSlpqFN--------EAG 293
Cdd:COG3964 211 HCfNGK-------------PNGILDEDG----KVR---PSVREAR-KRGVLFD----VGHGGAS---FSfkvaepaiAQG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698317205 294 ILVGMgIGS-VHVlwRDIREAV----------LRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSD 357
Cdd:COG3964 263 FLPDT-ISTdLHT--RNMNGPVfdlatvmskfLALGMPLEEVIAAVTWNPARAIGLPELGTLSVGADADITIFDL 334
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
20-357 |
4.78e-10 |
|
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: 60.42 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 20 DLLLVGNRIAALGDDLslPPYAKGEVYDLHGHYLVPGFIDAHVHICGGGGEAG--PSSRTPEvqlsqltrAGITTVV--G 95
Cdd:cd01307 1 DVAIENGKIAAVGAAL--AAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGdrPDMIGVK--------SGVTTVVdaG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 96 CLGTDSIsRSMEELLVKANALEeegltcfVYSggyqadrmifdtlrkdLVLIDKVigaGEIAIsdHRSAQPQKSELE--H 173
Cdd:cd01307 71 SAGADNI-DGFRYTVIERSATR-------VYA----------------FLNISRV---GLVAQ--DELPDPDNIDEDavV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 174 LAAEARVGGMLGDKAGVVHIHLGEGkrGLSPI---LKIIEETEIPisqfMPTHINRKETLLEQGVEFLKAGgtiDLTAGC 250
Cdd:cd01307 122 AAAREYPDVIVGLKARASKSVVGEW--GIKPLelaKKIAKEADLP----LMVHIGSPPPILDEVVPLLRRG---DVLTHC 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 251 ----------DDFEPHlqvPFVLKAlYEQGLLND----------RVTVTSDGNGSLPQFNEAGIlvgMGIGSVHVLWRDI 310
Cdd:cd01307 193 fngkpngivdEEGEVL---PLVRRA-RERGVIFDvghgtasfsfRVARAAIAAGLLPDTISSDI---HGRNRTNGPVYAL 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 698317205 311 ---REAVLRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSD 357
Cdd:cd01307 266 attLSKLLALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDL 315
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-68 |
6.73e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 60.58 E-value: 6.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEPLQER--DLLLVGNRIAALGDDLSLPPYAKG--EVYDLHGHYLVPGFIDAHVHICGGG 68
Cdd:COG1574 10 LLLTNGRIYTMDPAQPVaeAVAVRDGRIVAVGSDAEVRALAGPatEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-371 |
8.14e-10 |
|
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: 60.02 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 27 RIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHICGGGGEAGP---------SSRTPEV--------QLSQLTRA- 88
Cdd:cd01309 3 KIVAVGAEITTPADA--EVIDAKGKHVTPGLIDAHSHLGLDEEGGVRetsdaneetDPVTPHVraidginpDDEAFKRAr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 89 --GITTVVGCLGTDSISRSMEELL------VKANALEEEGLTCF--------VYSGGYQ--ADRM--------IFDTLRK 142
Cdd:cd01309 81 agGVTTVQVLPGSANLIGGQGVVIktdggtIEDMFIKAPAGLKMalgenpkrVYGGKGKepATRMgvaallrdAFIKAQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 143 DLVLIDKVIGAGeiaisdhRSAQPQKSELEHLAAearvggmLGDKAGVVHIHLGEGKRGLSpILKIIEETEIPISQFMPT 222
Cdd:cd01309 161 YGRKYDLGKNAK-------KDPPERDLKLEALLP-------VLKGEIPVRIHAHRADDILT-AIRIAKEFGIKITIEHGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 223 HinrkETLLeqgVEFLKAGGtIDLTAGCDDFEPHLQVPFVL-----KALYEQGLLndRVTVTSDGNGSLPQ--FNEAGIL 295
Cdd:cd01309 226 E----GYKL---ADELAKHG-IPVIYGPTLTLPKKVEEVNDaidtnAYLLKKGGV--AFAISSDHPVLNIRnlNLEAAKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 296 VgmgigsvhvlwrdireavlRYGIPLDTALRTITSNPARILQLKNK-GMIREGFDGDLVALSDDLM-----IEQVWAKGR 369
Cdd:cd01309 296 V-------------------KYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWNGDPLeptskPEQVYIDGR 356
|
..
