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Conserved domains on  [gi|494663131|ref|WP_007421075|]
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amidohydrolase family protein [Idiomarina sp. A28L]

Protein Classification

amidohydrolase family protein( domain architecture ID 10217779)

amidohydrolase family protein is a metallo-dependent hydrolase with a TIM barrel fold and a conserved metal binding site, involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 608-968 9.81e-125

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: 384.36  E-value: 9.81e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  608 NGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAIS--------QGVNEGTEAITAEVRIGDVVNPDDIHIYRSL 679
Cdd:cd01309     1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDeeggvretSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  680 AGGATIAHLLHGSANPIGGQGQTIKLRWGENAEglKFRETPPTIKFALGENVKQSNWGGAntiRYPQTRMGVAQIMQDAF 759
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIED--MFIKAPAGLKMALGENPKRVYGGKG---KEPATRMGVAALLRDAF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  760 QQAREYEQAKADYNslsraeKRRTAPPRIDYRLESVLQVINSERHTHVHSYVASEVLALMDVVEQQGFKIhTFTHILEGY 839
Cdd:cd01309   156 IKAQEYGRKYDLGK------NAKKDPPERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKI-TIEHGAEGY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  840 KVAKEIAAHGAGASGFADWWAFK--IEAFDAIPHNMCLMMEQGVLTSINSDSNDL-QRRLNTEAAKSVRYcGMSENDALK 916
Cdd:cd01309   229 KLADELAKHGIPVIYGPTLTLPKkvEEVNDAIDTNAYLLKKGGVAFAISSDHPVLnIRNLNLEAAKAVKY-GLSYEEALK 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494663131  917 MITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYAQVQETWIEGRKYF 968
Cdd:cd01309   308 AITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 38-437 1.02e-37

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


:

Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 146.26  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   38 YQHNPNLIAFTNATLVTEPGER-LENATLVMENGIIRSIERNN--RAPNGARVIDASGYTLYPGFVDAYSNYGVEqpGQP 114
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAAdlAVPAGAEVIDATGKTVLPGLIDAHTHLGLG--GGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  115 APRGRSGTPIYSnerqggnasnsaihaeksWVDTFKPNADQAKSYVAQGFTTVQS------ARLDGIFRGRATTVSLADT 188
Cdd:COG1228    81 AVEFEAGGGITP------------------TVDLVNPADKRLRRALAAGVTTVRDlpggplGLRDAIIAGESKLLPGPRV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  189 I-ANNAIYQANGQHfasfdkgsstQQYPASLMgsiALIRQTLSDSrwyTEAAGLRASNGQVEFNA-------ALAALAGL 260
Cdd:COG1228   143 LaAGPALSLTGGAH----------ARGPEEAR---AALRELLAEG---ADYIKVFAEGGAPDFSLeelrailEAAHALGL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  261 KeqgLLFHANDEQSLLRAHRvlntFEVPVTYIGSGFEYARLNDVKETNARLILPLnfPAAPQLGEQYAELDVSLADLRHW 340
Cdd:COG1228   207 P---VAAHAHQADDIRLAVE----AGVDSIEHGTYLDDEVADLLAEAGTVVLVPT--LSLFLALLEGAAAPVAAKARKVR 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  341 ERAPSNPAVLAEAGVEFAF-TLHGIDKTA--DFWPNIRKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIV 417
Cdd:COG1228   278 EAALANARRLHDAGVPVALgTDAGVGVPPgrSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357

                         410       420
                  ....*....|....*....|....
gi 494663131  418 VSRGDLFAD----GEIVSVWLQGE 437
Cdd:COG1228   358 LLDGDPLEDiaylEDVRAVMKDGR 381
 
Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 608-968 9.81e-125

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: 384.36  E-value: 9.81e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  608 NGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAIS--------QGVNEGTEAITAEVRIGDVVNPDDIHIYRSL 679
Cdd:cd01309     1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDeeggvretSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  680 AGGATIAHLLHGSANPIGGQGQTIKLRWGENAEglKFRETPPTIKFALGENVKQSNWGGAntiRYPQTRMGVAQIMQDAF 759
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIED--MFIKAPAGLKMALGENPKRVYGGKG---KEPATRMGVAALLRDAF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  760 QQAREYEQAKADYNslsraeKRRTAPPRIDYRLESVLQVINSERHTHVHSYVASEVLALMDVVEQQGFKIhTFTHILEGY 839
Cdd:cd01309   156 IKAQEYGRKYDLGK------NAKKDPPERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKI-TIEHGAEGY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  840 KVAKEIAAHGAGASGFADWWAFK--IEAFDAIPHNMCLMMEQGVLTSINSDSNDL-QRRLNTEAAKSVRYcGMSENDALK 916
Cdd:cd01309   229 KLADELAKHGIPVIYGPTLTLPKkvEEVNDAIDTNAYLLKKGGVAFAISSDHPVLnIRNLNLEAAKAVKY-GLSYEEALK 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494663131  917 MITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYAQVQETWIEGRKYF 968
Cdd:cd01309   308 AITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 574-969 1.59e-55

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 197.88  E-value: 1.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  574 RTSQPEQQNLHIRNATVWTADDQGVLENTDIIVRNGLIHRVGK--DLSTPRGYTVIDATGMHITPGIIDEHSHIAISQGV 651
Cdd:COG1228     1 KKAPAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  652 NEGTEAITAEVRIGDVVNPDDIHIYRSLAGGATIAHLLHGSA-----NPIGGQGQTIKlrwgenaeGLKFRETPPTIKFA 726
Cdd:COG1228    81 AVEFEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPlglrdAIIAGESKLLP--------GPRVLAAGPALSLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  727 LGENVkqsnwggantiRYPqtrmgvaqimQDAFQQAREYEQAKADYNslsraeKRRTAPPRIDYRLESVLQVINSER--- 803
Cdd:COG1228   153 GGAHA-----------RGP----------EEARAALRELLAEGADYI------KVFAEGGAPDFSLEELRAILEAAHalg 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  804 -HTHVHSYVASEVLALMDvveqqgFKIHTFTHILEGYK-VAKEIAAHG------------AGASGFADWWAFKI-EAFDA 868
Cdd:COG1228   206 lPVAAHAHQADDIRLAVE------AGVDSIEHGTYLDDeVADLLAEAGtvvlvptlslflALLEGAAAPVAAKArKVREA 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  869 IPHNMCLMMEQGVLTSINSDSNDLQ---RRLNTEAAKSVRYcGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVF 945
Cdd:COG1228   280 ALANARRLHDAGVPVALGTDAGVGVppgRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVL 358

                         410       420
                  ....*....|....*....|....*..
gi 494663131  946 WNAHPLSAYAQVQ---ETWIEGRKYFD 969
Cdd:COG1228   359 LDGDPLEDIAYLEdvrAVMKDGRVVDR 385
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 38-437 1.02e-37

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 146.26  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   38 YQHNPNLIAFTNATLVTEPGER-LENATLVMENGIIRSIERNN--RAPNGARVIDASGYTLYPGFVDAYSNYGVEqpGQP 114
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAAdlAVPAGAEVIDATGKTVLPGLIDAHTHLGLG--GGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  115 APRGRSGTPIYSnerqggnasnsaihaeksWVDTFKPNADQAKSYVAQGFTTVQS------ARLDGIFRGRATTVSLADT 188
Cdd:COG1228    81 AVEFEAGGGITP------------------TVDLVNPADKRLRRALAAGVTTVRDlpggplGLRDAIIAGESKLLPGPRV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  189 I-ANNAIYQANGQHfasfdkgsstQQYPASLMgsiALIRQTLSDSrwyTEAAGLRASNGQVEFNA-------ALAALAGL 260
Cdd:COG1228   143 LaAGPALSLTGGAH----------ARGPEEAR---AALRELLAEG---ADYIKVFAEGGAPDFSLeelrailEAAHALGL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  261 KeqgLLFHANDEQSLLRAHRvlntFEVPVTYIGSGFEYARLNDVKETNARLILPLnfPAAPQLGEQYAELDVSLADLRHW 340
Cdd:COG1228   207 P---VAAHAHQADDIRLAVE----AGVDSIEHGTYLDDEVADLLAEAGTVVLVPT--LSLFLALLEGAAAPVAAKARKVR 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  341 ERAPSNPAVLAEAGVEFAF-TLHGIDKTA--DFWPNIRKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIV 417
Cdd:COG1228   278 EAALANARRLHDAGVPVALgTDAGVGVPPgrSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357

