|
Name |
Accession |
Description |
Interval |
E-value |
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
36-418 |
6.31e-110 |
|
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: 328.64 E-value: 6.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 36 GRIGDLGTLQRLRRDHPVPIID-HPGCAILPGFINAHTHLELTHFPSwrlrsQLeeHPQRFVDWIIQLIKVKRGLTPDDM 114
Cdd:cd01312 1 DKILEVGDYEKLEKRYPGAKHEfFPNGVLLPGLINAHTHLEFSANVA-----QF--TYGRFRAWLLSVINSRDELLKQPW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 115 RASAREGIRMCLESGTTAVGEIVTARTLAPLYRGSRLSGRLFFELVGHDNSRFRELLREAVEL---SGESPAGSFSAGLS 191
Cdd:cd01312 74 EEAIRQGIRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERfkrSKSFESQLFIPAIS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 192 PHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFSSSGqlaerfYPFVGWERYLPPPR---RCSTSQLLERAG 268
Cdd:cd01312 154 PHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKG------WFKHFWESFLKLPKpkkLATAIDFLDMLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 269 LLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFALD 348
Cdd:cd01312 228 GLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLD 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118504519 349 AFGDELS---PADLFRMVTLGGATALGIqgDHGSLEKGKRADFQI--VGQAGKRESGLVERVMLRGVVEDVYVAG 418
Cdd:cd01312 308 LHPEEDLlelASELLLMATLGGARALGL--NNGEIEAGKRADFAVfeLPGPGIKEQAPLQFILHAKEVRHLFISG 380
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
10-420 |
1.57e-93 |
|
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: 287.88 E-value: 1.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 10 SFIVAASWLLS--PEAPPLAGGALLVRRGRIGDLGTLQRLRRDHP-VPIIDHPGCAILPGFINAHTHLELTHFpswrlRS 86
Cdd:COG0402 1 DLLIRGAWVLTmdPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPaAEVIDAGGKLVLPGLVNTHTHLPQTLL-----RG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 87 QLEEHPqrFVDWIIQLI-KVKRGLTPDDMRASAREGIRMCLESGTTAVGEIVT-----ARTLAPLYRGSRLSGRLFFELV 160
Cdd:COG0402 76 LADDLP--LLDWLEEYIwPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYvhpesADALAEAAAEAGIRAVLGRGLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 161 GHDN-----SRFRELLREAVEL---SGESPAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVF 232
Cdd:COG0402 154 DRGFpdglrEDADEGLADSERLierWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 233 SSSGQlaerfypfvgweRYLppprrcstsQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRA 312
Cdd:COG0402 234 ELYGK------------RPV---------EYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 313 PVALLRKLGIPLALGTDSLASNDSLSLWDELRFAL------DAFGDELSPADLFRMVTLGGATALGIQGDHGSLEKGKRA 386
Cdd:COG0402 293 PVPRLLAAGVRVGLGTDGAASNNSLDMFEEMRLAAllqrlrGGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRA 372
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 118504519 387 DFQIVGQAGKRESGLVERV------MLRGVVEDVYVAGER 420
Cdd:COG0402 373 DLVVLDLDAPHLAPLHDPLsalvyaADGRDVRTVWVAGRV 412
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
26-419 |
3.52e-70 |
|
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: 227.47 E-value: 3.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 26 LAGGALLVRRGRIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHlelthFPSWRLRSQLEEHPqrFVDWIIQLIKV 105
Cdd:cd01298 17 LEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTH-----LAMTLLRGLADDLP--LMEWLKDLIWP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 106 -KRGLTPDDMRASAREGIRMCLESGTTAV-------GEIV--TARTLaplyrGSR-LSGRLFFELVGHDNSRFRELLREA 174
Cdd:cd01298 90 lERLLTEEDVYLGALLALAEMIRSGTTTFadmyffyPDAVaeAAEEL-----GIRaVLGRGIMDLGTEDVEETEEALAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 175 VELSGES---PAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFsssgqlaerfypfvgwERY 251
Cdd:cd01298 165 ERLIREWhgaADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL----------------EKY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 252 lppprRCSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSL 331
Cdd:cd01298 229 -----GKRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 332 ASNDSLSLWDELRFAL----DAFGDE--LSPADLFRMVTLGGATALGIqGDHGSLEKGKRADFQIVGQAGKRESGLVE-- 403
Cdd:cd01298 304 ASNNNLDMFEEMRLAAllqkLAHGDPtaLPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDpi 382
|
410 420
....*....|....*....|
gi 118504519 404 ----RVMLRGVVEDVYVAGE 419
Cdd:cd01298 383 shlvYSANGGDVDTVIVNGR 402
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
11-391 |
3.39e-47 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 167.07 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 11 FIVAASWLLSPEAPP--LAGGALLVRrGRIGDLGTLQRLRRDHP-VPIIDHPGCAILPGFINAHTHLElthFPSwrLRSQ 87
Cdd:PRK08418 2 KIIGASYIFTCDENFeiLEDGAVVFD-DKILEIGDYENLKKKYPnAKIQFFKNSVLLPAFINPHTHLE---FSA--NKTT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 88 LEEhpQRFVDWIIQLIKVKRGLTPDDMRASAREGIRMCLESGTTAVGEIVTARTLAPLYRGSRLSGRLFFELVGHDNS-- 165
Cdd:PRK08418 76 LDY--GDFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASav 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 166 -----RFRELLREAVELSGESpagsFSAGLSPHAPYTLGEEtfpLIREA---AAGASLPLAIHCSESTEETNFVFSSSGQ 237
Cdd:PRK08418 154 delyqDFLARFEESKKFKSKK----FIPAIAIHSPYSVHPI---LAKKAlqlAKKENLLVSTHFLESKAEREWLEESKGW 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 238 LAERFypfvgwERYLPPPRRCSTSQllERAGLLTD-STLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVAL 316
Cdd:PRK08418 227 FKKFF------EKFLKEPKPLYTPK--EFLELFKGlRTLFTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEK 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118504519 317 LRKLGIPLALGTDSLASNDSLSLWDELRFALDAFGD----ELSpADLFRMVTLGGATALGIqgDHGSLEKGKRADFQIV 391
Cdd:PRK08418 299 AKKAGINYSIATDGLSSNISLSLLDELRAALLTHANmpllELA-KILLLSATRYGAKALGL--NNGEIKEGKDADLSVF 374
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
12-419 |
1.99e-45 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 163.16 E-value: 1.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 12 IVAASWLL--SPEAPPLAGGALLVRRGRIGD-LGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHLELTHF-------Ps 81
Cdd:PRK09045 10 LIEARWIVpvEPAGVVLEDHAVAIRDGRIVAiLPRAEARARYAAAETVELPDHVLIPGLINAHTHAAMSLLrgladdlP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 82 wrLRSQLEEH--P--QRFVDwiiqlikvkrgltPDDMRASAREGIRMCLESGTTAVGEI-----VTARtlAPLYRGSRls 152
