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Conserved domains on  [gi|1760014703|gb|KAB2970031|]
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MAG: amidohydrolase family protein [Thermoanaerobaculia bacterium]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 86-513 9.73e-69

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 226.00  E-value: 9.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  86 APPGATIVAFVHADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVKLPARAVRIDATGRYLLPAFADMHVHLLGEAWN-- 163
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRav 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 164 --VMLQPEAQKTSKDIPFDEFLFPFIANGVTLVQSMSATPEELvvRERIRRGE---LLGPRLILA-PMIDGpkkawppPL 237
Cdd:COG1228    83 efEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPLGL--RDAIIAGEsklLPGPRVLAAgPALSL-------TG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 238 STWVESAAEAHDAVHKAKHDGYDKIKVYS-----FLSRESYDSIISAAGDVQMDVIGHIPMSVSLDYVLDSGQKLIAHSE 312
Cdd:COG1228   154 GAHARGPEEARAALRELLAEGADYIKVFAeggapDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDSIEHGT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 313 EVakhaggdhSAEHIHELAgkmtASG-VWMTPTLvttrsilgvfadpdgllerpeavyfqhpmqqgvwsFITDNLYRPIP 391
Cdd:COG1228   234 YL--------DDEVADLLA----EAGtVVLVPTL-----------------------------------SLFLALLEGAA 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 392 AKAREQLRSDFESFQKPLtKAFHDGGGKLMTGTDTLFpGLVPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESER 471
Cdd:COG1228   267 APVAAKARKVREAALANA-RRLHDAGVPVALGTDAGV-GVPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDD 344

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1760014703 472 AGTIATGKETDLVLLDANPLEDVSAASKIAGVFVRGRWIARE 513
Cdd:COG1228   345 VGSLEPGKLADLVLLDGDPLEDIAYLEDVRAVMKDGRVVDRS 386
 
Name Accession Description Interval E-value
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 86-513 9.73e-69

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 226.00  E-value: 9.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  86 APPGATIVAFVHADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVKLPARAVRIDATGRYLLPAFADMHVHLLGEAWN-- 163
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRav 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 164 --VMLQPEAQKTSKDIPFDEFLFPFIANGVTLVQSMSATPEELvvRERIRRGE---LLGPRLILA-PMIDGpkkawppPL 237
Cdd:COG1228    83 efEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPLGL--RDAIIAGEsklLPGPRVLAAgPALSL-------TG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 238 STWVESAAEAHDAVHKAKHDGYDKIKVYS-----FLSRESYDSIISAAGDVQMDVIGHIPMSVSLDYVLDSGQKLIAHSE 312
Cdd:COG1228   154 GAHARGPEEARAALRELLAEGADYIKVFAeggapDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDSIEHGT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 313 EVakhaggdhSAEHIHELAgkmtASG-VWMTPTLvttrsilgvfadpdgllerpeavyfqhpmqqgvwsFITDNLYRPIP 391
Cdd:COG1228   234 YL--------DDEVADLLA----EAGtVVLVPTL-----------------------------------SLFLALLEGAA 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 392 AKAREQLRSDFESFQKPLtKAFHDGGGKLMTGTDTLFpGLVPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESER 471
Cdd:COG1228   267 APVAAKARKVREAALANA-RRLHDAGVPVALGTDAGV-GVPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDD 344

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1760014703 472 AGTIATGKETDLVLLDANPLEDVSAASKIAGVFVRGRWIARE 513
Cdd:COG1228   345 VGSLEPGKLADLVLLDGDPLEDIAYLEDVRAVMKDGRVVDRS 386
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 136-496 6.00e-35