gi 698317205 370 VM 371
Cdd:cd01309 357 LV 358
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-102 |
1.65e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 59.09 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEPL--QERDLLLVGNRIAALGDDLSlPPYAKgEVYDLHGHYLVPGFIDAHVHICGG----GGEAGPSSRt 77
Cdd:PRK09237 2 LLRGGRVIDPANGidGVIDIAIEDGKIAAVAGDID-GSQAK-KVIDLSGLYVSPGWIDLHVHVYPGstpyGDEPDEVGV- 78
|
90 100
....*....|....*....|....*..
gi 698317205 78 pevqlsqltRAGITTVV--GCLGTDSI 102
Cdd:PRK09237 79 ---------RSGVTTVVdaGSAGADNF 96
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-353 |
3.84e-09 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 58.17 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPpyaKGEVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPevqlS 83
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSP---AREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATG----S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 84 QLTRAGITTVVGCLGTDSISRSM--EELLVKANALEEEGLTCFVYSG-------------------GYQA---------- 132
Cdd:PRK06189 79 AALAAGGCTTYFDMPLNSIPPTVtrEALDAKAELARQKSAVDFALWGglvpgnlehlrelaeagviGFKAfmsnsgtdef 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 133 ----DRMIFDTLRK---------------DLV--LIDKVIGAGEIAISDHRSAQPQKSELEHLAAEARVGGMLGDKAGVV 191
Cdd:PRK06189 159 rssdDLTLYEGMKEiaalgkilalhaesdALTrhLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 192 HIHLGEGkrglspiLKIIEETE---IPISQfmpthinrkET----LLEQGVEFLKAGGtidlTAGCddfEPHLQVPFVLK 264
Cdd:PRK06189 239 HISSGKA-------VALIAEAKkrgVDVSV---------ETcphyLLFTEEDFERIGA----VAKC---APPLRSRSQKE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 265 ALYEQGLLNDRVTVTSDGNGSLPQFNEAG--ILVGMGI-GSVHVLWRDIREAVLRYGIPLDTALRTITSNPARILQLKNK 341
Cdd:PRK06189 296 ELWRGLLAGEIDMISSDHSPCPPELKEGDdfFLVWGGIsGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLPQK 375
|
410
....*....|..
gi 698317205 342 GMIREGFDGDLV 353
Cdd:PRK06189 376 GRLEVGADADFV 387
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
18-365 |
1.02e-08 |
|
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: 56.68 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 18 ERDLLLVGNRIAALGDdLSLPPYAkgEVYDLHGHYLVPGFIDAHVHIcgggGEAGPSSRTPEVQLSQLT-RAGITTVVGC 96
Cdd:TIGR00857 5 EVDILVEGGRIKKIGK-LRIPPDA--EVIDAKGLLVLPGFIDLHVHL----RDPGEEYKEDIESGSKAAaHGGFTTVADM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 97 LGTDSISRSMEELLVKANALEEEGLT-CFVYSG---GYQADRM--------------IF----------DTLRKDLVL-- 146
Cdd:TIGR00857 78 PNTKPPIDTPETLEWKLQRLKKVSLVdVHLYGGvtqGNQGKELteayelkeagavgrMFtddgsevqdiLSMRRALEYaa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 147 -IDKVIGA---------------GEIAISDHRSAQPQKSELEHLaaeARVGGMLGDKAGVVHI-HLGEgKRGLSPILKII 209
Cdd:TIGR00857 158 iAGVPIALhaedpdliyggvmheGPSAAQLGLPARPPEAEEVAV---ARLLELAKHAGCPVHIcHIST-KESLELIVKAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 210 EETEIPISQFMPTHInrkeTLLEQGVEFLKAGGTIDltagcddfePHLQVPFVLKALYEqGLLNDRVTV--------TSD 281
Cdd:TIGR00857 234 SQGIKITAEVTPHHL----LLSEEDVARLDGNGKVN---------PPLREKEDRLALIE-GLKDGIIDIiatdhaphTLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 282 GNGSLPQFNEAGIlvgmgIG---SVHVLWRDIREAVlrygIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALsdD 358
Cdd:TIGR00857 300 EKTKEFAAAPPGI-----PGletALPLLLQLLVKGL----ISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVF--D 368
|
....*..