Cdd:PRK09045 89 --LMTWLQDHiwPaeGAWVS-------------EEFVRDGTLLAIAEMLRGGTTCFNDMyffpeAAAE--AAHQAGMR-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 153 GRLFFELV------GHDNSrfrELLREAVELSGE---SPAGSFSagLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSE 223
Cdd:PRK09045 150 AQIGMPVLdfptawASDAD---EYLAKGLELHDQwrhHPLISTA--FAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 224 STEETNFVFSSSGQlaerfypfvgweRYLppprrcstsQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRS 303
Cdd:PRK09045 225 TAQEIADSLKQHGQ------------RPL---------ARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPES 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 304 NERLDVGRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFA-LDAFGDELSPADL-----FRMVTLGGATALGIQGDH 377
Cdd:PRK09045 284 NLKLASGFCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTAaLLAKAVAGDATALpahtaLRMATLNGARALGLDDEI 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 118504519 378 GSLEKGKRADFQIVGQAGKRE-------SGLVERVMlRGVVEDVYVAGE 419
Cdd:PRK09045 364 GSLEPGKQADLVAVDLSGLETqpvydpvSQLVYAAG-REQVSHVWVAGK 411
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
8-391 |
2.61e-43 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 156.83 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 8 NDSFIVAASWLLSPEAPPLAGGALLVRRGRIGDLGTLQRLRRDHpvpIIDHPGCAILPGFINAHTHLELTHFPSWRLRSQ 87
Cdd:PRK06038 1 MADIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADT---VIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 88 LEEhpqrfvdWIIQLI-KVKRGLTPDDMRASAREGirmCLE---SGTTAVGEIV-----TARTLaplyRGSRLSGRLFFE 158
Cdd:PRK06038 78 LAE-------WLNDHIwPAEAKLTAEDVYAGSLLA---CLEmikSGTTSFADMYfymdeVAKAV----EESGLRAALSYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 159 LV--GHDNSRFRELL--REAVELSGESPAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNfvfss 234
Cdd:PRK06038 144 MIdlGDDEKGEAELKegKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELN----- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 235 sgQLAERFypfvgwerylpppRRCSTsQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPV 314
Cdd:PRK06038 219 --QMKEQY-------------GMCSV-NYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 315 ALLRKLGIPLALGTDSLASNDSLSLWDELRFA-----LDAFGDELSPA-DLFRMVTLGGATALGIqgDHGSLEKGKRADF 388
Cdd:PRK06038 283 PKLLERGVNVSLGTDGCASNNNLDMFEEMKTAallhkVNTMDPTALPArQVLEMATVNGAKALGI--NTGMLKEGYLADI 360
|
...
gi 118504519 389 QIV 391
Cdd:PRK06038 361 IIV 363
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
63-419 |
3.30e-43 |
|
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: 154.20 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 63 ILPGFINAHTHLELTHFPSWRLRSQLEEHpqRFVDWIIQLIKvkRGLTP-DDMRASAREGIRMCLEsgttAVGEIVtart 141
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRGIPVPPEFAYE--ALRLGITTMLK--SGTTTvLDMGATTSTGIEALLE----AAEELP---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 142 LAPLYRGSRLSGRLFFELVGHDNSRfRELLREAVELSGESPAGSFsAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHC 221
Cdd:pfam01979 70 LGLRFLGPGCSLDTDGELEGRKALR-EKLKAGAEFIKGMADGVVF-VGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 222 SESTEETnfvfsssgQLAERFYPfVGWERYLPPprrcstsQLLERAGLLTDSTLAI-HCVQVSRADAEILRKR--GVSVA 298
Cdd:pfam01979 148 LETKGEV--------EDAIAAFG-GGIEHGTHL-------EVAESGGLLDIIKLILaHGVHLSPTEANLLAEHlkGAGVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 299 LCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFALDAFGDE---LSPADLFRMVTLGGATALGIQG 375
Cdd:pfam01979 212 HCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPeggLSPLEALRMATINPAKALGLDD 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 118504519 376 DHGSLEKGKRADFQIVgqAGKRESGLVErVMLRGVVEDVYVAGE 419
Cdd:pfam01979 292 KVGSIEVGKDADLVVV--DLDPLAAFFG-LKPDGNVKKVIVKGK 332
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
29-420 |
7.63e-36 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 136.67 E-value: 7.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 29 GALLVRRGRIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHLELTHFPSWRLRSQLEEhpqrfvdWIIQLI-KVKR 107
Cdd:PRK06687 22 GILAVKDSQIVYVGQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHE-------WLNDYIwPAES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 108 GLTPDDMRASAREGIRMCLESGTTAVGEIVTAR--TLAPLYRGSRLSG-RLFF---------ELVGHDNSRFRELLREAV 175
Cdd:PRK06687 95 EFTPDMTTNAVKEALTEMLQSGTTTFNDMYNPNgvDIQQIYQVVKTSKmRCYFsptlfssetETTAETISRTRSIIDEIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 176 ELSGESpagsFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFsssgqlaerfypfvgwERYLPPP 255
Cdd:PRK06687 175 KYKNPN----FKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIIL----------------KRYGKRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 256 RrcstsQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASND 335
Cdd:PRK06687 235 L-----AFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVASNN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 336 SLSLWDELRFAldAFGDELSPAD--------LFRMVTLGGATALGIQGDHGSLEKGKRADFQIVGQAGKRESGLVERVML 407
Cdd:PRK06687 310 NLDMFEEGRTA--ALLQKMKSGDasqfpietALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGKIHLQPQENMLS 387
|
410 420
....*....|....*....|
gi 118504519 408 RGV-------VEDVYVAGER 420
Cdd:PRK06687 388 HLVyavkssdVDDVYIAGEQ 407
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
55-391 |
2.16e-33 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 129.92 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 55 IIDHPGCAILPGFINAHTHLelthfPSWRLRSQLEEHPqrFVDWIIQLI-KVKRGLTPDDMRASAREGIRMCLESGTTA- 132
Cdd:PRK08393 44 VIDASGSVVSPGFINAHTHS-----PMVLLRGLADDVP--LMEWLQNYIwPRERKLKRKDIYWGAYLGLLEMIKSGTTTf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 133 VGEIVTARTLAPLYRGSRLSGRLFFELVGHDNSRFREL-LREAVEL-----SGESPAGSFSagLSPHAPYTLGEETFPLI 206
Cdd:PRK08393 117 VDMYFHMEEVAKATLEVGLRGYLSYGMVDLGDEEKREKeIKETEKLmefieKLNSPRVHFV--FGPHAPYTCSLALLKWV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 207 REAAAGASLPLAIHCSESTEETnfvfsssGQLAERFYPfvgwerylppprrcSTSQLLERAGLLTDSTLAIHCVQVSRAD 286
Cdd:PRK08393 195 REKAREWNKLITIHLSETMDEI-------KQIREKYGK--------------SPVVLLDEIGFLNEDVIAAHGVWLSSRD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 287 AEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFA-LDAFGDELSPA-----DLF 360
Cdd:PRK08393 254 IRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDMLREMKLAaLLHKVHNLDPTiadaeTVF 333
|
330 340 350
....*....|....*....|....*....|.