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: 133.96  E-value: 6.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 136 AVRIDATGRYLLPAFADMHVHLLGEAWnvmlqPEAQKTSKDIPFDEFLFPFIAN-----GVTLVQSMsATPEELVVRERI 210
Cdd:cd01299     1 AQVIDLGGKTLMPGLIDAHTHLGSDPG-----DLPLDLALPVEYRTIRATRQARaalraGFTTVRDA-GGADYGLLRDAI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 211 RRGELLGPRLILA-----------PMIDGPKKAWPPPLSTWVESAAEAHDAVHKAKHDGYDKIKVY-------------- 265
Cdd:cd01299    75 DAGLIPGPRVFASgralsqtgghgDPRGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRGADQIKIMatggvlspgdpppd 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 266 SFLSRESYDSIISAAGDVQMDVIGHipmsvsldyvldsgqkliAHSEEVAKHA--GGDHSAEHIH----ELAGKMTASGV 339
Cdd:cd01299   155 TQFSEEELRAIVDEAHKAGLYVAAH------------------AYGAEAIRRAirAGVDTIEHGFliddETIELMKEKGI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 340 WMTPTLVTTRSILGVFADPdGLLERPEAvyfqhpmqqgvwsfitdnlyrpipaKAREQLRSDFESFQKpltkaFHDGGGK 419
Cdd:cd01299   217 FLVPTLATYEALAAEGAAP-GLPADSAE-------------------------KVALVLEAGRDALRR-----AHKAGVK 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 420 LMTGTDTLFPGlVPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEDVSA 496
Cdd:cd01299   266 IAFGTDAGFPV-PPHGWNARELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAV 341
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 145-510 1.46e-15

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: 77.93  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 145 YLLPAFADMHVHL-LGEAWNVMLQPEAQKTSKDIpfdeFLFPFIANGVTLVQSMSATPEELVvrERIRR---GELLGPRL 220
Cdd:pfam01979   1 IVLPGLIDAHVHLeMGLLRGIPVPPEFAYEALRL----GITTMLKSGTTTVLDMGATTSTGI--EALLEaaeELPLGLRF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 221 ILAPMIDGPKKAWPPPLSTWVESAAEAHdaVHKAKHDGYDKIKVYSFLSRESYDSIISAAGDVQMDVigHIPMSVSLdyv 300
Cdd:pfam01979  75 LGPGCSLDTDGELEGRKALREKLKAGAE--FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKY--GLPVAIHA--- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 301 ldSGQKLIahsEEVAKHAGGDhSAEHIHELAGKMTAsgvwMTPTLVTTRSILGVFADPDGLLERPEAVyfqhpmqqgvws 380
Cdd:pfam01979 148 --LETKGE---VEDAIAAFGG-GIEHGTHLEVAESG----GLLDIIKLILAHGVHLSPTEANLLAEHL------------ 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 381 fitDNLYRPIPAKAREQLRSDFEsfqkPLTKAFHDGGgKLMTGTDTLFPG----LVPGFALHRELEELVDVGLTPFEALR 456
Cdd:pfam01979 206 ---KGAGVAHCPFSNSKLRSGRI----ALRKALEDGV-KVGLGTDGAGSGnslnMLEELRLALELQFDPEGGLSPLEALR 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 457 TTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEDVSAASK---IAGVFVRGRWI 510
Cdd:pfam01979 278 MATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPdgnVKKVIVKGKIV 334
PRK05985 PRK05985
cytosine deaminase; Provisional
 99-162 2.33e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 53.01  E-value: 2.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1760014703  99 DVIPMDRERvlrdHTVVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL----LGEAW 162
Cdd:PRK05985    8 NVRPAGGAA----VDILIRDGRIAAIGPALAA--PPGAEVEDGGGALALPGLVDGHIHLdktfWGDPW 69
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 111-157 2.66e-04

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: 43.59  E-value: 2.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1760014703 111 DHTVVIAGGRIAEVGpasAVKLPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:TIGR00857   5 EVDILVEGGRIKKIG---KLRIPPDAEVIDAKGLLVLPGFIDLHVHL 48
 
Name Accession Description Interval E-value
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 86-513 9.73e-69

