|
Name |
Accession |
Description |
Interval |
E-value |
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-378 |
2.01e-72 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 231.00 E-value: 2.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTWPRGNYITDGAVLVKDGVIAAVGTREELrAAHPDEPVLHHADSTLLPGLIDAHAHLASGGGPDPVAALGQ 80
Cdd:COG1228 10 LLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADL-AVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 81 SVETT--LLEAMRGRAEQLLRSGVTTVRDLGdGGHLALRlgDEVAEG---AVAGPRIISAGIPITPPGrpgsapGGEVSG 155
Cdd:COG1228 89 GITPTvdLVNPADKRLRRALAAGVTTVRDLP-GGPLGLR--DAIIAGeskLLPGPRVLAAGPALSLTG------GAHARG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 156 EDEIRALIRRNASAGAQVTQVMFTGGGgRQFTQAELTAVRLESLAARVRVVAHAHSRDSITAAVAADVDTIEFCSMaeds 235
Cdd:COG1228 160 PEEARAALRELLAEGADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDSIEHGTY---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 236 ieIDEQLLDEIIHWD-ISVCPAISPTWPILPRVIGEERA------DAICAAVLQMAEAGVRLIAGSDAGGRWAghEGFGL 308
Cdd:COG1228 235 --LDDEVADLLAEAGtVVLVPTLSLFLALLEGAAAPVAAkarkvrEAALANARRLHDAGVPVALGTDAGVGVP--PGRSL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 309 ASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVVRGNPLSDLSALREIREVFAAG 378
Cdd:COG1228 311 HRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDVRAVMKDG 380
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
54-368 |
2.08e-62 |
|
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: 203.68 E-value: 2.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 54 TLLPGLIDAHAHLASGGGPDPvAALGQSVETTLLEAmRGRAEQLLRSGVTTVRDLGDGGHLALRlgDEVAEGAVAGPRII 133
Cdd:cd01299 10 TLMPGLIDAHTHLGSDPGDLP-LDLALPVEYRTIRA-TRQARAALRAGFTTVRDAGGADYGLLR--DAIDAGLIPGPRVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 134 SAGIPITPPGRPGS-----------APGGEVSGEDEIRALIRRNASAGAQVTQVMFTGG--------GGRQFTQAELTAV 194
Cdd:cd01299 86 ASGRALSQTGGHGDprglsglfpagGLAAVVDGVEEVRAAVREQLRRGADQIKIMATGGvlspgdppPDTQFSEEELRAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 195 RLESLAARVRVVAHAHSRDSITAAVAADVDTIEFCSMaedsieIDEQLLDEIIHWDISVCPAIS-----------PTWPI 263
Cdd:cd01299 166 VDEAHKAGLYVAAHAYGAEAIRRAIRAGVDTIEHGFL------IDDETIELMKEKGIFLVPTLAtyealaaegaaPGLPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 264 LPRVIGEERADAICAAVLQMAEAGVRLIAGSDAGGRWAGHEGfgLASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKT 343
Cdd:cd01299 240 DSAEKVALVLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHGW--NARELELLVKAGGTPAEALRAATANAAELLGLSDEL 317
|
330 340
....*....|....*....|....*
gi 2764696544 344 GRIAVGYSADLLVVRGNPLSDLSAL 368
Cdd:cd01299 318 GVIEAGKLADLLVVDGDPLEDIAVL 342
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
54-378 |
4.14e-30 |
|
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: 117.99 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 54 TLLPGLIDAHAHLASGGGPDPVAALGQSVEttlleAMRGRAEQLLRSGVTTVRDLGDGGHLALRLGDEVAEGAVAGPRII 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE-----ALRLGITTMLKSGTTTVLDMGATTSTGIEALLEAAEELPLGLRFL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 134 SAGIPITPpgrpgsapggevSGEDEIRALIRRNASAGAQVTQVMFTGG--------GGRQFTQAELTAVRLESLAARVRV 205
Cdd:pfam01979 76 GPGCSLDT------------DGELEGRKALREKLKAGAEFIKGMADGVvfvglaphGAPTFSDDELKAALEEAKKYGLPV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 206 VAHAHS-RDSITAAVAADVDTIEFCSMAEDSIEIDeqLLDEI-------IH---WDISVCPAISPTWPILPRVIGEERAD 274
Cdd:pfam01979 144 AIHALEtKGEVEDAIAAFGGGIEHGTHLEVAESGG--LLDIIklilahgVHlspTEANLLAEHLKGAGVAHCPFSNSKLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 275 AICAAVLQMAEAGVRLIAGSD---AGGRWAGHEGFGLASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYS 351