gi 118504519 361 RMVTLGGATALGIQGdhGSLEKGKRADFQIV 391
Cdd:PRK08393 334 RMATQNGAKALGLKA--GVIKEGYLADIAVI 362
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
29-391 |
4.44e-32 |
|
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: 126.24 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 29 GALLVRRGRIGDLGTLQRLRRDHP--VPIIDHPGCAILPGFINAHTHlelthFPSWR-----LRSQL----------EEH 91
Cdd:cd01303 27 GLIVVVDGNIIAAGAAETLKRAAKpgARVIDSPNQFILPGFIDTHIH-----APQYAnigsgLGEPLldwletytfpEEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 92 pqRFVDwiiqlikvkrgltPDDMRASAREGIRMCLESGTTavgeivTARTLAPLYRGSrlsGRLFFELVGHDNSRF---- 167
Cdd:cd01303 102 --KFAD-------------PAYAREVYGRFLDELLRNGTT------TACYFATIHPES---TEALFEEAAKRGQRAiagk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 168 -------RELLREAVELSGE----------------SPAGS--FSAGLSPHAPYTLGE--ETFPlireaaagaSLPLAIH 220
Cdd:cd01303 158 vcmdrnaPEYYRDTAESSYRdtkrlierwhgksgrvKPAITprFAPSCSEELLAALGKlaKEHP---------DLHIQTH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 221 CSESTEETNFVfsssgqlAERFypfvgwerylppPRRCSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALC 300
Cdd:cd01303 229 ISENLDEIAWV-------KELF------------PGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 301 PRSNERLDVGRAPVALLRKLGIPLALGTDSLASNdSLSLWDELRFALD---------AFGDELSPADLFRMVTLGGATAL 371
Cdd:cd01303 290 PTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGT-SFSMLDTLRQAYKvsrllgyelGGHAKLSPAEAFYLATLGGAEAL 368
|
410 420
....*....|....*....|
gi 118504519 372 GIQGDHGSLEKGKRADFQIV 391
Cdd:cd01303 369 GLDDKIGNFEVGKEFDAVVI 388
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
26-413 |
1.52e-30 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 122.27 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 26 LAGGALLVRRGRIGDLGTLQRLRrDHPVPIIDHPGCAILPGFINAHtHleltHFPSWRLRSQLEEHPQRFVDWIIQLIKV 105
Cdd:PRK08203 21 IADGGLVVEGGRIVEVGPGGALP-QPADEVFDARGHVVTPGLVNTH-H----HFYQTLTRALPAAQDAELFPWLTTLYPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 106 KRGLTPDDMRASAREGIRMCLESG-TTAV---------------GEIVTARTL---APLYRGS----RLSGRLFFELVGH 162
Cdd:PRK08203 95 WARLTPEMVRVATQTALAELLLSGcTTSSdhhylfpnglrdaldDQIEAAREIgmrFHATRGSmslgESDGGLPPDSVVE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 163 DNSrfrELLREAVELSGESPAGSFSA----GLSPHAPYTLGEEtfpLIREAAAGAS---LPLAIHCSESTEETNFVfsss 235
Cdd:PRK08203 175 DED---AILADSQRLIDRYHDPGPGAmlriALAPCSPFSVSRE---LMRESAALARrlgVRLHTHLAETLDEEAFC---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 236 gqlAERFypfvGwerylppprrCSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVA 315
Cdd:PRK08203 245 ---LERF----G----------MRPVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 316 LLRKLGIPLALGTDSLASNDSLSLWDELRFAL----DAFG-DELSPADLFRMVTLGGATALGiQGDHGSLEKGKRADFQI 390
Cdd:PRK08203 308 ELRAAGVPVGLGVDGSASNDGSNLIGEARQALllqrLRYGpDAMTAREALEWATLGGARVLG-RDDIGSLAPGKLADLAL 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 118504519 391 VGQAGKRESGL--------------VERVMLRG--VVED 413
Cdd:PRK08203 387 FDLDELRFAGAhdpvaalvlcgpprADRVMVGGrwVVRD 425
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
29-391 |
1.94e-30 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 122.03 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 29 GALLVRRGRIGDLGTLQRLRrDHPvPIIDHPGCAILPGFINAHTHLELTHFpswrlRSQLEEhpQRFVDWIIQLI-KVKR 107
Cdd:PRK07228 22 GDVLIEDDRIAAVGDRLDLE-DYD-DHIDATGKVVIPGLIQGHIHLCQTLF-----RGIADD--LELLDWLKDRIwPLEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 108 GLTPDDMRASAREGIRMCLESGTTAVGEIVTARTLAPLYRGSRLSG-RLFFELVGHDNSR-----FRE----LLREAVEL 177
Cdd:PRK07228 93 AHDAESMYYSALLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGiRAVLGKVMMDYGDdvpegLQEdteaSLAESVRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 178 SGE---SPAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVfsssgqLAERFYPFVGWerylpp 254
Cdd:PRK07228 173 LEKwhgADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETV------EEETGMRNIHY------ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 255 prrcstsqlLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASN 334
Cdd:PRK07228 241 ---------LDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPCN 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118504519 335 DSLSLWDELRFA-----LDAFGDELSPA-DLFRMVTLGGATALGIQGDHGSLEKGKRADFQIV 391
Cdd:PRK07228 312 NTLDPFTEMRQAaliqkVDRLGPTAMPArTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAIL 374
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
12-411 |
6.62e-29 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 116.60 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 12 IVAASWLLSPEAPPLAGGALLVRRGRIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHLeltHFPSWRLRSQLEEH 91
Cdd:COG1228 12 ITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 92 PQRFVDwiiqlikvkrgltpdDMRASAREGIRMCLESGTTAVgEIV----------TARTLAPLYRGSR-LSGRLFFELV 160
Cdd:COG1228 89 GITPTV---------------DLVNPADKRLRRALAAGVTTV-RDLpggplglrdaIIAGESKLLPGPRvLAAGPALSLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 161 GHDNSRF----RELLREAVElsgespAG-SFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESteetnfvfsss 235
Cdd:COG1228 153 GGAHARGpeeaRAALRELLA------EGaDYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQA----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 236 gqlaerfypfvgwerylppprrcSTSQLLERAGLLTdstlAIHCVQVSRADAEILRKRGVsVALCP-------------- 301
Cdd:COG1228 216 -----------------------DDIRLAVEAGVDS----IEHGTYLDDEVADLLAEAGT-VVLVPtlslflallegaaa 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 302 ----RSNERLDVGRAPVALLRKLGIPLALGTDSLASNDS-LSLWDELRFALdAFGdeLSPADLFRMVTLGGATALGIQGD 376
Cdd:COG1228 268 pvaaKARKVREAALANARRLHDAGVPVALGTDAGVGVPPgRSLHRELALAV-EAG--LTPEEALRAATINAAKALGLDDD 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 118504519 377 HGSLEKGKRADFQIVgqagkreSG----------LVERVMLRGVV 411
Cdd:COG1228 345 VGSLEPGKLADLVLL-------DGdplediayleDVRAVMKDGRV 382
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
21-391 |
2.80e-25 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 106.94 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 21 PEAPPLAGGALLVRRGRIGDLGTLQRLRRDHPVP-IIDHPGCAILPGFINAHTHlelthFPSWRLR--SQLEEHPQRFVD 97