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 226.00  E-value: 9.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  86 APPGATIVAFVHADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVKLPARAVRIDATGRYLLPAFADMHVHLLGEAWN-- 163
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRav 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 164 --VMLQPEAQKTSKDIPFDEFLFPFIANGVTLVQSMSATPEELvvRERIRRGE---LLGPRLILA-PMIDGpkkawppPL 237
Cdd:COG1228    83 efEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPLGL--RDAIIAGEsklLPGPRVLAAgPALSL-------TG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 238 STWVESAAEAHDAVHKAKHDGYDKIKVYS-----FLSRESYDSIISAAGDVQMDVIGHIPMSVSLDYVLDSGQKLIAHSE 312
Cdd:COG1228   154 GAHARGPEEARAALRELLAEGADYIKVFAeggapDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDSIEHGT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 313 EVakhaggdhSAEHIHELAgkmtASG-VWMTPTLvttrsilgvfadpdgllerpeavyfqhpmqqgvwsFITDNLYRPIP 391
Cdd:COG1228   234 YL--------DDEVADLLA----EAGtVVLVPTL-----------------------------------SLFLALLEGAA 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 392 AKAREQLRSDFESFQKPLtKAFHDGGGKLMTGTDTLFpGLVPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESER 471
Cdd:COG1228   267 APVAAKARKVREAALANA-RRLHDAGVPVALGTDAGV-GVPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDD 344

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1760014703 472 AGTIATGKETDLVLLDANPLEDVSAASKIAGVFVRGRWIARE 513
Cdd:COG1228   345 VGSLEPGKLADLVLLDGDPLEDIAYLEDVRAVMKDGRVVDRS 386
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 136-496 6.00e-35

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: 133.96  E-value: 6.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 136 AVRIDATGRYLLPAFADMHVHLLGEAWnvmlqPEAQKTSKDIPFDEFLFPFIAN-----GVTLVQSMsATPEELVVRERI 210
Cdd:cd01299     1 AQVIDLGGKTLMPGLIDAHTHLGSDPG-----DLPLDLALPVEYRTIRATRQARaalraGFTTVRDA-GGADYGLLRDAI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 211 RRGELLGPRLILA-----------PMIDGPKKAWPPPLSTWVESAAEAHDAVHKAKHDGYDKIKVY-------------- 265
Cdd:cd01299    75 DAGLIPGPRVFASgralsqtgghgDPRGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRGADQIKIMatggvlspgdpppd 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 266 SFLSRESYDSIISAAGDVQMDVIGHipmsvsldyvldsgqkliAHSEEVAKHA--GGDHSAEHIH----ELAGKMTASGV 339
Cdd:cd01299   155 TQFSEEELRAIVDEAHKAGLYVAAH------------------AYGAEAIRRAirAGVDTIEHGFliddETIELMKEKGI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 340 WMTPTLVTTRSILGVFADPdGLLERPEAvyfqhpmqqgvwsfitdnlyrpipaKAREQLRSDFESFQKpltkaFHDGGGK 419
Cdd:cd01299   217 FLVPTLATYEALAAEGAAP-GLPADSAE-------------------------KVALVLEAGRDALRR-----AHKAGVK 265

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 420 LMTGTDTLFPGlVPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEDVSA 496
Cdd:cd01299   266 IAFGTDAGFPV-PPHGWNARELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIAV 341
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 145-510 1.46e-15

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: 77.93  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 145 YLLPAFADMHVHL-LGEAWNVMLQPEAQKTSKDIpfdeFLFPFIANGVTLVQSMSATPEELVvrERIRR---GELLGPRL 220
Cdd:pfam01979   1 IVLPGLIDAHVHLeMGLLRGIPVPPEFAYEALRL----GITTMLKSGTTTVLDMGATTSTGI--EALLEaaeELPLGLRF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 221 ILAPMIDGPKKAWPPPLSTWVESAAEAHdaVHKAKHDGYDKIKVYSFLSRESYDSIISAAGDVQMDVigHIPMSVSLdyv 300
Cdd:pfam01979  75 LGPGCSLDTDGELEGRKALREKLKAGAE--FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKY--GLPVAIHA--- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 301 ldSGQKLIahsEEVAKHAGGDhSAEHIHELAGKMTAsgvwMTPTLVTTRSILGVFADPDGLLERPEAVyfqhpmqqgvws 380
Cdd:pfam01979 148 --LETKGE---VEDAIAAFGG-GIEHGTHLEVAESG----GLLDIIKLILAHGVHLSPTEANLLAEHL------------ 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 381 fitDNLYRPIPAKAREQLRSDFEsfqkPLTKAFHDGGgKLMTGTDTLFPG----LVPGFALHRELEELVDVGLTPFEALR 456
Cdd:pfam01979 206 ---KGAGVAHCPFSNSKLRSGRI----ALRKALEDGV-KVGLGTDGAGSGnslnMLEELRLALELQFDPEGGLSPLEALR 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 457 TTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEDVSAASK---IAGVFVRGRWI 510
Cdd:pfam01979 278 MATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPdgnVKKVIVKGKIV 334
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 97-513 4.66e-14