gi 698317205 359 LmiEQVW 365
Cdd:TIGR00857 369 L--KKEW 373
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
44-358 |
2.07e-08 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 55.38 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 44 EVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPEV--------QLSQLTRAGITTVVGCLGTD--SISRSMEELLV-- 111
Cdd:cd01299 2 QVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEyrtiratrQARAALRAGFTTVRDAGGADygLLRDAIDAGLIpg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 112 --------------------KANALEEEGLTCFVYSGGYQADRMIFDTLRK--DLVlidKVIGAGEIAISDHRSAQPQKS 169
Cdd:cd01299 82 prvfasgralsqtgghgdprGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRgaDQI---KIMATGGVLSPGDPPPDTQFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 170 --ELEHLAAEARvggmlgdKAG---VVHIHLGEGKRGLspIL---KIIEeteipisqfmptHINRketLLEQGVEFLKAG 241
Cdd:cd01299 159 eeELRAIVDEAH-------KAGlyvAAHAYGAEAIRRA--IRagvDTIE------------HGFL---IDDETIELMKEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 242 GTIdltagcddFEPHLQVP-FVLKALYEQGLLNDRVT----VTSDGNGSLPQFNEAGILVGMG--IGSV----HVLWRDI 310
Cdd:cd01299 215 GIF--------LVPTLATYeALAAEGAAPGLPADSAEkvalVLEAGRDALRRAHKAGVKIAFGtdAGFPvpphGWNAREL 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 698317205 311 REAVlRYGIPLDTALRTITSNPARILQL-KNKGMIREGFDGDLVALSDD 358
Cdd:cd01299 287 ELLV-KAGGTPAEALRAATANAAELLGLsDELGVIEAGKLADLLVVDGD 334
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-64 |
2.07e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 55.95 E-value: 2.07e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 698317205 1 MWTLIKNAKLFAPEPLQERDLLLVGNRIAALGDDlslppyAKGEVYDLHGHYLVPGFIDAHVHI 64
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN------LGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-63 |
2.10e-08 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 55.59 E-value: 2.10e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 698317205 1 MWTLIKNAKLFAPEPLQER-DLLLVGNRIAALGDDlslPPYAKGEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEVaDVLIDDGKIAAIGEN---IEAEGAEVIDATGLVVAPGLVDLHVH 61
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
3-63 |
2.11e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 55.71 E-value: 2.11e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 3 TLIKNAKLFAPEPLqerDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK05985 4 LLFRNVRPAGGAAV---DILIRDGRIAAIGPALAAPPGA--EVEDGGGALALPGLVDGHIH 59
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-64 |
2.71e-08 |
|
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: 55.37 E-value: 2.71e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHI 64
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAE--EVIDAGGLVVMPGLIDTHVHI 61
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-378 |
7.20e-07 |
|
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: 50.71 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKL-FAPEPLQerDLLLVGNRIAALGDDLSLPPyaKGEVYDLHGHYLVPGFIDAHVHICGG--GGEAGPSSRTPev 80
Cdd:cd01293 1 LLRNARLaDGGTALV--DIAIEDGRIAAIGPALAVPP--DAEEVDAKGRLVLPAFVDPHIHLDKTftGGRWPNNSGGT-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 81 qlsqlTRAGITTvvgcLGTDSISRSMEELLVKAnaleEEGLTCFVySGGYQADRMIFDtlrkdlvlIDKVIGAGEI-AIS 159
Cdd:cd01293 75 -----LLEAIIA----WEERKLLLTAEDVKERA----ERALELAI-AHGTTAIRTHVD--------VDPAAGLKALeALL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 160 DHRS-----------AQPQ-----KSELEHLAAEA-RVGG-MLGdkaGVVHI-HLGEGKRGLSPILKIIEETEIPISqfm 220
Cdd:cd01293 133 ELREewadlidlqivAFPQhgllsTPGGEELMREAlKMGAdVVG---GIPPAeIDEDGEESLDTLFELAQEHGLDID--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 221 pTHINRKETLLEQGVEFL-----KAGGTIDLTAG-CDDFepHLQVPFVLKALYEQ---------------GLLNDRVTVT 279
Cdd:cd01293 207 -LHLDETDDPGSRTLEELaeeaeRRGMQGRVTCShATAL--GSLPEAEVSRLADLlaeagisvvslppinLYLQGREDTT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 280 SDGNG--SLPQFNEAGILVGMGIGSVHVLWR-----DIRE----AVLRYGIP----LDTALRTITSNPARILQLKNKGmI 344
Cdd:cd01293 284 PKRRGvtPVKELRAAGVNVALGSDNVRDPWYpfgsgDMLEvanlAAHIAQLGtpedLALALDLITGNAARALGLEDYG-I 362
|
410 420 430
....*....|....*....|....*....|....*...