Cdd:PRK07203 14 PAKPVIEDGAIAIEGNVIVEIGTTDELKAKYPDAeFIDAKGKLIMPGLINSHNH-----IYSGLARgmMANIPPPPDFIS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 98 WIIQL-IKVKRGLTPDDMRASAREGIRMCLESGTTAV-------GEIvtARTLAPLYRGSR---LSGRLFFELVGHDNsr 166
Cdd:PRK07203 89 ILKNLwWRLDRALTLEDVYYSALICSLEAIKNGVTTVfdhhaspNYI--GGSLFTIADAAKkvgLRAMLCYETSDRDG-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 167 fRELLREAVE-------LSGESPAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFSSSGQ-L 238
Cdd:PRK07203 165 -EKELQEGVEenirfikHIDEAKDDMVEAMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGKdI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 239 AERFYPFvgwerylppprrcstsqlleraGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLR 318
Cdd:PRK07203 244 VERLADF----------------------GLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 319 KLGIPLALGTDSLASNdslsLWDELRFALDAFGDELSP-----ADLFRMVTLGGATALG--IQGDHGSLEKGKRADFQIV 391
Cdd:PRK07203 302 KNGILLGLGTDGYTSD----MFESYKVANFKHKHAGGDpnvgwPESPAMLFENNNKIAEryFGAKFGILEEGAKADLIIV 377
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
29-420 |
3.62e-24 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 103.73 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 29 GALLVRRGRIGDLGTLQRLRRDHP--VPIIDHPGCAILPGFINAHTHlelthFP------SW--RLRSQLEEH--P--QR 94
Cdd:PRK09228 32 GLLLVEDGRIVAAGPYAELRAQLPadAEVTDYRGKLILPGFIDTHIH-----YPqtdmiaSYgeQLLDWLNTYtfPeeRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 95 FVDwiiqlikvkrgltPDDMRASAREGIRMCLESGTTavgeivTARTLAPLYRGS---------RLSGRLFFELVGHD-N 164
Cdd:PRK09228 107 FAD-------------PAYAREVAEFFLDELLRNGTT------TALVFGTVHPQSvdalfeaaeARNMRMIAGKVLMDrN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 165 SRfrELLREAVElSG--ESPA--------GSFSAGLSPH-APyTLGEETFplireAAAGA------SLPLAIHCSESTEE 227
Cdd:PRK09228 168 AP--DGLRDTAE-SGydDSKAlierwhgkGRLLYAITPRfAP-TSTPEQL-----EAAGAlarehpDVWIQTHLSENLDE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 228 TNFVfsssgqlAERFypfvgwerylppPRRCSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERL 307
Cdd:PRK09228 239 IAWV-------KELF------------PEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 308 DVGRAPVALLRKLGIPLALGTDSLASNdSLSLwdeLRFALDAF------GDELSPADLFRMVTLGGATALGIQGDHGSLE 381
Cdd:PRK09228 300 GSGLFDLKRADAAGVRVGLGTDVGGGT-SFSM---LQTMNEAYkvqqlqGYRLSPFQAFYLATLGGARALGLDDRIGNLA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 118504519 382 KGKRADFQIVGQAG--------KRESGLVER---VMLRG---VVEDVYVAGER 420
Cdd:PRK09228 376 PGKEADFVVLDPAAtpllalrtARAESLEELlfaLMTLGddrAVAETYVAGRP 428
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
63-370 |
1.41e-23 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 99.01 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 63 ILPGFINAHTHLELTHFPSWRLRSQLEEhpqrfvdwiiqLIKVKRGL--------TPDDMRASAREGIRMCLESGTTAVG 134
Cdd:cd01305 2 LIPALVNAHTHLGDSAIKEVGDGLPLDD-----------LVAPPDGLkhrllaqaDDRELAEAMRKVLRDMRETGIGAFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 135 EIVT--ARTLAPLYRGSRLSGRLFFELVGHDNSrfrellreaVELSGESPAGSFSAGLSphapyTLGEETFPLIREAAAG 212
Cdd:cd01305 71 DFREggVEGIELLRRALGKLPVPFEVILGRPTE---------PDDPEILLEVADGLGLS-----SANDVDLEDILELLRR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 213 ASLPLAIHCSEsteetnfvfsssgqlaerfypfvgwerylppPRRCSTSQLLERAgLLTDSTLAIHCVQVSRADAEILRK 292
Cdd:cd01305 137 RGKLFAIHASE-------------------------------TRESVGMTDIERA-LDLEPDLLVHGTHLTDEDLELVRE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 293 RGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNdSLSLWDELRFALDAFG--DELSPADLFRMVTLGGATA 370
Cdd:cd01305 185 NGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEMEFLAKYSRlqGYLSPLEILRMATVNAAEF 263
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
55-391 |
4.47e-23 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 100.34 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 55 IIDHPGCAILPGFINAHTHLELTHFPSWRLRSQLEehpqrfvDWIIQLIKVKRGLTPDDMRASAREGIRMCLESGTTAV- 133
Cdd:PRK06380 44 IIDATGKVVMPGLINTHAHVGMTASKGLFDDVDLE-------EFLMKTFKYDSKRTREGIYNSAKLGMYEMINSGITAFv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 134 ----GEIVTARTLAPL----YRGSRLSGRLFFELVGHDNSRFRELLREAVELSGESPAgsfsagLSPHAPYTLGEETFPL 205
Cdd:PRK06380 117 dlyySEDIIAKAAEELgiraFLSWAVLDEEITTQKGDPLNNAENFIREHRNEELVTPS------IGVQGIYVANDETYLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 206 IREAAAGASLPLAIHCSESTEEtnfVFSSSGQLAERfyPfVGWerylppprrcstsqlLERAGLLTDSTLAIHCVQVSRA 285
Cdd:PRK06380 191 AKEIAEKYDTIMHMHLSETRKE---VYDHVKRTGER--P-VEH---------------LEKIGFLNSKLIAAHCVWATYH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 286 DAEILRKRGVSVALCPRSNERLDVG-RAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFALDAFGDE------LSPAD 358
Cdd:PRK06380 250 EIKLLSKNGVKVSWNSVSNFKLGTGgSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKFSALSVKNErwdasiIKAQE 329
|
330 340 350
....*....|....*....|....*....|...
gi 118504519 359 LFRMVTLGGATALGIQGdhGSLEKGKRADFQIV 391
Cdd:PRK06380 330 ILDFATINAAKALELNA--GSIEVGKLADLVIL 360
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
67-370 |
8.61e-23 |
|
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: 97.40 E-value: 8.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 67 FINAHTHLELTHFPSWRLRSQLEEhpqrfvdwiiqlikvKRGLTPDDMRASAREGIRMCLESGTTAVGEIVT-------- 138
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKE---------------AEELSPEDLYEDTLRALEALLAGGVTTVVDMGStppptttk 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 139 -----ARTLAPLYRGSRLS-GRLFFELVGHDNSRFRELLREAVELSGESPAGSFSAGLSPHAPYTLGEETFPLIREAAAg 212
Cdd:cd01292 66 aaieaVAEAARASAGIRVVlGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLEEARK- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 213 ASLPLAIHCSESTEETnfvfsssgqlaerfypfvgwerylppprrcSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRK 292
Cdd:cd01292 145 LGLPVVIHAGELPDPT------------------------------RALEDLVALLRLGGRVVIGHVSHLDPELLELLKE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 293 RGVSVALCPRSNERLDV---GRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFALDAFGDELSPADLFRMVTLGGAT 369
Cdd:cd01292 195 AGVSLEVCPLSNYLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
.