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 74.09  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  97 HADVIPMDRE-RVLRDHTVVIAGGRIAEVGPASAVKLPARAVR-IDATGRYLLPAFADMHVHllgeAWNVMLQPEAQkts 174
Cdd:COG0402     6 GAWVLTMDPAgGVLEDGAVLVEDGRIAAVGPGAELPARYPAAEvIDAGGKLVLPGLVNTHTH----LPQTLLRGLAD--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 175 kDIPFDEFL----FPF--------------------IANGVTLVQSMSATPEELVvrERIRRG-ELLGPRLILAP-MIDG 228
Cdd:COG0402    79 -DLPLLDWLeeyiWPLearldpedvyagallalaemLRSGTTTVADFYYVHPESA--DALAEAaAEAGIRAVLGRgLMDR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 229 PKkawPPPLSTWVESAAEAHDAVHKAKHDGYDkikvysflsresydsiisaaGDVQMDVIGHIPMSVSLDyvldsgqkLI 308
Cdd:COG0402   156 GF---PDGLREDADEGLADSERLIERWHGAAD--------------------GRIRVALAPHAPYTVSPE--------LL 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 309 AHSEEVAKHAGGD---HSAEHIHELAGKMTASGvwMTPT-------LVTTRSIL--GVFADPD--GLLER--------PE 366
Cdd:COG0402   205 RAAAALARELGLPlhtHLAETRDEVEWVLELYG--KRPVeyldelgLLGPRTLLahCVHLTDEeiALLAEtgasvahcPT 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 367 AvyfqhpmqqgvwsfitdNLYrpipakareqLRSDFESFQKpltkaFHDGGGKLMTGTDTlfPGLVPGFALHRELEELVD 446
Cdd:COG0402   283 S-----------------NLK----------LGSGIAPVPR-----LLAAGVRVGLGTDG--AASNNSLDMFEEMRLAAL 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 447 VG---------LTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDAN-----PLEDVSAA-------SKIAGVFV 505
Cdd:COG0402   329 LQrlrggdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDaphlaPLHDPLSAlvyaadgRDVRTVWV 408


                  ....*...
gi 1760014703 506 RGRWIARE 513
Cdd:COG0402   409 AGRVVVRD 416
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 119-508 3.53e-12

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: 67.72  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 119 GRIAEVGPAsaVKLPARAVRIDATGRYLLPAFADMHVHL-LGEAWNVMLQPEAQKTSKDI-----------PFDEFLFPF 186
Cdd:cd01309     2 GKIVAVGAE--ITTPADAEVIDAKGKHVTPGLIDAHSHLgLDEEGGVRETSDANEETDPVtphvraidginPDDEAFKRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 187 IANGVTLVQSM--SATP---EELVVRErirRGELLGPRLILAPMidGPKKAWP--PPLSTWVES---------AAEAHDA 250
Cdd:cd01309    80 RAGGVTTVQVLpgSANLiggQGVVIKT---DGGTIEDMFIKAPA--GLKMALGenPKRVYGGKGkepatrmgvAALLRDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 251 VHKAKHDGYdKIKVYSFLSRESYDSiisaagDVQMDVI-----GHIPMSVSLdYVLDSGQKLIAHSEEVAKHAGGDHSAE 325
Cdd:cd01309   155 FIKAQEYGR-KYDLGKNAKKDPPER------DLKLEALlpvlkGEIPVRIHA-HRADDILTAIRIAKEFGIKITIEHGAE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 326 HiHELAGKMTASGVwmtptlvttrsilGVFADPDgllerpeavyfqhpmqqgvWSfitdnlyrpipakareqLRSDFESF 405
Cdd:cd01309   227 G-YKLADELAKHGI-------------PVIYGPT-------------------LT-----------------LPKKVEEV 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 406 QKPLTKAF---HDGGGKLMTGTDtlFPGLvPGFALHRELEELVDVGLTPFEALRTTTSAPFEYLGESERAGTIATGKETD 482
Cdd:cd01309   257 NDAIDTNAyllKKGGVAFAISSD--HPVL-NIRNLNLEAAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDAD 333