Cdd:pfam01979 222 SGRIALRKALEDGVKVGLGTDgagSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKD 301
|
330 340 350
....*....|....*....|....*....|
gi 2764696544 352 ADLLVVRGNPLSDLSAL---REIREVFAAG 378
Cdd:pfam01979 302 ADLVVVDLDPLAAFFGLkpdGNVKKVIVKG 331
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-378 |
4.16e-27 |
|
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: 111.46 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 2 LIHASRVLTW-PRGNYITDGAVLVKDGVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHLAS----GGGPD--- 73
Cdd:COG0402 3 LIRGAWVLTMdPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHLPQtllrGLADDlpl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 74 ---------PVAAlGQSVETTLLEAMRGRAEqLLRSGVTTVRDLGDGGHLALrlgDEVAEGAV-AGPRIIsAGIPITPPG 143
Cdd:COG0402 83 ldwleeyiwPLEA-RLDPEDVYAGALLALAE-MLRSGTTTVADFYYVHPESA---DALAEAAAeAGIRAV-LGRGLMDRG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 144 RPGSAPGGEVSGEDEIRALIRRNASAGAQVTQVMFTGGGGRQFTQAELTAVRLESLAARVRVVAHAH-SRDSITAAVAA- 221
Cdd:COG0402 157 FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAeTRDEVEWVLELy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 222 DVDTIEFCSmaedsieiDEQLLDE---IIH--------WD--------ISVCPaISptwpilprvigeER--ADAIcAAV 280
Cdd:COG0402 237 GKRPVEYLD--------ELGLLGPrtlLAHcvhltdeeIAllaetgasVAHCP-TS------------NLklGSGI-APV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 281 LQMAEAGVRLIAGSDAGgrwAGHEGFGLASTLEFYEYLG---------LSNDRIVEMATSEAAQALGVGDKTGRIAVGYS 351
Cdd:COG0402 295 PRLLAAGVRVGLGTDGA---ASNNSLDMFEEMRLAALLQrlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKR 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 2764696544 352 ADLLVVRGN-----PLSD-LSAL------REIREVFAAG 378
Cdd:COG0402 372 ADLVVLDLDaphlaPLHDpLSALvyaadgRDVRTVWVAG 410
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
21-372 |
2.10e-14 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 74.45 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 21 AVLVKDGVIAAVGTREELRA-AHPDEPVLHHADSTLLPGLIDAHAHLASGG----GPDPVAAlgQSVEtTLLEAMRGRAE 95
Cdd:COG1574 29 AVAVRDGRIVAVGSDAEVRAlAGPATEVIDLGGKTVLPGFIDAHVHLLGGGlallGVDLSGA--RSLD-ELLARLRAAAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 96 QLLRSGVTTVR-----DLGDGGHLALRLGDEVAEG--------------------AVAGpriISAGIPITPPGRPGSAPG 150
Cdd:COG1574 106 ELPPGEWILGRgwdesLWPEGRFPTRADLDAVSPDrpvvltrvdghaawvnsaalELAG---ITADTPDPEGGEIERDAD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 151 GEVSG------------------EDEIRALIRR----NASAGaqVTQVMFTGGGGRQFtQAELTAVRLESLAARVRVVAH 208
Cdd:COG1574 183 GEPTGvlreaamdlvraaippptPEELRAALRAalreLASLG--ITSVHDAGLGPDDL-AAYRELAAAGELPLRVVLYLG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 209 AHSRD-----------------------------SI---TAAVAAD------------------VDTIEFCSMA------ 232
Cdd:COG1574 260 ADDEDleellalglrtgygddrlrvggvklfadgSLgsrTAALLEPyaddpgnrglllldpeelRELVRAADAAglqvav 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 233 --------EDSIEIDEQLLDE---------IIH------WDIS------VCPAISPTW-----PILPRVIGEERADAICA 278
Cdd:COG1574 340 haigdaavDEVLDAYEAARAAngrrdrrhrIEHaqlvdpDDLArfaelgVIASMQPTHatsdgDWAEDRLGPERAARAYP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 279 AVlQMAEAGVRLIAGSDA---------------------GGRWAGHEGFGLASTLEFYeylglsndrivemaTSEAAQAL 337
Cdd:COG1574 420 FR-SLLDAGAPLAFGSDApvepldpllgiyaavtrrtpsGRGLGPEERLTVEEALRAY--------------TIGAAYAA 484
|
490 500 510
....*....|....*....|....*....|....*.