gi 118504519 370 A 370
Cdd:cd01292 275 A 275
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
31-391 |
1.05e-21 |
|
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: 95.79 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 31 LLVRRGRIGDLGTLQRLRRDHP--VPIIDHPGCAILPGFINAHTHL----ELTHFPSWRL--RSQLEEHPQRfvDWIIQL 102
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPaaAEEIDAGGRAVTPGLVDCHTHLvfagDRVDEFAARLagASYEEILAAG--GGILST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 103 IKVKRGLTPDDMRASAREGIRMCLESGTTAVgEIVTArtlaplYrgsrlsgrlffelvGHDNSRFRELLREAVELSGESP 182
Cdd:cd01296 79 VRATRAASEDELFASALRRLARMLRHGTTTV-EVKSG------Y--------------GLDLETELKMLRVIRRLKEEGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 183 AGSFSAGLSPHAP---YTLGEETFPLIREA--AAGASLPLAIHCSESTEETNFVFSSSGQLAERfypfvGWERYLPPprR 257
Cdd:cd01296 138 VDLVSTFLGAHAVppeYKGREEYIDLVIEEvlPAVAEENLADFCDVFCEKGAFSLEQSRRILEA-----AKEAGLPV--K 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 258 CSTSQL-----LERAGLLtDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDS-- 330
Cdd:cd01296 211 IHADELsniggAELAAEL-GALSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFnp 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118504519 331 LASNDSLSLwdeLRFALDAFGDELSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQIV 391
Cdd:cd01296 290 GSSPTSSMP---LVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVIL 347
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
19-401 |
1.93e-21 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 95.90 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 19 LSPEAPPLAGGALLVRRGRIGDLGTLQRLRRDhpvPIIDHPGCAILPGFINAHTHL---ELTHFPS---WRLRSQLEEHP 92
Cdd:PRK12393 16 LPGDAARLGGPDIRIRDGRIAAIGALTPLPGE---RVIDATDCVVYPGWVNTHHHLfqsLLKGVPAginQSLTAWLAAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 93 QRFVdwiiqlikvkRGLTPDDMRASAREGIRMCLESGTTAV---------------GEIV--TARTLA---PLYRGSRLS 152
Cdd:PRK12393 93 YRFR----------ARFDEDLFRLAARIGLVELLRSGCTTVadhhylyhpgmpfdtGDILfdEAEALGmrfVLCRGGATQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 153 GRLF------------FELVGHDNSRFRELLREAvelsgeSPAGSFSAGLSPHAP-YTLGEETFPLIREAAAGASLPLAI 219
Cdd:PRK12393 163 TRGDhpglptalrpetLDQMLADVERLVSRYHDA------SPDSLRRVVVAPTTPtFSLPPELLREVARAARGMGLRLHS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 220 HCSESTEETNFVFSSSGQLAERFYPFVGWerylppprrcstsqlleraglLTDSTLAIHCVQVSRADAEILRKRGVSVAL 299
Cdd:PRK12393 237 HLSETVDYVDFCREKYGMTPVQFVAEHDW---------------------LGPDVWFAHLVKLDAEEIALLAQTGTGIAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 300 CPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNDSLSLWDELRFA-----LDAFGDELSPADLFRMVTLGGATALGIQ 374
Cdd:PRK12393 296 CPQSNGRLGSGIAPALAMEAAGVPVSLGVDGAASNESADMLSEAHAAwllhrAEGGADATTVEDVVHWGTAGGARVLGLD 375
|
410 420
....*....|....*....|....*..
gi 118504519 375 GDhGSLEKGKRADFQIVGQAGKRESGL 401
Cdd:PRK12393 376 AI-GTLAVGQAADLAIYDLDDPRFFGL 401
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
55-400 |
3.01e-19 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 88.56 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 55 IIDHPGCAIlPGFINAHTHLElthfpswrlrsqleehpqrfvDWII----------QLIKVKRGL--------TPDDMRA 116
Cdd:PRK07213 41 VIDAKGLVI-PPLINAHTHIG---------------------DSSIkdigigksldELVKPPNGLkhkflnscSDKELVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 117 SAREGIRMCLESGTTAVGEivtartlaplYRGSRLSG-RLFFE----------LVGHDNSRFRELLREAVELSGESPAGs 185
Cdd:PRK07213 99 GMKEGLYDMYNNGIKAFCD----------FREGGIKGiNLLKKassdlpikpiILGRPTEADENELKKEIREILKNSDG- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 186 fsAGLSPHAPYTlgEETFPLIREAAAGASLPLAIHCSESTEETNFVFSSSGQlaerfypfvgwerylppprrcSTSQLLE 265
Cdd:PRK07213 168 --IGLSGANEYS--DEELKFICKECKREKKIFSIHAAEHKGSVEYSLEKYGM---------------------TEIERLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 266 RAGLLTDstLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLALGTDSLASNdSLSLWDELRF 345
Cdd:PRK07213 223 NLGFKPD--FIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNFMAN-SPSIFREMEF 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 118504519 346 ALDAFgdELSPADLFRMVTLGGATALGIQgDHGSLEKGKRADFQIVGQAGKRESG 400
Cdd:PRK07213 300 IYKLY--HIEPKEILKMATINGAKILGLI-NVGLIEEGFKADFTFIKPTNIKFSK 351
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
42-419 |
6.20e-19 |
|
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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 88.28 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 42 GTLQRLRRDHPVPIIDHPGCAILPGFINAHTHLELTHFpswRLRSQLEEHPQ-RFVDWIIQLIKVKRGLTPDDMRASARE 120
Cdd:cd01313 19 GRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAM---AGLTEYRGSAAdSFWTWRELMYRFAARLTPEQIEAIARQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 121 GIRMCLESGTTAVGE----------------------IVTAR-------TLAP-LYRGSRLSGRLFFEL---VGHDNSRF 167
Cdd:cd01313 96 LYIEMLLAGITAVGEfhyvhhdpdgtpyadpaelaqrVIAAAsdagigiTLLPvLYARAGFGGPAPNPGqrrFINGYEDF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 168 RELLREAVELSGESPAGSFsaGLSPHapyTLGEETFPLIREAAAGAS--LPLAIHCSESTEETNFVFSSSGQlaerfypf 245