gi 698317205 345 REGFDGDLVAL----SDDLMIEQvwAKGRVMIRNRKPV 378
Cdd:cd01293 363 KVGCPADLVLLdaedVAEAVARQ--PPRRVVIRKGRVV 398
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
304-370 |
7.64e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 50.99 E-value: 7.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 698317205 304 HVLWRDIReavlrygIPLDTALRTITSNPARILQL-KNKGMIREGFDGDLVALSDDLM-----------IEQVWAKGRV 370
Cdd:pfam07969 391 EVLGPDEE-------LSLEEALALYTSGPAKALGLeDRKGTLGVGKDADLVVLDDDPLtvdppaiadirVRLTVVDGRV 462
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-68 |
8.33e-07 |
|
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: 50.77 E-value: 8.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 698317205 25 GNRIAALGDDLSLPPYA--KGEVYDLHGHYLVPGFIDAHVHICGGG 68
Cdd:cd01300 6 DGRIVAVGSDAEAKALKgpATEVIDLKGKTVLPGFIDSHSHLLLGG 51
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
52-359 |
9.33e-07 |
|
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: 50.47 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 52 YLVPGFIDAHVHIcgggGEAGPSSRTPEVQLSqlTRA----GITTVVGCLGTDSISRSMEELLVKANALEEEGLTCFVYS 127
Cdd:cd01302 2 LVLPGFIDIHVHL----RDPGGTTYKEDFESG--SRAaaagGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 128 GGYqADRMIFDTLRKdlvLIDKVI----------GAGEIAISD---HRSAQPQKSELEHLAAEARVGGMLGDKAG----V 190
Cdd:cd01302 76 AGI-GPGDVTDELKK---LFDAGInslkvfmnyyFGELFDVDDgtlMRTFLEIASRGGPVMVHAERAAQLAEEAGanvhI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 191 VHIHLGEG----KRGLSPILKIIEETEipisqfmPTHINRKETLLEQGVEFLKaggtidltagcddFEPHLQVPFVLKAL 266
Cdd:cd01302 152 AHVSSGEAleliKFAKNKGVKVTCEVC-------PHHLFLDESMLRLNGAWGK-------------VNPPLRSKEDREAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 267 YEqGLLNDRV-TVTSDGNGSLPQFNEAGILV---GMGIGSVHVLWRDIREAVLRYGIPLDTALRTITSNPARILQLKNKG 342
Cdd:cd01302 212 WE-GVKNGKIdTIASDHAPHSKEEKESGKDIwkaPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKG 290
|
330
....*....|....*..
gi 698317205 343 MIREGFDGDLVALSDDL 359
Cdd:cd01302 291 TIAVGYDADLVIVDPKK 307
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-65 |
2.23e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 49.61 E-value: 2.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 698317205 1 MWTLIKNAKLF---APEPLQERDLLLVGNRIAALGDDLSLPPYAKgeVYDLHGHYLVPGFIDAHVHIC 65
Cdd:PRK07228 1 MTILIKNAGIVtmnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDD--HIDATGKVVIPGLIQGHIHLC 66
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
3-63 |
2.73e-06 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 49.10 E-value: 2.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDdlSLPPYAKGEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKIAS--SISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
21-63 |
4.13e-06 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 48.65 E-value: 4.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 698317205 21 LLLVGN-RIAALGD--DLS--LPPYAkgEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK09228 33 LLLVEDgRIVAAGPyaELRaqLPADA--EVTDYRGKLILPGFIDTHIH 78
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-382 |
6.90e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.07 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEP----LQERDLLLVGNRIAALGDDLSLPpyaKGEVYDLHGHYLVPGFIDAHVH-----ICGGGGEAGP 73
Cdd:PRK08204 4 TLIRGGTVLTMDPaigdLPRGDILIEGDRIAAVAPSIEAP---DAEVVDARGMIVMPGLVDTHRHtwqsvLRGIGADWTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 74 ------------SSRTPE--------VQLSQLTrAGITTVVgclgtD--SISRSMEELLVKANALEEEGL-TCFVYSGGY 130
Cdd:PRK08204 81 qtyfreihgnlgPMFRPEdvyianllGALEALD-AGVTTLL-----DwsHINNSPEHADAAIRGLAEAGIrAVFAHGSPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 131 QADRMIFDTLRKDLVLIDKVIGAG----------------------EIAISDHRSAQpqksELEHLAAEARVGGMLGDKA 188
Cdd:PRK08204 155 PSPYWPFDSVPHPREDIRRVKKRYfssddglltlglairgpefsswEVARADFRLAR----ELGLPISMHQGFGPWGATP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 189 GVVHIHLGEGKrgLSPILKIIeeteipisqfmptHINR-KETLLEQGVEflkAGGTIDLTAGCDDFEPHLQVPF--VLKA 265