gi 2764696544 338 GVGDKTGRIAVGYSADLLVVRGNPLS-DLSALREIR 372
Cdd:COG1574 485 FEEDEKGSLEPGKLADFVVLDRDPLTvPPEEIKDIK 520
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
16-65 |
1.45e-11 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 65.60 E-value: 1.45e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2764696544 16 YITDGAVLVKDGVIAAVGTREELRAAHPDE-PVLHHADSTLLPGLIDAHAH 65
Cdd:PRK09228 28 YIEDGLLLVEDGRIVAAGPYAELRAQLPADaEVTDYRGKLILPGFIDTHIH 78
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
26-363 |
1.56e-11 |
|
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: 65.03 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 26 DGVIAAVGTREELRAAHP--DEPVLHhadstLLPGLIDAHAHLA--SGGGPDPVAALGQSVE--TTLLEAMRG------- 92
Cdd:cd01309 1 DGKIVAVGAEITTPADAEviDAKGKH-----VTPGLIDAHSHLGldEEGGVRETSDANEETDpvTPHVRAIDGinpddea 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 93 --RAeqlLRSGVTTV------RDLGDGGHLALRL-GDEVAEGAVAGPRIISAGIPITPPgRPGSAPGGEVSGEDEIRALI 163
Cdd:cd01309 76 fkRA---RAGGVTTVqvlpgsANLIGGQGVVIKTdGGTIEDMFIKAPAGLKMALGENPK-RVYGGKGKEPATRMGVAALL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 164 RRNASAGAQVTQVMFTG-GGGRQFTQAELtavRLESLAARVR----VVAHAHSRDSITAAV--AADVD---TIEFCSMAE 233
Cdd:cd01309 152 RDAFIKAQEYGRKYDLGkNAKKDPPERDL---KLEALLPVLKgeipVRIHAHRADDILTAIriAKEFGikiTIEHGAEGY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 234 dsieideQLLDEIIHWDISVcpAISPTWpILPRVIgEERADAICAAVLQMAEAGVRLIAGSDAGGRWAGHEGFGLAstlE 313
Cdd:cd01309 229 -------KLADELAKHGIPV--IYGPTL-TLPKKV-EEVNDAIDTNAYLLKKGGVAFAISSDHPVLNIRNLNLEAA---K 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2764696544 314 FYEYlGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVVRGNPLS 363
Cdd:cd01309 295 AVKY-GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLE 343
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
29-372 |
3.67e-11 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 64.47 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 29 IAAVGTREELRAAHPDEPVL-----HH---ADSTLLPGLIDAH----------AHLASGGGP------DPVAALGQSVET 84
Cdd:pfam07969 68 TRFPYALADLDEVAPDGPVLlralhTHaavANSAALDLAGITKatedppggeiARDANGEGLtgllreGAYALPPLLARE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 85 TLLEAMRGRAEQLLRSGVTTVRDLGDGGHlalRLGDEVAEGAVAGPRIISAGIPitPPGRPGSAPGGEVSGEDEIRALIR 164
Cdd:pfam07969 148 AEAAAVAAALAALPGFGITSVDGGGGNVH---SLDDYEPLRELTAAEKLKELLD--APERLGLPHSIYELRIGAMKLFAD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 165 RNASAG-AQVTQVMF--TGGGGRQFTQAELTAVRLESLAARVRVVAHAHSRDSITAAVAA-----------DVDTIEFCS 230
Cdd:pfam07969 223 GVLGSRtAALTEPYFdaPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAfeavaeklgnqGRVRIEHAQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 231 MAEDsieIDEQLLDEI--IHWDISVCPAISPTW-PILPRVIGEERADAIcAAVLQMAEAGVRLIAGSDA-GGRWAGHEGF 306
Cdd:pfam07969 303 GVVP---YTYSQIERVaaLGGAAGVQPVFDPLWgDWLQDRLGAERARGL-TPVKELLNAGVKVALGSDApVGPFDPWPRI 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764696544 307 GLASTLEFYEYLGLSNDR-------IVEMATSEAAQALGVGDKTGRIAVGYSADLLVVRGNPLS-DLSALREIR 372
Cdd:pfam07969 379 GAAVMRQTAGGGEVLGPDeelsleeALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTvDPPAIADIR 452
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1-107 |
6.11e-11 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 63.42 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTW-PRGNYITDGAVLVKDGVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHLASG-------GGP 72
Cdd:PRK07203 2 LLIGNGTAITRdPAKPVIEDGAIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGlargmmaNIP 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2764696544 73 DP-------------------VAALGQSVETTLLEAmrgraeqlLRSGVTTVRD 107
Cdd:PRK07203 82 PPpdfisilknlwwrldraltLEDVYYSALICSLEA--------IKNGVTTVFD 127
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
22-357 |
9.36e-11 |
|
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: 62.66 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 22 VLVKDGVIAAVGTREELRAAHP-DEPVLHHADSTLLPGLIDAHAHL-----------------------ASGGG-PDPVA 76