Cdd:cd01313 176 LGLLEKALRAVKEHAAARI--GVAPH---SLRAVPAEQLAALAALASekAPVHIHLAEQPKEVDDCLAAHGR-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 246 vgwerylppprrcSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLRKLGIPLA 325
Cdd:cd01313 243 -------------RPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 326 LGTDslaSNDSLSLWDELRFA-------------LDAFGDeLSPADLFRMVTLGGATALGIqgDHGSLEKGKRADFQIVG 392
Cdd:cd01313 310 IGSD---SNARIDLLEELRQLeysqrlrdrarnvLATAGG-SSARALLDAALAGGAQALGL--ATGALEAGARADLLSLD 383
|
410 420 430
....*....|....*....|....*....|....*
gi 118504519 393 Q-----AGKRESGLVERVMLRG---VVEDVYVAGE 419
Cdd:cd01313 384 LdhpslAGALPDTLLDAWVFAAgdrEVRDVVVGGR 418
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
10-424 |
8.92e-19 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 87.81 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 10 SFIVAASWLLSPEAPPLAGGALLVRRGRIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHLELThfpswRLRSQLE 89
Cdd:PRK15493 4 TYVNATIVTMNEQNEVIENGYIIVENDQIIDVNSGEFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMS-----LLRGIGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 90 EhpQRFVDWI-IQLIKVKRGLTPDDMRASAREGIRMCLESGTTAVGEI-----VTARTLAPLYRGSRLSG---RLFFELV 160
Cdd:PRK15493 79 D--MLLQPWLeTRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMfnpigVDQDAIMETVSRSGMRAavsRTLFSFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 161 GHDNSRfrELLREAVELSGE--SPAGSFSAGLSPHAPYTLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFSSSGQL 238
Cdd:PRK15493 157 TKEDEK--KAIEEAEKYVKRyyNESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 239 AERFypfvgwerylppprrcstsqlLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLR 318
Cdd:PRK15493 235 PVEY---------------------AASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAML 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 319 KLGIPLALGTDSLASNDSLSLWDELRFAL--------DAFGDELSPAdlFRMVTLGGATALGIQgDHGSLEKGKRADFQI 390
Cdd:PRK15493 294 EAGIKVGIATDSVASNNNLDMFEEMRIATllqkgihqDATALPVETA--LTLATKGAAEVIGMK-QTGSLEVGKCADFIT 370
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 118504519 391 VGQAGKRESGLVERVMLRGV-------VEDVYVAGER--FDGE 424
Cdd:PRK15493 371 IDPSNKPHLQPADEVLSHLVyaasgkdISDVIINGKRvvWNGE 413
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
37-420 |
2.03e-18 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 86.83 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 37 RIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHL------ELTH--------FPSWRlrsqleEHPQRFVDwiiql 102
Cdd:PRK09229 23 TVDADGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAfqramaGLTEvrgppqdsFWSWR------ELMYRFAL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 103 ikvkrGLTPDDMRASAREG-IRMcLESGTTAVGE----------------------IVTAR-------TLAP-LYRGSRL 151
Cdd:PRK09229 92 -----RLTPDQLEAIARQLyVEM-LEAGYTSVGEfhylhhdpdgtpyadpaemalrIVAAAraagiglTLLPvLYAHSGF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 152 SG-------RLFfelvGHDNSRFRELLREAVELSGESPAGSFsaGLSPHapyTLGEETFPLIREAAAGA--SLPLAIHCS 222
Cdd:PRK09229 166 GGqppnpgqRRF----INDPDGFLRLLEALRRALAALPGARL--GLAPH---SLRAVTPDQLAAVLALAapDGPVHIHIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 223 ESTEETNFVFSSSGQlaerfypfvgwerylppprrcSTSQLLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPR 302
Cdd:PRK09229 237 EQTKEVDDCLAWSGA---------------------RPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 303 SNERLDVGRAPVALLRKLGIPLALGTDslaSNDSLSLWDELRfALD-------------AFGDELSPAD-LFRMVTLGGA 368
Cdd:PRK09229 296 TEANLGDGIFPAVDYLAAGGRFGIGSD---SHVSIDLVEELR-LLEygqrlrdrrrnvlAAAAQPSVGRrLFDAALAGGA 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 369 TALGIqgDHGSLEKGKRADFQIVGQAGKRESGLVERVML--------RGVVEDVYVAGER 420
Cdd:PRK09229 372 QALGR--AIGGLAVGARADLVVLDLDHPALAGREGDALLdrwvfaggDAAVRDVWVAGRW 429
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
29-411 |
8.01e-15 |
|
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: 75.53 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 29 GALLVRRGRIGDLGTLQRLRRDHPVPIIDHPGCAILPGFINAHTHL-----ELTHFpSWRLRSQLEEHPQRFVDWIIQLI 103
Cdd:TIGR01224 4 AVILIHGGKIVWIGQLAALPGEEATEIIDCGGGLVTPGLVDPHTHLvfagdRVNEF-EMKLQGASYLEILAQGGGILSTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 104 KVKRGLTPDDMRASAREGIRMCLESGTTAV-----------GEIVTARTLAPLYRGSRLSGRLFF--------ELVGHDN 164
Cdd:TIGR01224 83 RATRAASEEELLKLALFRLKSMLRSGTTTAevksgygldleTELKMLRAAKALHEEQPVDVVTTFlgahavppEFQGRPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 165 SRFR----ELLREAVELSGESPAGSF--SAGLSPHAPYTlgeetfplIREAAAGASLPLAIHcsesteetnfvfsssgql 238
Cdd:TIGR01224 163 DYVDgiceELIPQVAEEGLASFADVFceAGVFSVEQSRR--------ILQAAQEAGLPVKLH------------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 239 AERFYPFVGwerylppprrcstSQLLERAGLLTdstlAIHCVQVSRADAEILRKRGVSVALCPRSNERLDVGRAPVALLR 318
Cdd:TIGR01224 217 AEELSNLGG-------------AELAAKLGAVS----ADHLEHASDAGIKALAEAGTVAVLLPGTTFYLRETYPPARQLI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 319 KLGIPLALGTDslaSNDSLSLWDELRFALD--AFGDELSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQIVGQAGK 396
Cdd:TIGR01224 280 DYGVPVALATD---LNPGSSPTLSMQLIMSlaCRLMKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSY 356
|
410 420
....*....|....*....|.