                         410       420
                  ....*....|....*....|....
gi 494663131  418 VSRGDLFAD----GEIVSVWLQGE 437
Cdd:COG1228   358 LLDGDPLEDiaylEDVRAVMKDGR 381
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 69-438 1.97e-28

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: 118.18  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   69 NGIIRSIERNNRAPNGARVIDASGYTLYPGFVDAYSNYGVeqpgQPAPRGRsgtpiysnERQGGNASNSAIHAEKSWVDT 148
Cdd:cd01309     1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGL----DEEGGVR--------ETSDANEETDPVTPHVRAIDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  149 FKPNADQAKSYVAQGFTTVQ----SARLDGifrGRATTVSLADTIANNAIYQANGQ-HFA-------SFDKGSstqQYPA 216
Cdd:cd01309    69 INPDDEAFKRARAGGVTTVQvlpgSANLIG---GQGVVIKTDGGTIEDMFIKAPAGlKMAlgenpkrVYGGKG---KEPA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  217 SLMGSIALIRQTLSDSRWYTEAAGLrASNGQVEFNAALAALAGL-----KEQGLLFHANDEQSLLRAHRVLNTFEVPVTy 291
Cdd:cd01309   143 TRMGVAALLRDAFIKAQEYGRKYDL-GKNAKKDPPERDLKLEALlpvlkGEIPVRIHAHRADDILTAIRIAKEFGIKIT- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  292 IGSGFEYARLNDV-KETNARLILPlnfpaaPQLGEQYaelDVSLADLRHWerapsNPAVLAEAG-VEFAFTlhgidktAD 369
Cdd:cd01309   221 IEHGAEGYKLADElAKHGIPVIYG------PTLTLPK---KVEEVNDAID-----TNAYLLKKGgVAFAIS-------SD 279

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494663131  370 fWPNI---------RKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVSRGDLF-ADGEIVSVWLQGEE 438
Cdd:cd01309   280 -HPVLnirnlnleaAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLePTSKPEQVYIDGRL 357
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 634-965 1.93e-09

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: 60.59  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   634 ITPGIIDEHSHIAISQGVNEGTEAITAEVRIgdvvnpdDIHIYRSLAGGatiahllHGSANPIGGQGQTIKLRWGENAEG 713
Cdd:pfam01979    2 VLPGLIDAHVHLEMGLLRGIPVPPEFAYEAL-------RLGITTMLKSG-------TTTVLDMGATTSTGIEALLEAAEE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   714 L--------KFRETPPTIKFALGENVKQSNWGGANTIRYPQTRMGVAQIMqDAFQQAREYEQAKAdynSLSRAEKRRtap 785
Cdd:pfam01979   68 LplglrflgPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLA-PHGAPTFSDDELKA---ALEEAKKYG--- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   786 pridyrlesvLQVinserHTHVHsyvasEVLALMDVVEQQGFKIHTFTHILEGYK------VAKEIAAHGAGASGfaDWW 859
Cdd:pfam01979  141 ----------LPV-----AIHAL-----ETKGEVEDAIAAFGGGIEHGTHLEVAEsgglldIIKLILAHGVHLSP--TEA 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   860 AFKIEAFDAIPHNMCL---------------MMEQGVLTSINSDS-------NDLQR-RLNTEAAKSVRYcGMSENDALK 916
Cdd:pfam01979  199 NLLAEHLKGAGVAHCPfsnsklrsgrialrkALEDGVKVGLGTDGagsgnslNMLEElRLALELQFDPEG-GLSPLEALR 277