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPaAAEEIDAGGRAVTPGLVDCHTHLvfagdrvdefaarlagasyeeilAAGGGiLSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 77 ALGQSVETTLLEAMRGRAEQLLRSGVTTVrDLGDGGHL-------ALRLGDEVAEgavAGPRIISA---GIPITPPGRPG 146
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTV-EVKSGYGLdletelkMLRVIRRLKE---EGPVDLVStflGAHAVPPEYKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 147 SAPGGEVSGEDEIRALIRRNASAGAQVtqvmFTGGGgrQFTQAELTAVRLESLAARVRVVAHAhsrDSIT----AAVAAD 222
Cdd:cd01296 157 REEYIDLVIEEVLPAVAEENLADFCDV----FCEKG--AFSLEQSRRILEAAKEAGLPVKIHA---DELSniggAELAAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 223 VDtiefCSMAEDSIEIDEQLLDEIIHwdiSVCPAIsptwpILPRVIGEERADAicAAVLQMAEAGVRLIAGSDAGGRWAG 302
Cdd:cd01296 228 LG----ALSADHLEHTSDEGIAALAE---AGTVAV-----LLPGTAFSLRETY--PPARKLIDAGVPVALGTDFNPGSSP 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2764696544 303 HEGFGLASTLEfYEYLGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVV 357
Cdd:cd01296 294 TSSMPLVMHLA-CRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVIL 347
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
1-357 |
1.09e-09 |
|
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: 59.51 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTwprGNYITDGAVLVKDGVIAAVGTREElraAHPDEPVLHHADSTLLPGLIDAHAHlasGGGpdpvaalGQ 80
Cdd:cd00854 1 LIIKNARILT---PGGLEDGAVLVEDGKIVAIGPEDE---LEEADEIIDLKGQYLVPGFIDIHIH---GGG-------GA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 81 SVETTLLEAMRGRAEQLLRSGVT-----TVRDLGDGGHLALRLGDEVAEGAVaGPRIisAGI----PITPPGRPGSAPGG 151
Cdd:cd00854 65 DFMDGTAEALKTIAEALAKHGTTsflptTVTAPPEEIAKALAAIAEAIAEGQ-GAEI--LGIhlegPFISPEKKGAHPPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 152 --EVSGEDEIRALIRRnasagaqvtqvmfTGGGGRQFTQA-ELTAVR--LESLAARVRVVAHAHS---RDSITAAVAADV 223
Cdd:cd00854 142 ylRAPDPEELKKWLEA-------------AGGLIKLVTLApELDGALelIRYLVERGIIVSIGHSdatYEQAVAAFEAGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 224 DTIE--FCSM---------AEDSIEIDEQLLDEIIHWDISVCPAispTWPILPRVIGEERA----DAICAA--------- 279
Cdd:cd00854 209 THVThlFNAMsplhhrepgVVGAALSDDDVYAELIADGIHVHPA---AVRLAYRAKGADKIvlvtDAMAAAglpdgeyel 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 280 ---VLQMAEAGVRLIAGSDAGgrwaghegfglaSTL-------EFYEYLGLSNDRIVEMATSEAAQALGVGDKTGRIAVG 349
Cdd:cd00854 286 ggqTVTVKDGVARLADGTLAG------------STLtmdqavrNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPG 353
|
....*...
gi 2764696544 350 YSADLLVV 357
Cdd:cd00854 354 KDADLVVL 361
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-358 |
2.47e-09 |
|
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: 58.37 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTWPRGNYITDGAVLVKDGVIAAVGTREELRAAHPDEpVLHHADSTLLPGLIDAHAHLASG---GGPD---- 73
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADE-VIDAKGKVVMPGLVNTHTHLAMTllrGLADdlpl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 74 ---------PVAAL------GQSVETTLLEamrgraeqLLRSGVTTVRDlgdggHLALrLGDEVAEGAV-AGPR-IISAG 136
Cdd:cd01298 80 mewlkdliwPLERLlteedvYLGALLALAE--------MIRSGTTTFAD-----MYFF-YPDAVAEAAEeLGIRaVLGRG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 137 IpitpPGRPGSAPGGEVSGEDEIRALIRRNASAGAQVTQVMFtggGGRQ-FTQAELTAVRLESLAARVRVVAHAHsrdsi 215
Cdd:cd01298 146 I----MDLGTEDVEETEEALAEAERLIREWHGAADGRIRVAL---APHApYTCSDELLREVAELAREYGVPLHIH----- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 216 TAAVAADVDTI---------EFC---------SMAEDSIEIDEQLLDEIIHWDISV--CPA--------ISPtwpilprv 267
Cdd:cd01298 214 LAETEDEVEESlekygkrpvEYLeelgllgpdVVLAHCVWLTDEEIELLAETGTGVahNPAsnmklasgIAP-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 268 igeeradaicaaVLQMAEAGVRLIAGSDAGGRWAGHEGFG---LASTLE---FYEYLGLSNDRIVEMATSEAAQALGVgD 341
Cdd:cd01298 286 ------------VPEMLEAGVNVGLGTDGAASNNNLDMFEemrLAALLQklaHGDPTALPAEEALEMATIGGAKALGL-D 352
|
410
....*....|....*..