                         410       420
                  ....*....|....*....|....*.
gi 1760014703 483 LVLLDANPLEdvsAASKIAGVFVRGR 508
Cdd:cd01309   334 LVVWNGDPLE---PTSKPEQVYIDGR 356
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 97-157 2.03e-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: 59.52  E-value: 2.03e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760014703  97 HADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVKLPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:cd01298     5 NGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
85-161 2.69e-09

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 59.43  E-value: 2.69e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1760014703  85 AAPPGATIVaFVHADVIPMDRERVLRDHtVVIAGGRIAEVGPASAVK--LPARAVRIDATGRYLLPAFADMHVHLLGEA 161
Cdd:COG1574     3 LAAAAADLL-LTNGRIYTMDPAQPVAEA-VAVRDGRIVAVGSDAEVRalAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 114-157 3.68e-08

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: 55.87  E-value: 3.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:COG0044    18 VLIEDGRIAAIGPDLAA--PEAAEVIDATGLLVLPGLIDLHVHL 59
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 105-217 1.44e-07

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 53.74  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 105 RERVLRDHTVVIAGGRIAEVGPASAvkLPARAVRIDATGRYLLPAFADMHVHLLGEAwNVM-LQPEAQKTskdipFDEFL 183
Cdd:cd00854    10 TPGGLEDGAVLVEDGKIVAIGPEDE--LEEADEIIDLKGQYLVPGFIDIHIHGGGGA-DFMdGTAEALKT-----IAEAL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 184 fpfIANGVT--LVQSMSATPEEL-----VVRERIRRG---ELLG 217
Cdd:cd00854    82 ---AKHGTTsfLPTTVTAPPEEIakalaAIAEAIAEGqgaEILG 122
PRK05985 PRK05985
cytosine deaminase; Provisional
 99-162 2.33e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 53.01  E-value: 2.33e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1760014703  99 DVIPMDRERvlrdHTVVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL----LGEAW 162
Cdd:PRK05985    8 NVRPAGGAA----VDILIRDGRIAAIGPALAA--PPGAEVEDGGGALALPGLVDGHIHLdktfWGDPW 69
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 112-157 2.60e-07

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 53.02  E-value: 2.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1760014703 112 HTVVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:cd01293    15 VDIAIEDGRIAAIGPALAV--PPDAEEVDAKGRLVLPAFVDPHIHL 58
PRK09228 PRK09228
guanine deaminase; Provisional
 90-156 4.82e-07

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 52.12  E-value: 4.82e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760014703  90 ATIVAFVH--ADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVK--LPARAVRIDATGRYLLPAFADMHVH 156
Cdd:PRK09228    8 GRLLHFTAdpAEVDDEDALRYIEDGLLLVEDGRIVAAGPYAELRaqLPADAEVTDYRGKLILPGFIDTHIH 78
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
98-157 5.28e-07

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 51.92  E-value: 5.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  98 ADVIPMDRERVLRDHTVVIAGGRIAEVGPASAVKLPARavRIDATGRYLLPAFADMHVHL 157
Cdd:PRK07228    8 AGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDYDD--HIDATGKVVIPGLIQGHIHL 65
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
109-156 7.28e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 51.64  E-value: 7.28e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1760014703 109 LRDHTVVIAGGRIAEVGPAsavKLPARAVrIDATGRYLLPAFADMHVH 156
Cdd:COG1001    22 ILEGDIAIAGGRIAGVGDY---IGEATEV-IDAAGRYLVPGFIDGHVH 65
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 114-194 7.90e-07

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 51.71  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 114 VVIAGGRIAEVGPASAVklPARAVrIDATGRYLLPAFADMHVHLLGEawnVMLQPEAQktskdipfdeflfPFIANGVTL 193
Cdd:COG3653    24 VAIKGGRIVAVGDLAAA--EAARV-IDATGLVVAPGFIDIHTHYDLQ---LLWDPRLE-------------PSLRQGVTT 84