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 494663131   917 MITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYA------QVQETWIEGR 965
Cdd:pfam01979  278 MATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFglkpdgNVKKVIVKGK 332
PRK02382 PRK02382
dihydroorotase; Provisional
 582-644 7.58e-09

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 59.28  E-value: 7.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494663131  582 NLHIRNATVWTaddQGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK02382    3 DALLKDGRVYY---NNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 42-101 4.58e-07

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 53.26  E-value: 4.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   42 PNLIAFTNATLVTEpgERLENATLVMENGIIRSIERNNRAPNGArvIDASGYTLYPGFVD 101
Cdd:PRK15446    1 MMEMILSNARLVLP--DEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD 56
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 352-437 3.23e-03

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: 40.95  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   352 EAGVEFAFtlhGID-----KTADFWPNIRKAV------AHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVSR 420
Cdd:pfam01979  232 EDGVKVGL---GTDgagsgNSLNMLEELRLALelqfdpEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVD 308

                           90       100
                   ....*....|....*....|....
gi 494663131   421 GDLFA-------DGEIVSVWLQGE 437
Cdd:pfam01979  309 LDPLAaffglkpDGNVKKVIVKGK 332
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 600-648 9.44e-03

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: 39.70  E-value: 9.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 494663131   600 ENTDIIVRNGLIHRVGK--DLSTPRGYTVIDATGMHITPGIIDEHSHIAIS 648
Cdd:TIGR01224    2 EDAVILIHGGKIVWIGQlaALPGEEATEIIDCGGGLVTPGLVDPHTHLVFA 52
 
Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 608-968 9.81e-125

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: 384.36  E-value: 9.81e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  608 NGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAIS--------QGVNEGTEAITAEVRIGDVVNPDDIHIYRSL 679
Cdd:cd01309     1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLDeeggvretSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  680 AGGATIAHLLHGSANPIGGQGQTIKLRWGENAEglKFRETPPTIKFALGENVKQSNWGGAntiRYPQTRMGVAQIMQDAF 759
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIED--MFIKAPAGLKMALGENPKRVYGGKG---KEPATRMGVAALLRDAF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  760 QQAREYEQAKADYNslsraeKRRTAPPRIDYRLESVLQVINSERHTHVHSYVASEVLALMDVVEQQGFKIhTFTHILEGY 839
Cdd:cd01309   156 IKAQEYGRKYDLGK------NAKKDPPERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIKI-TIEHGAEGY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  840 KVAKEIAAHGAGASGFADWWAFK--IEAFDAIPHNMCLMMEQGVLTSINSDSNDL-QRRLNTEAAKSVRYcGMSENDALK 916
Cdd:cd01309   229 KLADELAKHGIPVIYGPTLTLPKkvEEVNDAIDTNAYLLKKGGVAFAISSDHPVLnIRNLNLEAAKAVKY-GLSYEEALK 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494663131  917 MITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYAQVQETWIEGRKYF 968
Cdd:cd01309   308 AITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 574-969 1.59e-55