Cdd:PRK08204 231 RGVEQLHDAGL--LGPDLNLV-------------HGNDlSDDELKLLAD---SGGSFSVTPEIEMMMGHGYPVTgrLLAH 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 266 LYEQGLLNDRVTVTsdgNGSLpqFNEAGILVGMGIGSVH-VLWRDIREAVLRYGIPLDTALRTITSNPARILQLKNK-GM 343
Cdd:PRK08204 293 GVRPSLGVDVVTST---GGDM--FTQMRFALQAERARDNaVHLREGGMPPPRLTLTARQVLEWATIEGARALGLEDRiGS 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 698317205 344 IREGFDGDLVALS-DDLM-------------------IEQVWAKGRVMIRNRKPVVLGV 382
Cdd:PRK08204 368 LTPGKQADLVLIDaTDLNlapvhdpvgavvqsahpgnVDSVMVAGRAVKRNGKLLGVDL 426
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
318-370 |
8.28e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 47.48 E-value: 8.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 698317205 318 GIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSDDL---MIEQVWAKGRV 370
Cdd:PRK15446 323 GLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGglpVVRAVWRGGRR 378
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-63 |
1.34e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 46.98 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 698317205 1 MWTLIKNAKLFAPE-PLQERDLLLVGNRIAALGDDLSLPPYAKgeVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK07575 3 MSLLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISATAVDT--VIDAEGLTLLPGVIDPQVH 64
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-63 |
1.84e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 46.45 E-value: 1.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDdlsLPPYAKGEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD---LSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
17-63 |
2.11e-05 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 46.48 E-value: 2.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 698317205 17 QERDLLLVGN-RIAALGDDLSLPP--YAKGEVYDLHGHYLVPGFIDAHVH 63
Cdd:TIGR02967 4 FEDGLLVVENgRIVAVGDYAELKEtlPAGVEIDDYRGHLIMPGFIDTHIH 53
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-121 |
2.57e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 45.98 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 1 MWTLIKNAKLFAP-EPLQERDLLLVGNRIAALGDDLSLPPYAKgeVYDLHGHYLVPGFIDAHVHICGGGGEAGPSSRTPE 79
Cdd:TIGR00221 3 ESYLLKDIAIVTGnEVIDNGAVGINDGKISTVSTEAELEPEIK--EIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 698317205 80 VQLSQLTRAGITTVVGCLGTDSIS------RSMEELLVKANALEEEGL 121
Cdd:TIGR00221 81 IMSERLPKSGCTSFLPTLITQPDEnikqavKNMREYLAKEKNAQALGL 128
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
3-358 |
3.97e-05 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 45.62 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPyakgEVYDLHGHYLVPGFIDAHVHIC--GGGGEAGPSSRTpev 80
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK----EVMDASGLVVSPGMVDAHTHISepGRSHWEGYETGT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 81 qlSQLTRAGITTVVGCLGTD---SISRSMEELLVKA-----------------------NALEEEGLT---CFVYSGGyq 131
Cdd:PRK08044 78 --RAAAKGGITTMIEMPLNQlpaTVDRASIELKFDAakgkltidaaqlgglvsynldrlHELDEVGVVgfkCFVATCG-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 132 aDRMIFDTLR-----------KDLVLIDKVI-------------GA-----GEIAISDHRSAQPQKSELEHLAAEARVGG 182
Cdd:PRK08044 154 -DRGIDNDFRdvndwqfykgaQKLGELGQPVlvhcenalicdelGEeakreGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 183 MLGDKAGVVHIHLGEgkrGLSPILKIIEETEIPISQFMPTHINRKETLLEQgveflkaggtIDLTAGCddfEPHLQVPFV 262
Cdd:PRK08044 233 VAGCRLHVCHISSPE---GVEEVTRARQEGQDVTCESCPHYFVLDTDQFEE----------IGTLAKC---SPPIRDLEN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 263 LKALYEQGLLNDRVTVTSDGNGSLPQFNEAGILVGMG-----IGSVHVLWrdiREAVLRYGIPLDTALRTITSNPARILQ 337
Cdd:PRK08044 297 QKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGgiaglQNCMDVMF---DEAVQKRGMSLPMFGKLMATNAADIFG 373
|
410 420
....*....|....*....|.