gi 2764696544 342 KTGRIAVGYSADLLVVR 358
Cdd:cd01298 353 EIGSLEVGKKADLILID 369
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-70 |
3.14e-09 |
|
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: 58.47 E-value: 3.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2764696544 21 AVLVKDGVIAAVGTREELRA-AHPDEPVLHHADSTLLPGLIDAHAHLASGG 70
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlKGPATEVIDLKGKTVLPGFIDSHSHLLLGG 51
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-377 |
7.53e-09 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.93 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTWPRGNYITDGAVLVKDGVIAAVGTREELRAAhPDepVLHHADSTLLPGLIDAHAHLasgggpdpVAAL-- 78
Cdd:PRK07228 3 ILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDY-DD--HIDATGKVVIPGLIQGHIHL--------CQTLfr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 79 GQSVETTLL----------------EAMRGRAE----QLLRSGVTTVRDlgdggHLALRLGDEVAEGAV-AGPRIISaGI 137
Cdd:PRK07228 72 GIADDLELLdwlkdriwpleaahdaESMYYSALlgigELIESGTTTIVD-----MESVHHTDSAFEAAGeSGIRAVL-GK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 138 PITPPGRpGSAPGGEVSGEDEIR---ALIRRNASAGAQVTQVMFTGGGGRQFTQAELTAVRleSLAAR--VRVVAHAHSR 212
Cdd:PRK07228 146 VMMDYGD-DVPEGLQEDTEASLAesvRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVR--DLADEygVRIHTHASEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 213 DSITAAVAAD--------VDTI----EFCSMAEdSIEIDEQLLDEIIHWDISV--CPAISptwpilprvigEERADAIcA 278
Cdd:PRK07228 223 RGEIETVEEEtgmrnihyLDEVgltgEDLILAH-CVWLDEEEREILAETGTHVthCPSSN-----------LKLASGI-A 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 279 AVLQMAEAGVRLIAGSDAGGRWAGHEGFG---LASTLEFYEYLG---LSNDRIVEMATSEAAQALGVGDKTGRIAVGYSA 352
Cdd:PRK07228 290 PVPDLLERGINVALGADGAPCNNTLDPFTemrQAALIQKVDRLGptaMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKA 369
|
410 420 430
....*....|....*....|....*....|
gi 2764696544 353 DLLVV-----RGNPLSDLSALREIreVFAA 377
Cdd:PRK07228 370 DLAILdldglHATPSHGVDVLSHL--VYAA 397
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
2-104 |
4.06e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 54.72 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 2 LIHASRVLTwPRGNyITDGAVLVKDGVIAAVGtreelRAAHPDEPVLHHADSTLLPGLIDAHAHlasGGGpdpvaalGQS 81
Cdd:COG1820 1 AITNARIFT-GDGV-LEDGALLIEDGRIAAIG-----PGAEPDAEVIDLGGGYLAPGFIDLHVH---GGG-------GVD 63
|
90 100
....*....|....*....|...
gi 2764696544 82 VETTLLEAMRGRAEQLLRSGVTT 104
Cdd:COG1820 64 FMDGTPEALRTIARAHARHGTTS 86
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
16-105 |
1.45e-07 |
|
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: 53.05 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 16 YITDGAVLVKDGVIAAVGTREEL-RAAHPDEPVLHHADSTLLPGLIDAHAH------LASGGGPdpvaALGQSVET-TLL 87
Cdd:cd01303 23 VVEDGLIVVVDGNIIAAGAAETLkRAAKPGARVIDSPNQFILPGFIDTHIHapqyanIGSGLGE----PLLDWLETyTFP 98
|
90 100 110
....*....|....*....|....*....|
gi 2764696544 88 EAMR-----------GRA-EQLLRSGVTTV 105
Cdd:cd01303 99 EEAKfadpayarevyGRFlDELLRNGTTTA 128
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
17-360 |
2.74e-07 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 52.03 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 17 ITDGAVLVKDGVIAAVGTREELRAAHPDEPVlHHADSTLLPGLIDAHAH-----------------------LASGGG-P 72
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGEEATEII-DCGGGLVTPGLVDPHTHlvfagdrvnefemklqgasyleiLAQGGGiL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 73 DPVAALGQSVETTLLEAMRGRAEQLLRSGVTTVrDLGDGGHL----ALRLGDEVAEGAVAGPRIISA---GIPITPPGRP 145
Cdd:TIGR01224 80 STVRATRAASEEELLKLALFRLKSMLRSGTTTA-EVKSGYGLdletELKMLRAAKALHEEQPVDVVTtflGAHAVPPEFQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 146 GSaPGGEVSG--EDEIRALIRRNASAGAQV--TQVMFTGGGGRQFTQA-------------ELTAVRLESLAARVrvvaH 208
Cdd:TIGR01224 159 GR-PDDYVDGicEELIPQVAEEGLASFADVfcEAGVFSVEQSRRILQAaqeaglpvklhaeELSNLGGAELAAKL----G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 209 AHSRDSITAAVAADVDtiefcSMAEDSieideqlldeiihwdisvcpAISPTWPILPRVIGEERADAicaavLQMAEAGV 288
Cdd:TIGR01224 234 AVSADHLEHASDAGIK-----ALAEAG--------------------TVAVLLPGTTFYLRETYPPA-----RQLIDYGV 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764696544 289 RLIAGSDAGGRWAGHEGFGLASTLEFYEYLgLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVVRGN 360
Cdd:TIGR01224 284 PVALATDLNPGSSPTLSMQLIMSLACRLMK-MTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAP 354
|
|
| PLN02795 |
PLN02795 |
allantoinase |
3-66 |
6.24e-07 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 51.32 E-value: 6.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764696544 3 IHASRVLTwPRGnyITDGAVLVKDGVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHL 66