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 197.88  E-value: 1.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  574 RTSQPEQQNLHIRNATVWTADDQGVLENTDIIVRNGLIHRVGK--DLSTPRGYTVIDATGMHITPGIIDEHSHIAISQGV 651
Cdd:COG1228     1 KKAPAQAGTLLITNATLVDGTGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  652 NEGTEAITAEVRIGDVVNPDDIHIYRSLAGGATIAHLLHGSA-----NPIGGQGQTIKlrwgenaeGLKFRETPPTIKFA 726
Cdd:COG1228    81 AVEFEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPGGPlglrdAIIAGESKLLP--------GPRVLAAGPALSLT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  727 LGENVkqsnwggantiRYPqtrmgvaqimQDAFQQAREYEQAKADYNslsraeKRRTAPPRIDYRLESVLQVINSER--- 803
Cdd:COG1228   153 GGAHA-----------RGP----------EEARAALRELLAEGADYI------KVFAEGGAPDFSLEELRAILEAAHalg 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  804 -HTHVHSYVASEVLALMDvveqqgFKIHTFTHILEGYK-VAKEIAAHG------------AGASGFADWWAFKI-EAFDA 868
Cdd:COG1228   206 lPVAAHAHQADDIRLAVE------AGVDSIEHGTYLDDeVADLLAEAGtvvlvptlslflALLEGAAAPVAAKArKVREA 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  869 IPHNMCLMMEQGVLTSINSDSNDLQ---RRLNTEAAKSVRYcGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVF 945
Cdd:COG1228   280 ALANARRLHDAGVPVALGTDAGVGVppgRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVL 358

                         410       420
                  ....*....|....*....|....*..
gi 494663131  946 WNAHPLSAYAQVQ---ETWIEGRKYFD 969
Cdd:COG1228   359 LDGDPLEDIAYLEdvrAVMKDGRVVDR 385
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 38-437 1.02e-37

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 146.26  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   38 YQHNPNLIAFTNATLVTEPGER-LENATLVMENGIIRSIERNN--RAPNGARVIDASGYTLYPGFVDAYSNYGVEqpGQP 114
Cdd:COG1228     3 APAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAAdlAVPAGAEVIDATGKTVLPGLIDAHTHLGLG--GGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  115 APRGRSGTPIYSnerqggnasnsaihaeksWVDTFKPNADQAKSYVAQGFTTVQS------ARLDGIFRGRATTVSLADT 188
Cdd:COG1228    81 AVEFEAGGGITP------------------TVDLVNPADKRLRRALAAGVTTVRDlpggplGLRDAIIAGESKLLPGPRV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  189 I-ANNAIYQANGQHfasfdkgsstQQYPASLMgsiALIRQTLSDSrwyTEAAGLRASNGQVEFNA-------ALAALAGL 260
Cdd:COG1228   143 LaAGPALSLTGGAH----------ARGPEEAR---AALRELLAEG---ADYIKVFAEGGAPDFSLeelrailEAAHALGL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  261 KeqgLLFHANDEQSLLRAHRvlntFEVPVTYIGSGFEYARLNDVKETNARLILPLnfPAAPQLGEQYAELDVSLADLRHW 340
Cdd:COG1228   207 P---VAAHAHQADDIRLAVE----AGVDSIEHGTYLDDEVADLLAEAGTVVLVPT--LSLFLALLEGAAAPVAAKARKVR 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  341 ERAPSNPAVLAEAGVEFAF-TLHGIDKTA--DFWPNIRKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIV 417
Cdd:COG1228   278 EAALANARRLHDAGVPVALgTDAGVGVPPgrSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357

                         410       420
                  ....*....|....*....|....
gi 494663131  418 VSRGDLFAD----GEIVSVWLQGE 437
Cdd:COG1228   358 LLDGDPLEDiaylEDVRAVMKDGR 381
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 69-438 1.97e-28