                  .
gi 1760014703 194 V 194
Cdd:COG3653    85 V 85
Amidohydro_3 pfam07969
Amidohydrolase family;
139-511 1.35e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 50.99  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 139 IDATGRYLLPAFADMHVHLLGEAWNVMLQP------------EAQKTSKDIP-----FDEFLFPFIANGVT---LVQSMS 198
Cdd:pfam07969   3 IDAKGRLVLPGFVDPHTHLDGGGLNLRELRlpdvlpnavvkgQAGRTPKGRWlvgegWDEAQFAETRFPYAladLDEVAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 199 ATPeeLVVRERIRRGELLGPRLILAPMIDGPKKAwPPPLSTWVESAAEAHDAVHKAKHDgydkiKVYSFLSRESYDSIIS 278
Cdd:pfam07969  83 DGP--VLLRALHTHAAVANSAALDLAGITKATED-PPGGEIARDANGEGLTGLLREGAY-----ALPPLLAREAEAAAVA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 279 AA-----GDVQMDVIGHIPMSVSLD----YVLDSGQKLIAHSEEVAKHAGGDHSAEHIHELAGKMTASGVWMTPTLVTTR 349
Cdd:pfam07969 155 AAlaalpGFGITSVDGGGGNVHSLDdyepLRELTAAEKLKELLDAPERLGLPHSIYELRIGAMKLFADGVLGSRTAALTE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 350 SIL-----------------------------GVFADPDG----LLERPEAVYFQHPMQQGVW----SFITDNLYRPIPA 392
Cdd:pfam07969 235 PYFdapgtgwpdfedealaelvaaarergldvAIHAIGDAtidtALDAFEAVAEKLGNQGRVRiehaQGVVPYTYSQIER 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 393 KAREQLRSDFE---------SFQKPLTKAFHDG----------GGKLMTGTDTLFPGLVPGFAL-----HRELEELVDVG 448
Cdd:pfam07969 315 VAALGGAAGVQpvfdplwgdWLQDRLGAERARGltpvkellnaGVKVALGSDAPVGPFDPWPRIgaavmRQTAGGGEVLG 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 449 ----LTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEdvSAASKIAGVFVRGRWIA 511
Cdd:pfam07969 395 pdeeLSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLT--VDPPAIADIRVRLTVVD 459
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 114-157 1.96e-06

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: 50.29  E-value: 1.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPASAVKLPARavRIDATGRYLLPAFADMHVHL 157
Cdd:cd01314    19 ILIEDGKIVAIGPNLEAPGGVE--VIDATGKYVLPGGIDPHTHL 60
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 113-163 2.30e-06

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: 49.99  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1760014703 113 TVVIAGGRIAEVGPASAVklPARAVrIDATGRYLLPAFADMHVHLLGEAWN 163
Cdd:cd01297    21 DVGIRDGRIAAIGPILST--SAREV-IDAAGLVVAPGFIDVHTHYDGQVFW 68
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
114-156 2.92e-06

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 49.40  E-value: 2.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPASAvklPARAVR-IDATGRYLLPAFADMHVH 156
Cdd:COG3964    22 IAIKDGKIAAVAKDID---AAEAKKvIDASGLYVTPGLIDLHTH 62
PRK07583 PRK07583
cytosine deaminase;
82-157 4.93e-06

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 48.83  E-value: 4.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014703  82 LSQAAPPGATIVAFVHADVipmdrervlrdhtvVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:PRK07583   25 LEGGVPPGDTLEGLVLVDI--------------EIADGKIAAILPAGGA--PDELPAVDLKGRMVWPCFVDMHTHL 84
pyrC PRK09357
dihydroorotase; Validated
 114-157 6.34e-06

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 48.65  E-value: 6.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPASAvklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:PRK09357   22 VLIDDGKIAAIGENIE---AEGAEVIDATGLVVAPGLVDLHVHL 62
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 114-161 1.19e-05