Cdd:PLN02795 48 LYSKRVVT-PAG--VIPGAVEVEGGRIVSVTKEEEAPKSQKKPHVLDYGNAVVMPGLIDVHVHL 108
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
2-66 |
6.62e-07 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 51.12 E-value: 6.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764696544 2 LIHASRVLTwPRGNY--ITDGAVLVkDGVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHL 66
Cdd:PRK08418 3 IIGASYIFT-CDENFeiLEDGAVVF-DDKILEIGDYENLKKKYPNAKIQFFKNSVLLPAFINPHTHL 67
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
22-379 |
1.23e-06 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 49.94 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 22 VLVKDGVIAAVGTREElraAHPDEPVLHHADSTLLPGLIDAHAHLASG--GGPDPVAALGQSVE----------TTLLEA 89
Cdd:cd01293 17 IAIEDGRIAAIGPALA---VPPDAEEVDAKGRLVLPAFVDPHIHLDKTftGGRWPNNSGGTLLEaiiaweerklLLTAED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 90 MRGRAEQLLR----SGVTTVR---DLGDG-GHLALRLGDEVAEgAVAGprIISAGIPITPPGRPGSAPGGEvsgedeirA 161
Cdd:cd01293 94 VKERAERALElaiaHGTTAIRthvDVDPAaGLKALEALLELRE-EWAD--LIDLQIVAFPQHGLLSTPGGE--------E 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 162 LIRRNASAGAQVtqvmftGGGGRQFTQAELTAVRLE---SLAAR--VRVVAHAHSRDSITAA----VAADVDTIEF---- 228
Cdd:cd01293 163 LMREALKMGADV------VGGIPPAEIDEDGEESLDtlfELAQEhgLDIDLHLDETDDPGSRtleeLAEEAERRGMqgrv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 229 -----CSMAEDSIEIDEQLLDEIIHWDISVCPAISPTWPILPRVIGEERADAIcAAVLQMAEAGVRLIAGS----DAGGR 299
Cdd:cd01293 237 tcshaTALGSLPEAEVSRLADLLAEAGISVVSLPPINLYLQGREDTTPKRRGV-TPVKELRAAGVNVALGSdnvrDPWYP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 300 WAGHEGFGLAS-TLEFYEYLGLSND-RIVEMATSEAAQALGVGDktGRIAVGYSADLLVVRGNPLSDLSALR-EIREVFA 376
Cdd:cd01293 316 FGSGDMLEVANlAAHIAQLGTPEDLaLALDLITGNAARALGLED--YGIKVGCPADLVLLDAEDVAEAVARQpPRRVVIR 393
|
...
gi 2764696544 377 AGT 379
Cdd:cd01293 394 KGR 396
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
1-67 |
1.35e-06 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 49.91 E-value: 1.35e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764696544 1 MLIHASRVLTW-PRGNYITDGAVLVKDGVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHLA 67
Cdd:PRK09045 9 LLIEARWIVPVePAGVVLEDHAVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLINAHTHAA 76
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
27-108 |
2.60e-06 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 48.98 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 27 GVIAAVGTREELRAAHPDEPVLHHADSTLLPGLIDAHAHLASGGGP------------DPV-----AALGQSVETTLLEA 89
Cdd:cd01312 1 DKILEVGDYEKLEKRYPGAKHEFFPNGVLLPGLINAHTHLEFSANVaqftygrfrawlLSVinsrdELLKQPWEEAIRQG 80
|
90
....*....|....*....
gi 2764696544 90 MRgraeQLLRSGVTTVRDL 108
Cdd:cd01312 81 IR----QMLESGTTSIGAI 95
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
59-336 |
7.52e-06 |
|
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: 46.94 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 59 LIDAHAHLASGGGPDPVAALGQS-----VETTLLEAMRGRAEQLLRSGVTTVRDLGDGGHL--ALRLGDEVAEGAVAGPR 131
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKeaeelSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPttTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 132 IISAGIPITPPGRPGSAPGGEVSGEDEIRALIRRNASAGAQVTQVMFTGGGGRQFTQAELTAVRLESLaarvrVVAHAHS 211
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARKLGLP-----VVIHAGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 212 RDSITAAVAADVD--------TIEFCSMAEDSIEidEQLLDEIIHwdISVCPAISPtwPILPRVIGEERADAICaavlqm 283
Cdd:cd01292 156 LPDPTRALEDLVAllrlggrvVIGHVSHLDPELL--ELLKEAGVS--LEVCPLSNY--LLGRDGEGAEALRRLL------ 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2764696544 284 aEAGVRLIAGSDAGGRWAGHEGFGLASTLEFYEYLGLSNDRIVEMATSEAAQA 336
Cdd:cd01292 224 -ELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
2-71 |
2.36e-05 |
|
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: 46.24 E-value: 2.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 2 LIHASRVLTwPRGNYITDgaVLVKDGVIAAVGtrEELRAAHPDEpVLHHADSTLLPGLIDAHAHLASGGG 71
Cdd:COG0044 1 LIKNGRVVD-PGGLERAD--VLIEDGRIAAIG--PDLAAPEAAE-VIDATGLLVLPGLIDLHVHLREPGL 64
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
22-112 |
3.98e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 45.16 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 22 VLVKDGVIAAVGTREELRAAhpdEPVLHHADSTLLPGLIDAHAHLASGGG-----PDPVAalgqsvettlleamrgraeq 96
Cdd:COG3964 22 IAIKDGKIAAVAKDIDAAEA---KKVIDASGLYVTPGLIDLHTHVFPGGTdygvdPDGVG-------------------- 78
|
90
....*....|....*.