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: 118.18  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   69 NGIIRSIERNNRAPNGARVIDASGYTLYPGFVDAYSNYGVeqpgQPAPRGRsgtpiysnERQGGNASNSAIHAEKSWVDT 148
Cdd:cd01309     1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGL----DEEGGVR--------ETSDANEETDPVTPHVRAIDG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  149 FKPNADQAKSYVAQGFTTVQ----SARLDGifrGRATTVSLADTIANNAIYQANGQ-HFA-------SFDKGSstqQYPA 216
Cdd:cd01309    69 INPDDEAFKRARAGGVTTVQvlpgSANLIG---GQGVVIKTDGGTIEDMFIKAPAGlKMAlgenpkrVYGGKG---KEPA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  217 SLMGSIALIRQTLSDSRWYTEAAGLrASNGQVEFNAALAALAGL-----KEQGLLFHANDEQSLLRAHRVLNTFEVPVTy 291
Cdd:cd01309   143 TRMGVAALLRDAFIKAQEYGRKYDL-GKNAKKDPPERDLKLEALlpvlkGEIPVRIHAHRADDILTAIRIAKEFGIKIT- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  292 IGSGFEYARLNDV-KETNARLILPlnfpaaPQLGEQYaelDVSLADLRHWerapsNPAVLAEAG-VEFAFTlhgidktAD 369
Cdd:cd01309   221 IEHGAEGYKLADElAKHGIPVIYG------PTLTLPK---KVEEVNDAID-----TNAYLLKKGgVAFAIS-------SD 279

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494663131  370 fWPNI---------RKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVSRGDLF-ADGEIVSVWLQGEE 438
Cdd:cd01309   280 -HPVLnirnlnleaAKAVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLePTSKPEQVYIDGRL 357
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 584-645 6.82e-13

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: 72.05  E-value: 6.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  584 HIRNATVWTADDqgvLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:COG0044     1 LIKNGRVVDPGG---LERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHL 59
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 585-645 8.11e-12

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: 68.78  E-value: 8.11e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131  585 IRNATVWTADDQgvlENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:cd01314     3 IKNGTIVTADGS---FKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHL 60
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
585-677 1.75e-11

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 67.11  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVwtADD-QGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHiaisqgVNEGTEAITaevr 663
Cdd:COG3964     4 IKGGRV--IDPaNGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH------VFPGGTDYG---- 71

                          90
                  ....*....|....
gi 494663131  664 igdvVNPDDIHIYR 677
Cdd:COG3964    72 ----VDPDGVGVRS 81
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 583-965 1.01e-10

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: 65.23  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  583 LHIRNATVWTADDQ-GVLENTDIIVRNGLIHRVGKDLSTPRGYT---VIDATGMHITPGIIDEHSHIAIS--QGVNEGTE 656
Cdd:COG0402     2 LLIRGAWVLTMDPAgGVLEDGAVLVEDGRIAAVGPGAELPARYPaaeVIDAGGKLVLPGLVNTHTHLPQTllRGLADDLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  657 AIT--AEV--RIGDVVNPDDIH------IYRSLAGGAT----IAHLLHGSANPIGGQGQTIKLR------WGENAEGLKF 716
Cdd:COG0402    82 LLDwlEEYiwPLEARLDPEDVYagallaLAEMLRSGTTtvadFYYVHPESADALAEAAAEAGIRavlgrgLMDRGFPDGL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  717 RETPPTIkFALGENVKQsNWGGANtirYPQTRMGVA---------QIMQDAFQQAREY---------EQAKADYNSLSRA 778
Cdd:COG0402   162 REDADEG-LADSERLIE-RWHGAA---DGRIRVALAphapytvspELLRAAAALARELglplhthlaETRDEVEWVLELY 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  779 EKRRTAppridyRLES--VLqvinSERHTHVHS-YVASEVLALMdvveqqgfkihtfthilegykvakeiAAHGAG---- 851
Cdd:COG0402   237 GKRPVE------YLDElgLL----GPRTLLAHCvHLTDEEIALL--------------------------AETGASvahc 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  852 -------ASGFADWWAfkieafdaiphnmclMMEQGVLTSINSD---SND-------------LQRRLNTEAAKsvrycg 908
Cdd:COG0402   281 ptsnlklGSGIAPVPR---------------LLAAGVRVGLGTDgaaSNNsldmfeemrlaalLQRLRGGDPTA------ 339

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  909 MSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNA---------HPLSA--YA----QVQETWIEGR 965
Cdd:COG0402   340 LSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLdaphlaplhDPLSAlvYAadgrDVRTVWVAGR 411
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
904-965 2.00e-10