gi 698317205 338 LKNKGMIREGFDGDLVALSDD 358
Cdd:PRK08044 374 LQQKGRIAPGKDADFVFIQPN 394
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-61 |
6.97e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 44.78 E-value: 6.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 1 MWTLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSLPPYAKgevyDLHGHYLVPGFIDAH 61
Cdd:PRK15446 2 MEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAI----DAEGDYLLPGLVDLH 58
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-64 |
7.28e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 44.69 E-value: 7.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698317205 3 TLIKNAKLFAPEPLQERDLLLVGNRIAALGDDLSlppyAKGEVYDLHGHYLVPGFIDAHVHI 64
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG----PGAREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
4-94 |
1.24e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 43.98 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAKLFAPEP--LQERDLLLVGNRIAalgdDLSLPPYAKGE-VYDLHGHYLVPGFIDAHVHICGGGGEAGPSsrtPEV 80
Cdd:PRK12394 6 LITNGHIIDPARniNEINNLRIINDIIV----DADKYPVASETrIIHADGCIVTPGLIDYHAHVFYDGTEGGVR---PDM 78
|
90
....*....|....
gi 698317205 81 QLSQLtraGITTVV 94
Cdd:PRK12394 79 YMPPN---GVTTVV 89
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
318-368 |
1.63e-04 |
|
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: 43.42 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 698317205 318 GIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSDDL---MIEQVWAKG 368
Cdd:cd01306 272 GWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDgvpVVRTVWRGG 325
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
4-369 |
3.04e-04 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 42.84 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 4 LIKNAK---LFAPEPLQErDLLLVGNRIAALGDdlslppYAKGEVYDLHGHYLVPGFIDAHVHIcggggeagPSSRTPEV 80
Cdd:TIGR01178 3 VIKNAKiidVYNGEIIPG-DIAIANGHIAGVGK------YNGVKVIDALGEYAVPGFIDAHIHI--------ESSMLTPS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 81 QLSQLTRA-GITTVV-------GCLGTDSISRSMEEL-------------LVKANALEEegltcfvySGGYQADRMIfdt 139
Cdd:TIGR01178 68 EFAKLVLPhGVTTVVsdpheiaNVNGEDGINFMLNNAkktplnfyfmlpsCVPALQFET--------SGAVLTAEDI--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 140 lrKDLVLIDKVIGAGEIAisDHRSAQPQKSELEHLAAEARVGGMLGDKagvvhiHLGegkrGLSPilkiiEETEIPISQF 219
Cdd:TIGR01178 137 --DELMELDEVLGLAEVM--DYPGVINADIEMLNKINSARKRNKVIDG------HCP----GLSG-----KLLNKYISAG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 220 MPThiNRKETLLEQGVEFLKAGGTIDLTAG--CDDFEPhlqvpfVLKALYEQGllNDRVTVTSDGNGSLPQFNEAGILvg 297
Cdd:TIGR01178 198 ISN--DHESTSIEEAREKLRLGMKLMIREGsaAKNLEA------LHPLINEKN--CRSLMLCTDDRHVNDILNEGHIN-- 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 698317205 298 mgigsvHVLWRDIreavlRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALSD--DLMIEQVWAKGR 369
Cdd:TIGR01178 266 ------HIVRRAI-----EHGVDPFDALQMASINPAEHFGIDVGGLIAPGDPADFVILKDlrNFKVNKTYVKGK 328
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
4-64 |
7.38e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.46 E-value: 7.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 698317205 4 LIKNAKLF---APEPLQER-DLLLVGNRIAALG--DDLSlPPYAKGEVYDLHGHYLVPGFIDAHVHI 64
Cdd:PRK07203 3 LIGNGTAItrdPAKPVIEDgAIAIEGNVIVEIGttDELK-AKYPDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
21-63 |
1.37e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 40.72 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 698317205 21 LLLVGNRIAALGDDLS-----LPPYAkgEVYDLHGHYLVPGFIDAHVH 63
Cdd:cd01303 28 LIVVVDGNIIAAGAAEtlkraAKPGA--RVIDSPNQFILPGFIDTHIH 73
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
308-355 |