gi 2764696544 97 lLRSGVTTVRDLGDGG 112
Cdd:COG3964 79 -VRSGVTTVVDAGSAG 93
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-66 |
4.09e-05 |
|
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: 45.36 E-value: 4.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764696544 1 MLIHASRVLTwprGNYITDGAVLVKDGVIAAVGTREELRAAhpdEPVLHHADSTLLPGLIDAHAHL 66
Cdd:cd01315 2 LVIKNGRVVT---PDGVREADIAVKGGKIAAIGPDIANTEA---EEVIDAGGLVVMPGLIDTHVHI 61
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
16-365 |
5.02e-05 |
|
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: 44.98 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 16 YITDgaVLVKDGVIAAVGTReelrAAHPDEPVLHHADSTLLPGLIDAHAH--LASGGGPDPVAALGQSVETTLL------ 87
Cdd:cd01297 18 FTAD--VGIRDGRIAAIGPI----LSTSAREVIDAAGLVVAPGFIDVHTHydGQVFWDPDLRPSSRQGVTTVVLgncgvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 88 -EAMRGRAEQLLRSGVTTVRDLGDGGHLALRLGDEVAEGAVAGPRIISAGIPItppgrPGSAPGGEVSGED--------- 157
Cdd:cd01297 92 pAPANPDDLARLIMLMEGLVALGEGLPWGWATFAEYLDALEARPPAVNVAALV-----GHAALRRAVMGLDareateeel 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 158 -EIRALIRRNASAGAQVTQVMFTGGGGRQFTQAELTAvrLESLAARVRVVAHAHSRDSITAAVAADVDTIEF-------- 228
Cdd:cd01297 167 aKMRELLREALEAGALGISTGLAYAPRLYAGTAELVA--LARVAARYGGVYQTHVRYEGDSILEALDELLRLgretgrpv 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 229 ------CSMAEDSIEIDEQL--LDEIIHWDISVcpaispTWPILPRVIGEEradaicAAVLQMAEAGVRLIaGSDAGGRW 300
Cdd:cd01297 245 hishlkSAGAPNWGKIDRLLalIEAARAEGLQV------TADVYPYGAGSE------DDVRRIMAHPVVMG-GSDGGALG 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764696544 301 AGHEG----FGLASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKtGRIAVGYSADLLVVRGNPLSDL 365
Cdd:cd01297 312 KPHPRsygdFTRVLGHYVRERKLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADR 379
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
15-108 |
8.36e-05 |
|
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: 44.36 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 15 NYITDGAVLVKDGVIAAVGtreeLRAAHPDEPVLHHADSTLLPGLIDAHAHLASGGGPDPvaalgQSVETTLLEAMRGra 94
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIG----KLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYK-----EDIESGSKAAAHG-- 69
|
90
....*....|....
gi 2764696544 95 eqllrsGVTTVRDL 108
Cdd:TIGR00857 70 ------GFTTVADM 77
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
17-108 |
2.90e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 42.45 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 17 ITDGAVLVKDGVIAAVGTREElraahPDEPVLHHADSTLLPGLIDAHAHLAsgggpDPVAALGQSVETTLLEAMRGraeq 96
Cdd:PRK04250 12 IVEGGIGIENGRISKISLRDL-----KGKEVIKVKGGIILPGLIDVHVHLR-----DFEESYKETIESGTKAALHG---- 77
|
90
....*....|..
gi 2764696544 97 llrsGVTTVRDL 108
Cdd:PRK04250 78 ----GITLVFDM 85
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
319-372 |
4.13e-04 |
|
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: 41.94 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2764696544 319 GLSNDRIVEMATSEAAQALGVGDKtGRIAVGYSADLLVVrgnplsDLSALREIR 372
Cdd:cd01318 286 ILSLSRVVRLTSHNPARIFGIKNK-GRIAEGYDADLTVV------DLKEERTIR 332
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
1-107 |
4.17e-04 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 42.36 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLI-HASRVLTWPRGNYITDGA--VLVKDGVIAAVGTREelraAHPDEPVLHHADSTLLPGLIDAHAHLASG---GGPD- 73
Cdd:PRK12393 4 LLIrNAAAIMTGLPGDAARLGGpdIRIRDGRIAAIGALT----PLPGERVIDATDCVVYPGWVNTHHHLFQSllkGVPAg 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2764696544 74 ------------PVAALGQSVETTLLEAMR-GRAEqLLRSGVTTVRD 107
Cdd:PRK12393 80 inqsltawlaavPYRFRARFDEDLFRLAARiGLVE-LLRSGCTTVAD 125
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
326-384 |
4.87e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.70 E-value: 4.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764696544 326 VEMATSEAAQALGVGDKtGRIAVGYSADLLVVRgnplsDLSALREIREVFAAGTRCHSA 384
Cdd:PRK15446 330 VALVTANPARAAGLDDR-GEIAPGKRADLVRVR-----RAGGLPVVRAVWRGGRRVFLA 382
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
306-358 |
5.22e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 41.76 E-value: 5.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2764696544 306 FGLASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKtGRIAVGYSADLLVVR 358
Cdd:PRK09237 282 YSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPEL-GRLQVGSDADLTLFT 333
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
320-368 |
6.91e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 41.44 E-value: 6.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2764696544 320 LSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVVrgnplsDLSAL 368