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 63.96  E-value: 2.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  904 VRYCGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNAHpLsayaQVQETWIEGR 965
Cdd:COG1820   317 VEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD-L----NVRATWVGGE 373
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 582-645 1.52e-09

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: 61.54  E-value: 1.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  582 NLHIRNATVWTADdqGVLEnTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:cd01315     1 DLVIKNGRVVTPD--GVRE-ADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 634-965 1.93e-09

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: 60.59  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   634 ITPGIIDEHSHIAISQGVNEGTEAITAEVRIgdvvnpdDIHIYRSLAGGatiahllHGSANPIGGQGQTIKLRWGENAEG 713
Cdd:pfam01979    2 VLPGLIDAHVHLEMGLLRGIPVPPEFAYEAL-------RLGITTMLKSG-------TTTVLDMGATTSTGIEALLEAAEE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   714 L--------KFRETPPTIKFALGENVKQSNWGGANTIRYPQTRMGVAQIMqDAFQQAREYEQAKAdynSLSRAEKRRtap 785
Cdd:pfam01979   68 LplglrflgPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLA-PHGAPTFSDDELKA---ALEEAKKYG--- 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   786 pridyrlesvLQVinserHTHVHsyvasEVLALMDVVEQQGFKIHTFTHILEGYK------VAKEIAAHGAGASGfaDWW 859
Cdd:pfam01979  141 ----------LPV-----AIHAL-----ETKGEVEDAIAAFGGGIEHGTHLEVAEsgglldIIKLILAHGVHLSP--TEA 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   860 AFKIEAFDAIPHNMCL---------------MMEQGVLTSINSDS-------NDLQR-RLNTEAAKSVRYcGMSENDALK 916
Cdd:pfam01979  199 NLLAEHLKGAGVAHCPfsnsklrsgrialrkALEDGVKVGLGTDGagsgnslNMLEElRLALELQFDPEG-GLSPLEALR 277

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 494663131   917 MITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYA------QVQETWIEGR 965
Cdd:pfam01979  278 MATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFglkpdgNVKKVIVKGK 332
PRK02382 PRK02382
dihydroorotase; Provisional
 582-644 7.58e-09

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 59.28  E-value: 7.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494663131  582 NLHIRNATVWTaddQGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK02382    3 DALLKDGRVYY---NNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
585-645 7.81e-09

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 58.71  E-value: 7.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131  585 IRNATVwTADDQGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:PRK09237    3 LRGGRV-IDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV 62
PRK08323 PRK08323
phenylhydantoinase; Validated
 583-647 1.74e-08

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 58.26  E-value: 1.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494663131  583 LHIRNATVWTADDQGvleNTDIIVRNGLIHRVGKDlstpRGYTVIDATGMHITPGIIDEHSHIAI 647
Cdd:PRK08323    3 TLIKNGTVVTADDTY---KADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEM 60
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 585-646 1.99e-08

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: 57.60  E-value: 1.99e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNATVWTADDQGVLENTDIIVRNGLIHRVGKDLSTPRGY--TVIDATGMHITPGIIDEHSHIA 646
Cdd:cd01298     3 IRNGTIVTTDPRRVLEDGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLA 66
PLN02942 PLN02942
dihydropyrimidinase
 583-658 2.38e-08

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 57.93  E-value: 2.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131  583 LHIRNATVWTADDQgvlENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAISqgvNEGTEAI 658
Cdd:PLN02942    7 ILIKGGTVVNAHHQ---ELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMP---FMGTETI 76
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
913-971 8.71e-08

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 55.96  E-value: 8.71e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494663131  913 DALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNAHPLSAYA------QVQETWIEGRKYFDRA 971
Cdd:COG1574   471 EALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPeeikdiKVLLTVVGGRVVYEAE 535
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 603-645 1.66e-07

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: 54.64  E-value: 1.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 494663131  603 DIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:cd01307     1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV 43
PRK09060 PRK09060
dihydroorotase; Validated
 583-644 1.78e-07