gi 118504519 397 RE------SGLVERVMLRGVV 411
Cdd:TIGR01224 357 AEipyhygVNHVHAVIKNGNI 377
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
19-418 |
1.32e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 75.42 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 19 LSPEAPPLAGGALLVRRGRIGDLGtlQRLRRDHpVPIIDHPGCAILPGFINAHTHLelthfpsWR--LRSqleehpqRFV 96
Cdd:PRK08204 14 MDPAIGDLPRGDILIEGDRIAAVA--PSIEAPD-AEVVDARGMIVMPGLVDTHRHT-------WQsvLRG-------IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 97 DWIIQ--LIKVKRGL----TPDDMRASAREGIRMCLESGTTAVGEIvTARTLAPLY-----RGSRLSG------------ 153
Cdd:PRK08204 77 DWTLQtyFREIHGNLgpmfRPEDVYIANLLGALEALDAGVTTLLDW-SHINNSPEHadaaiRGLAEAGiravfahgspgp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 154 --RLFFELVGHDNSRFRELLREAVElsgeSPAGSFSAGLSPHAPYTLGEET----FPLIREAAagasLPLAIHcsestee 227
Cdd:PRK08204 156 spYWPFDSVPHPREDIRRVKKRYFS----SDDGLLTLGLAIRGPEFSSWEVaradFRLARELG----LPISMH------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 228 tnfvfSSSGQLAERFYpfvGWERylppprrcstsqlLERAGLLTDSTLAIHCVQVSRADAEILRKRGVSVALCPRSNERL 307
Cdd:PRK08204 221 -----QGFGPWGATPR---GVEQ-------------LHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 308 DVGRAPVALLRKLGIPLALGTDSLASnDSLSLWDELRFALDA----FGDE-------------LSPADLFRMVTLGGATA 370
Cdd:PRK08204 280 GHGYPVTGRLLAHGVRPSLGVDVVTS-TGGDMFTQMRFALQAerarDNAVhlreggmppprltLTARQVLEWATIEGARA 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118504519 371 LGIQGDHGSLEKGKRADF------------------QIVGQAGkresglvervmlRGVVEDVYVAG 418
Cdd:PRK08204 359 LGLEDRIGSLTPGKQADLvlidatdlnlapvhdpvgAVVQSAH------------PGNVDSVMVAG 412
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
205-428 |
3.57e-12 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 67.76 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 205 LIREAAAGASL--PLAIHCSESTEETNFVfsssgqlaERFYpfvgwerylppprRCSTSQLLERAGLLTDSTLAIHCVQV 282
Cdd:PRK06151 223 LRRTAAAARELgcPVRLHCAQGVLEVETV--------RRLH-------------GTTPLEWLADVGLLGPRLLIPHATYI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 283 SR---------ADAEILRKRGVSVALCPrsnerLDVGRAPVAL-----LRKLGIPLALGTDSlASNDSLSlwdELRFAL- 347
Cdd:PRK06151 282 SGsprlnysggDDLALLAEHGVSIVHCP-----LVSARHGSALnsfdrYREAGINLALGTDT-FPPDMVM---NMRVGLi 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 348 -----DAFGDELSPADLFRMVTLGGATALGiQGDHGSLEKGKRADFQIVGQAGKRESGLVERV---MLRGV---VEDVYV 416
Cdd:PRK06151 353 lgrvvEGDLDAASAADLFDAATLGGARALG-RDDLGRLAPGAKADIVVFDLDGLHMGPVFDPIrtlVTGGSgrdVRAVFV 431
|
250
....*....|..
gi 118504519 417 AGERFDGERTSP 428
Cdd:PRK06151 432 DGRVVMEDGRLP 443
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
31-388 |
1.52e-11 |
|
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: 65.73 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 31 LLVRRGRIGDLGTlqRLRRDHPVPIIDHPGCAILPGFINAHTHLELTHF-PSWRLRS---QLEEhpqrfvdwIIQLIKVK 106
Cdd:cd01293 17 IAIEDGRIAAIGP--ALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTgGRWPNNSggtLLEA--------IIAWEERK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 107 RGLTPDDMRASAREGIRMCLESGTTA------VGEIVTARTLAPLYR-GSRLSGRLFFELVG---HD---NSRFRELLRE 173
Cdd:cd01293 87 LLLTAEDVKERAERALELAIAHGTTAirthvdVDPAAGLKALEALLElREEWADLIDLQIVAfpqHGllsTPGGEELMRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 174 AVELSGEspagsfSAGLSPHAPY-TLGEETFPLIREAAAGASLPLAIHCSESTEETNFVFsssGQLAERfypfvgweryl 252
Cdd:cd01293 167 ALKMGAD------VVGGIPPAEIdEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTL---EELAEE----------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 253 ppprrcstsqlLERAGLLTDSTLAiHCV--------QVSRAdAEILRKRGVSVALCPRSNERLDV---------GRAPVA 315
Cdd:cd01293 227 -----------AERRGMQGRVTCS-HATalgslpeaEVSRL-ADLLAEAGISVVSLPPINLYLQGredttpkrrGVTPVK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 316 LLRKLGIPLALGTDS-------LASNDSLSLwdeLRFALDAFG----DELspADLFRMVTLGGATALGIQgDHGsLEKGK 384
Cdd:cd01293 294 ELRAAGVNVALGSDNvrdpwypFGSGDMLEV---ANLAAHIAQlgtpEDL--ALALDLITGNAARALGLE-DYG-IKVGC 366
|
....
gi 118504519 385 RADF 388
Cdd:cd01293 367 PADL 370
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
30-393 |
6.98e-11 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 64.05 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 30 ALLVRRGRIGDLGTLQRLR--RDHPVPIIDHPGCAILPGFINAHTHL----------ELTHFPSW-----RLRSQLEEHP 92
Cdd:COG1574 29 AVAVRDGRIVAVGSDAEVRalAGPATEVIDLGGKTVLPGFIDAHVHLlggglallgvDLSGARSLdellaRLRAAAAELP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 93 QRfvDWII------QLIKVKRGLT-------------------------------------------------------- 110
Cdd:COG1574 109 PG--EWILgrgwdeSLWPEGRFPTradldavspdrpvvltrvdghaawvnsaalelagitadtpdpeggeierdadgept 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 111 -------------------PDDMRASAREGIRMCLESGTTAVGEIVTARTLAPLYRGSRLSGRLFFELVG---HDNSRFR 168
Cdd:COG1574 187 gvlreaamdlvraaippptPEELRAALRAALRELASLGITSVHDAGLGPDDLAAYRELAAAGELPLRVVLylgADDEDLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 169 ELLREAVELSGESP--------------AGSFSAGLSphAPY-----TLGEETFP------LIREAAAgASLPLAIHC-- 221
Cdd:COG1574 267 ELLALGLRTGYGDDrlrvggvklfadgsLGSRTAALL--EPYaddpgNRGLLLLDpeelreLVRAADA-AGLQVAVHAig 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 222 SESTEETnfvfsssgqLAerfypfvGWERYL---PPPRRcstsqlleRAGLltdstlaIHCVQVSRADAEILRKRGVSVA 298
Cdd:COG1574 344 DAAVDEV---------LD-------AYEAARaanGRRDR--------RHRI-------EHAQLVDPDDLARFAELGVIAS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 299 LCPR--------SNERLDVGRA----PVALLRKLGIPLALGTDslASNDSLSLWDELRFAL-------DAFGDE--LSPA 357
Cdd:COG1574 393 MQPThatsdgdwAEDRLGPERAarayPFRSLLDAGAPLAFGSD--APVEPLDPLLGIYAAVtrrtpsgRGLGPEerLTVE 470
|
490 500 510
....*....|....*....|....*....|....*.