Cdd:PRK09045 340 LPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAV------DLSGL 382
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
318-359 |
7.99e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 41.14 E-value: 7.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2764696544 318 LGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLVVRG 359
Cdd:PRK08204 340 LTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDA 381
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
306-358 |
9.09e-04 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 40.77 E-value: 9.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2764696544 306 FGLASTLEFYEYLGLSNDRIVEMATSEAAQALGVGDKtGRIAVGYSADLLVVR 358
Cdd:cd01307 263 YALATTLSKLLALGMPLEEVIEAVTANPARMLGLAEI-GTLAVGYDADLTVFD 314
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-105 |
9.51e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 40.95 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTWPRGNYITDgaVLVKDGVIAAVGTREelraAHPDEPVLHHADSTLLPGLIDAHAHLASGGGPDPvaalgQ 80
Cdd:PRK09357 3 ILIKNGRVIDPKGLDEVAD--VLIDDGKIAAIGENI----EAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDK-----E 71
|
90 100
....*....|....*....|....*
gi 2764696544 81 SVETTLLEAMRGraeqllrsGVTTV 105
Cdd:PRK09357 72 TIETGSRAAAAG--------GFTTV 88
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
22-66 |
1.24e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 40.69 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2764696544 22 VLVKDGVIAAVGTReelRAAHPDEPVLHHADSTLLPGLIDAHAHL 66
Cdd:PRK05985 19 ILIRDGRIAAIGPA---LAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-125 |
1.84e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 1 MLIHASRVLTwprGNYITDGAVLVKDGVIAAVGTREELRAAHPDEpvlhhADSTLLPGLIDAH-----AHLAsgggPDPv 75
Cdd:PRK15446 4 MILSNARLVL---PDEVVDGSLLIEDGRIAAIDPGASALPGAIDA-----EGDYLLPGLVDLHtdnleKHLA----PRP- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2764696544 76 aalgqSVETTLLEAMRGRAEQLLRSGVTTVRDlgdgghlALRLGDEVAEG 125
Cdd:PRK15446 71 -----GVDWPADAALAAHDAQLAAAGITTVFD-------ALSVGDEEDGG 108
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
316-356 |
2.11e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.96 E-value: 2.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2764696544 316 EYLGLSNDRIVEMATSEAAQALGVGDKTGRIAVGYSADLLV 356
Cdd:PRK11170 322 EHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTA 362
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
22-109 |
2.30e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 39.83 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764696544 22 VLVKDGVIAAVGTREElraAHPDEPVLHHADSTLLPGLIDAHAHLASGGG-----PDPVAAlgqsvettlleamrgraeq 96
Cdd:PRK09237 21 IAIEDGKIAAVAGDID---GSQAKKVIDLSGLYVSPGWIDLHVHVYPGSTpygdePDEVGV------------------- 78
|
90
....*....|...
gi 2764696544 97 llRSGVTTVRDLG 109
Cdd:PRK09237 79 --RSGVTTVVDAG 89
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-68 |
4.94e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 38.93 E-value: 4.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2764696544 17 ITDGAVLVKDGVIAAVGTreelrAAHPDEPVLHHADSTLLPGLIDAHAHLAS 68
Cdd:COG1001 22 ILEGDIAIAGGRIAGVGD-----YIGEATEVIDAAGRYLVPGFIDGHVHIES 68
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
320-381 |
5.07e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 38.75 E-value: 5.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764696544 320 LSNDRIVEMATSEAAQALGVGDKtGRIAVGYSADLLVVrgnplsDLSALREIREVFAAgTRC 381
Cdd:PRK09060 344 LSLERFVDLTSAGPARIFGIAGK-GRIAVGYDADFTIV------DLKRRETITNEWIA-SRC 397
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1-68 |
5.84e-03 |
|
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: 38.74 E-value: 5.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764696544 1 MLIHASRVLTwPRGNYITDgaVLVKDGVIAAVGTREElraAHPDEPVLHHADSTLLPGLIDAHAHLAS 68
Cdd:cd01314 1 LIIKNGTIVT-ADGSFKAD--ILIEDGKIVAIGPNLE---APGGVEVIDATGKYVLPGGIDPHTHLEL 62
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
12-65 |
6.07e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 38.48 E-value: 6.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2764696544 12 PRGNYITDGAVLVKDGVIAAVGtrEELRAAHPDEpVLHHADSTLLPGLIDAHAH 65
Cdd:PRK02382 12 YYNNSLQPRDVRIDGGKITAVG--KDLDGSSSEE-VIDARGMLLLPGGIDVHVH 62
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
328-378 |
6.38e-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: 38.41 E-value: 6.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764696544 328 MATSEAAQALGVGDKTGRIAVGYSADLLVV----------RGNPLSDLSAL----------REIREVFAAG 378
Cdd:cd01303 359 LATLGGAEALGLDDKIGNFEVGKEFDAVVIdpsatplladRMFRVESLEEAlfkflylgddRNIREVYVAG 429
|
|
| |