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 47.69  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1760014703 114 VVIAGGRIAEVGPASAVKL--PARAVRIDATGRYLLPAFADMHVHLLGEA 161
Cdd:cd01300     2 VAVRDGRIVAVGSDAEAKAlkGPATEVIDLKGKTVLPGFIDSHSHLLLGG 51
PRK08323 PRK08323
phenylhydantoinase; Validated
 114-157 2.68e-05

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 46.70  E-value: 2.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPASAVKlparavRIDATGRYLLPAFADMHVHL 157
Cdd:PRK08323   21 VLIEDGKIAAIGANLGDE------VIDATGKYVMPGGIDPHTHM 58
PRK09236 PRK09236
dihydroorotase; Reviewed
 114-156 2.93e-05

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 46.40  E-value: 2.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1760014703 114 VVIAGGRIAEVGPASAVKLPARAvrIDATGRYLLPAFADMHVH 156
Cdd:PRK09236   22 VLIENGRIAKIASSISAKSADTV--IDAAGRYLLPGMIDDQVH 62
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 114-158 3.56e-05

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: 46.10  E-value: 3.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1760014703 114 VVIAGGRIAEVGPASAVKL--PARAVRIDATGRYLLPAFADMHVHLL 158
Cdd:cd01296     1 IAIRDGRIAAVGPAASLPApgPAAAEEIDAGGRAVTPGLVDCHTHLV 47
PRK06846 PRK06846
putative deaminase; Validated
 112-176 3.56e-05

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 46.16  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 112 HTVVIAGGRIAEVGPASAVkLPARAVRIDATGRYLLPAFADMHVHL----LGEAW-------NVM--------LQPEAQK 172
Cdd:PRK06846   32 CTLEIQDGKIVAIRPNKQV-PDATLPTYDANGLLMLPAFREMHIHLdktyYGGPWkacrpakTIQdrieleqkELPELLP 110


                  ....
gi 1760014703 173 TSKD 176
Cdd:PRK06846  111 TTQE 114
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 97-157 4.09e-05

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 46.00  E-value: 4.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760014703  97 HADVI-PMD-RERVLRDHTVVIAGGRIAEVGPASAVKLPArAVRIDATGRYLLPAFADMHVHL 157
Cdd:PRK08203    7 NPLAIvTMDaARREIADGGLVVEGGRIVEVGPGGALPQPA-DEVFDARGHVVTPGLVNTHHHF 68
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 102-157 5.28e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 45.84  E-value: 5.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014703 102 PMDRERVLRDHTVV-----------IAGGRIAEVGPAsavkLPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:PRK13404    1 MMAFDLVIRGGTVVtatdtfqadigIRGGRIAALGEG----LGPGAREIDATGRLVLPGGVDSHCHI 63
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
114-156 5.43e-05

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 45.61  E-value: 5.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1760014703 114 VVIAGGRIAEVGPAsaVKLPARAVRIDATGRYLLPAFADMHVH 156
Cdd:PRK09237   21 IAIEDGKIAAVAGD--IDGSQAKKVIDLSGLYVSPGWIDLHVH 61
PRK06189 PRK06189
allantoinase; Provisional
 114-157 6.74e-05

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 45.46  E-value: 6.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 114 VVIAGGRIAEVGPAsaVKLPARAVrIDATGRYLLPAFADMHVHL 157
Cdd:PRK06189   23 IGIKNGKIAEIAPE--ISSPAREI-IDADGLYVFPGMIDVHVHF 63
PRK07572 PRK07572
cytosine deaminase; Validated
 110-157 1.41e-04

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 44.24  E-value: 1.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1760014703 110 RDHTVVIAGGRIAEVGPAsavkLPARAVR-IDATGRYLLPAFADMHVHL 157
Cdd:PRK07572   16 TGIDIGIAGGRIAAVEPG----LQAEAAEeIDAAGRLVSPPFVDPHFHM 60
PRK02382 PRK02382
dihydroorotase; Provisional
 101-156 2.40e-04

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 43.49  E-value: 2.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014703 101 IPMDRERVLRDhtVVIAGGRIAEVGPASAVKLPARavRIDATGRYLLPAFADMHVH 156
Cdd:PRK02382   11 VYYNNSLQPRD--VRIDGGKITAVGKDLDGSSSEE--VIDARGMLLLPGGIDVHVH 62
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 111-157 2.66e-04