gi 118504519 358 DLFRMVTLGGATALGIQGDHGSLEKGKRADFQIVGQ 393
Cdd:COG1574 471 EALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR 506
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
278-391 |
2.78e-09 |
|
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: 58.46 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 278 HCVQVSRADAEILRKRGVsvALCP-----------------------RSNERLDVGRAPVALLRKLGIPLALGTDSLASN 334
Cdd:cd01299 199 HGFLIDDETIELMKEKGI--FLVPtlatyealaaegaapglpadsaeKVALVLEAGRDALRRAHKAGVKIAFGTDAGFPV 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 118504519 335 DSL-SLWDELRFALDAFGdelSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQIV 391
Cdd:cd01299 277 PPHgWNARELELLVKAGG---TPAEALRAATANAAELLGLSDELGVIEAGKLADLLVV 331
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
109-390 |
1.65e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 56.39 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 109 LTPDDMRASAREGIRMCLESGTTAV---GEIVTAR-TLAPLYRGSR----LSGRLFFELVGHDNSRfRELLREAVELSGE 180
Cdd:pfam07969 144 LAREAEAAAVAAALAALPGFGITSVdggGGNVHSLdDYEPLRELTAaeklKELLDAPERLGLPHSI-YELRIGAMKLFAD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 181 SPAGSFSAGLSP--HAPYTLGEETFPLIR-----EAAAGASLPLAIHCSESTEETNFVfsssGQLAErfypfVGWERYLP 253
Cdd:pfam07969 223 GVLGSRTAALTEpyFDAPGTGWPDFEDEAlaelvAAARERGLDVAIHAIGDATIDTAL----DAFEA-----VAEKLGNQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 254 PPRRCSTSQLLeraGLLTDStlaihcvQVSRadaeiLRKRGVSVALCPRSN--------ERLDVGRA----PVALLRKLG 321
Cdd:pfam07969 294 GRVRIEHAQGV---VPYTYS-------QIER-----VAALGGAAGVQPVFDplwgdwlqDRLGAERArgltPVKELLNAG 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118504519 322 IPLALGTDSLASN--------DSLSLWDELRFALDAFGDELSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQI 390
Cdd:pfam07969 359 VKVALGSDAPVGPfdpwprigAAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVV 435
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
88-388 |
6.19e-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: 51.54 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 88 LEEHPQRFVdwiiqlIKVKRGLTPDDMRASAREGIRMCLESGTTAVGEI-VTARTLAPLYRGSRLSGRLFFELVG----H 162
Cdd:cd01300 161 LVEAAAALV------LEAVPPPTPEERRAALRAAARELASLGVTTVHDAgGGAADDIEAYRRLAAAGELTLRVRValyvS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 163 DNSRFRELLREAVELSGESP--------------AGSFSAGLSphAPY-----TLGEETFP------LIREAAAgASLPL 217
Cdd:cd01300 235 PLAEDLLEELGARKNGAGDDrlrlggvklfadgsLGSRTAALS--EPYldspgTGGLLLISpeeleeLVRAADE-AGLQV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 218 AIHC--SESTEETNFVFSSsgqlAERFYPFVGwerylPPPRrcstsqlLERAGLLTDSTLA-------IHCVQVSRA--D 286
Cdd:cd01300 312 AIHAigDRAVDTVLDALEA----ALKDNPRAD-----HRHR-------IEHAQLVSPDDIPrfaklgvIASVQPNHLysD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 287 AEILRKRGVSVALCPRSNerldvgraPVALLRKLGIPLALGTDSLASndSLSLWDELRFALD---------AFGDE-LSP 356
Cdd:cd01300 376 GDAAEDRRLGEERAKRSY--------PFRSLLDAGVPVALGSDAPVA--PPDPLLGIWAAVTrktpgggvlGNPEErLSL 445
|
330 340 350
....*....|....*....|....*....|..
gi 118504519 357 ADLFRMVTLGGATALGIQGDHGSLEKGKRADF 388
Cdd:cd01300 446 EEALRAYTIGAAYAIGEEDEKGSLEPGKLADF 477
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
337-410 |
6.56e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.79 E-value: 6.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118504519 337 LSLWDELRFALDAFGdeLSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQIVGQAGKresglVERVMLRGV 410
Cdd:COG1820 307 LTMDDAVRNLVEWTG--LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLN-----VRATWVGGE 373
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-133 |
4.01e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.69 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 26 LAGGA---LLVRRGRIGDLGtlQRLRRDHPVPIIDHPGCAILPGFINAHTHLELTHFPS-WrlrsqleeHPQRFVDWIIQ 101
Cdd:PRK05985 11 PAGGAavdILIRDGRIAAIG--PALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpW--------YPNEPGPSLRE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 118504519 102 LIKVKRGLTPD---DMRASAREGIRMCLESGTTAV 133
Cdd:PRK05985 81 RIANERRRRAAsghPAAERALALARAAAAAGTTAM 115
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
326-409 |
6.62e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 44.88 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 326 LGTDSLASNDsLSLWDELRFALDAFGdeLSPADLFRMVTLGGATALGIQGDHGSLEKGKRADFQIVGqagkrESGLVERV 405
Cdd:cd00854 299 LADGTLAGST-LTMDQAVRNMVKWGG--CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD-----DDLNVKAT 370
|
....
gi 118504519 406 MLRG 409
Cdd:cd00854 371 WING 374
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
287-390 |
1.24e-04 |
|
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: 43.84 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118504519 287 AEILRKRGVSVALCP------RSNERLDVGRAPVALLRKLGIPLALGTDSLASNdSLSLWDELRFALdAFGdeLSPADLF 360
Cdd:cd01309 231 ADELAKHGIPVIYGPtltlpkKVEEVNDAIDTNAYLLKKGGVAFAISSDHPVLN-IRNLNLEAAKAV-KYG--LSYEEAL 306
|
90 100 110
....*....|....*....|....*....|
gi 118504519 361 RMVTLGGATALGIQGDHGSLEKGKRADFQI 390
Cdd:cd01309 307 KAITINPAKILGIEDRVGSLEPGKDADLVV 336
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
28-73 |
1.29e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 40.64 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 118504519 28 GGALLVRRGRIGDLGTLQRLRRDHPvpIIDHPGCAILPGFINAHTH 73
Cdd:cd00854 16 DGAVLVEDGKIVAIGPEDELEEADE--IIDLKGQYLVPGFIDIHIH 59
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
26-73 |
1.66e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.47 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 118504519 26 LAGGALLVRRGRIGDLGTlqrlRRDHPVPIIDHPGCAILPGFINAHTH 73
Cdd:COG1820 14 LEDGALLIEDGRIAAIGP----GAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
31-76 |
1.84e-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: 40.28 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 118504519 31 LLVRRGRIGDLGtlQRLRRDHPVPIIDHPGCAILPGFINAHTHLEL 76
Cdd:cd01314 19 ILIEDGKIVAIG--PNLEAPGGVEVIDATGKYVLPGGIDPHTHLEL 62
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
31-76 |
3.78e-03 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 39.29 E-value: 3.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 118504519 31 LLVRRGRIGDLGTLqrLRRDHPVPIIDHPGCAILPGFINAHTHLEL 76
Cdd:TIGR02033 19 VLIEGGKIVAVGDN--LIPPDAVEVIDATGKYVLPGGIDVHTHLEM 62
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
31-76 |
3.84e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 39.38 E-value: 3.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 118504519 31 LLVRRGRIGDLGtlqrlrRDHPVPIIDHPGCAILPGFINAHTHLEL 76
Cdd:PRK08323 21 VLIEDGKIAAIG------ANLGDEVIDATGKYVMPGGIDPHTHMEM 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
360-420 |
9.41e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 37.85 E-value: 9.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118504519 360 FRMVTLGGATALGIQgDHGSLEKGKRADFQIVGQAGkresGLVervmlrgVVEDVYVAGER 420
Cdd:PRK15446 330 VALVTANPARAAGLD-DRGEIAPGKRADLVRVRRAG----GLP-------VVRAVWRGGRR 378
|
|
| |