1.96e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.06 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 698317205 308 RDIREAVLRYG-IPLDTALRTITSNPARIL-----QLKNKGMIREGFDGDLVAL 355
Cdd:PRK09061 404 RFLREYVRERKaLSLLEAIRKCTLMPAQILedsvpAMRRKGRLQAGADADIVVF 457
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
1-67 |
3.62e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.19 E-value: 3.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 698317205 1 MWTLIkNAKLF-APEPLQERDLLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHICGG 67
Cdd:PRK11170 1 MYALT-NGRIYtGHEVLDDHAVVIADGLIEAVCPVAELPPGI--EQRDLNGAILSPGFIDLQLNGCGG 65
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
21-68 |
3.95e-03 |
|
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: 39.16 E-value: 3.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 698317205 21 LLLVGNRIAALG--DDLSLPPYAKGEVYDLHGHYLVPGFIDAHVHICGGG 68
Cdd:cd01296 1 IAIRDGRIAAVGpaASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
311-356 |
4.47e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 39.20 E-value: 4.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 698317205 311 REAV--LRYGIPLDTALRTITSNPARILQLKNKGMIREGFDGDLVALS 356
Cdd:PRK07583 350 REAVriLHLDHPYDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVLFK 397
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
3-63 |
5.41e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.68 E-value: 5.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 698317205 3 TLIKNAKLFAPEPLQER-----DLLLVGNRIAALGDDLSLPPYAkGEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK08203 3 LWIKNPLAIVTMDAARReiadgGLVVEGGRIVEVGPGGALPQPA-DEVFDARGHVVTPGLVNTHHH 67
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
4-64 |
5.54e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 38.85 E-value: 5.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 4 LIKNAKLfaPEPLQERDLLLVGNRIAALGDDLSLPPyakGEVYDLHGHYLVPGFIDAHVHI 64
Cdd:PRK07572 5 IVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEA---AEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
286-352 |
6.56e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 38.48 E-value: 6.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 698317205 286 LPQFNEAGILVGMGIGSVHVLWRDI-REAVLRYGI----PLDTaLRTITSNPARILQLKNKGMIREGFDGDL 352
Cdd:PRK07213 269 LNEMLEKGILLGIGTDNFMANSPSIfREMEFIYKLyhiePKEI-LKMATINGAKILGLINVGLIEEGFKADF 339
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
21-94 |
6.89e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 38.66 E-value: 6.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698317205 21 LLLVGNRIAALGDDLSLPPYAkgEVYDLHGHYLVPGFIDAHVHIcggggeaGPSSRTP-EVQLSQLTRaGITTVV 94
Cdd:PRK10027 52 IVIKGRYIAGVGAEYADAPAL--QRIDARGATAVPGFIDAHLHI-------ESSMMTPvTFETATLPR-GLTTVI 116
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-113 |
8.17e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 38.33 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698317205 1 MWTLIKNAKLFAPEPLQE---RDLLLVGNRIAALGDDlslPPYAKgEVYDLHGHYLVPGFIDAHVHIcGGGGEAG----- 72
Cdd:PRK06380 1 MSILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGDV---NEEAD-YIIDATGKVVMPGLINTHAHV-GMTASKGlfddv 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 698317205 73 ------------PSSRTPE-------VQLSQLTRAGITTVVGCLGT-DSISRSMEELLVKA 113
Cdd:PRK06380 76 dleeflmktfkyDSKRTREgiynsakLGMYEMINSGITAFVDLYYSeDIIAKAAEELGIRA 136
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-63 |
9.10e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 37.86 E-value: 9.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 698317205 1 MWTLIKNAKLFAPEPLQ--ERDLLLVGNRIAALGDDLSLPpyaKGEVYDLHGHYLVPGFIDAHVH 63
Cdd:PRK08393 1 MSILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNINKP---ADTVIDASGSVVSPGFINAHTH 62
|
|
| |