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: 43.59  E-value: 2.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1760014703 111 DHTVVIAGGRIAEVGpasAVKLPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:TIGR00857   5 EVDILVEGGRIKKIG---KLRIPPDAEVIDAKGLLVLPGFIDLHVHL 48
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 111-154 4.61e-04

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 42.47  E-value: 4.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1760014703 111 DHTVVIAGGRIAEVGPASAvklpARAVRIDATGRYLLPAFADMH 154
Cdd:PRK15446   19 DGSLLIEDGRIAAIDPGAS----ALPGAIDAEGDYLLPGLVDLH 58
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 448-507 5.03e-04

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: 42.63  E-value: 5.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760014703 448 GLTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEDVS---AASKIAGVFVRG 507
Cdd:cd01296   309 RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAyrfGVNLVEYVIKNG 371
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 114-156 6.28e-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: 41.93  E-value: 6.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1760014703 114 VVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVH 156
Cdd:cd01307     2 VAIENGKIAAVGAALAA--PAATQIVDAGGCYVSPGWIDLHVH 42
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
449-510 8.99e-04

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 42.09  E-value: 8.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014703 449 LTPFEALRTTTSAPFEYLGESERAGTIATGKETDLVLLDANPLEdVSAAS----KIAGVFVRGRWI 510
Cdd:COG1574   467 LTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLT-VPPEEikdiKVLLTVVGGRVV 531
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 109-157 1.27e-03

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: 41.51  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1760014703 109 LRDHTVVIAGGRIAEVGPASAVklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:cd01315    15 VREADIAVKGGKIAAIGPDIAN--TEAEEVIDAGGLVVMPGLIDTHVHI 61
PRK08204 PRK08204
hypothetical protein; Provisional
 98-157 1.64e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 41.14  E-value: 1.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760014703  98 ADVIPMDRER-VLRDHTVVIAGGRIAEVGPASAvklPARAVRIDATGRYLLPAFADMHVHL 157
Cdd:PRK08204    9 GTVLTMDPAIgDLPRGDILIEGDRIAAVAPSIE---APDAEVVDARGMIVMPGLVDTHRHT 66
PRK07575 PRK07575
dihydroorotase; Provisional
 97-156 2.33e-03

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 40.43  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  97 HADVIPMDRERVLRDhtVVIAGGRIAEVGPASAVKLPARAvrIDATGRYLLPAFADMHVH 156
Cdd:PRK07575    9 NARILLPSGELLLGD--VLVEDGKIVAIAPEISATAVDTV--IDAEGLTLLPGVIDPQVH 64
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 98-157 3.18e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 40.12  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703  98 ADVIPMDRERvLRDHTVVIAGGRIAEVGPASAVKlpARAVrIDATGRYLLPAFADMHVHL 157
Cdd:PRK06038    9 AYVLTMDAGD-LKKGSVVIEDGTITEVSESTPGD--ADTV-IDAKGSVVMPGLVNTHTHA 64
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 114-209 4.74e-03

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 39.30  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014703 114 VVIAGGRIAEVGPA-SAVKLPARAVrIDATGRYLLPAFADMHVHLL---GEAWNVMLQPEAQKTSkdipfdeflfpFIAN 189
Cdd:cd01308    20 ILIAGGKILAIEDQlNLPGYENVTV-VDLHGKILVPGFIDQHVHIIgggGEGGPSTRTPEVTLSD-----------LTTA 87

                          90       100
                  ....*....|....*....|....*.
gi 1760014703 190 GVTLV------QSMSATPEELVVRER 209
Cdd:cd01308    88 GVTTVvgclgtDGISRSMEDLLAKAR 113
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
100-156 6.34e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 39.12  E-value: 6.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1760014703 100 VIPMD-RERVLRDHTVVIAGGRIAEVGP-ASAVKLPARAVRIDATGRYLLPAFADMHVH 156
Cdd:PRK09045   16 IVPVEpAGVVLEDHAVAIRDGRIVAILPrAEARARYAAAETVELPDHVLIPGLINAHTH 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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