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 54.93  E-value: 1.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  583 LHIRNATVWTADDQGVlenTDIIVRNGLIHRVGkDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK09060    7 LILKGGTVVNPDGEGR---ADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVH 64
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
46-101 1.83e-07

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 54.72  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   46 AFTNATLVTePGERLENATLVMENGIIRSIERnnRAPNGARVIDASGYTLYPGFVD 101
Cdd:COG1820     1 AITNARIFT-GDGVLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFID 53
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 585-646 2.11e-07

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 54.70  E-value: 2.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  585 IRNATVWTADDQgvlENTDIIVRNGLIHRVGKDLSTprGYTVIDATGMHITPGIIDEHSHIA 646
Cdd:PRK13404    8 IRGGTVVTATDT---FQADIGIRGGRIAALGEGLGP--GAREIDATGRLVLPGGVDSHCHID 64
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 904-964 2.81e-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: 54.12  E-value: 2.81e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131  904 VRYCGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNahplSAYaQVQETWIEG 964
Cdd:cd00854   319 VKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD----DDL-NVKATWING 374
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
585-644 3.69e-07

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 53.56  E-value: 3.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADdqGVLENTDIIVRNGLIHRVGKDlsTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:COG1820     2 ITNARIFTGD--GVLEDGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 42-101 4.58e-07

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 53.26  E-value: 4.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   42 PNLIAFTNATLVTEpgERLENATLVMENGIIRSIERNNRAPNGArvIDASGYTLYPGFVD 101
Cdd:PRK15446    1 MMEMILSNARLVLP--DEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD 56
PRK09236 PRK09236
dihydroorotase; Reviewed
 585-644 5.50e-07

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 53.34  E-value: 5.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNATVwtaddqgVLENT----DIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK09236    6 IKNARI-------VNEGKifegDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH 62
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 585-644 6.69e-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: 52.58  E-value: 6.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTaddQGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:cd00854     3 IKNARILT---PGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 47-102 7.77e-07

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: 52.79  E-value: 7.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   47 FTNATLVTEpgERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDA 102
Cdd:COG0044     2 IKNGRVVDP--GGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDL 55
pyrC PRK09357
dihydroorotase; Validated
 585-644 1.15e-06

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 52.12  E-value: 1.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWtaDDQGVLENTDIIVRNGLIHRVGKDLSTPrGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK09357    5 IKNGRVI--DPKGLDEVADVLIDDGKIAAIGENIEAE-GAEVIDATGLVVAPGLVDLHVH 61
PRK07575 PRK07575
dihydroorotase; Provisional
 581-644 1.27e-06

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 51.98  E-value: 1.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  581 QNLHIRNATVWTADdqGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK07575    3 MSLLIRNARILLPS--GELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVH 64
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 585-644 1.79e-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: 51.53  E-value: 1.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131  585 IRNATVwtADDQGVL-ENTDIIVRNGLIHRVGKDLSTPrGYTVIDATGMHITPGIIDEHSH 644
Cdd:cd01297     4 IRNGTV--VDGTGAPpFTADVGIRDGRIAAIGPILSTS-AREVIDAAGLVVAPGFIDVHTH 61
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 603-651 1.94e-06

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: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131  603 DIIVRNGLIHRVGkDLSTPRGYTVIDATGMHITPGIIDEHSHI------------AISQGV 651
Cdd:COG3653    23 DVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHTHYdlqllwdprlepSLRQGV 82
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 45-101 2.20e-06

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: 51.04  E-value: 2.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 494663131   45 IAFTNATLVTEpgERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVD 101
Cdd:cd00854     1 LIIKNARILTP--GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFID 55
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
374-437 3.51e-06

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 50.48  E-value: 3.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494663131  374 IRKAVAH-GLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVsrgdLFADGEIVSVWLQGE 437
Cdd:COG1820   313 VRNLVEWtGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVV----LDDDLNVRATWVGGE 373
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 876-948 3.98e-06

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: 50.33  E-value: 3.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131  876 MMEQGVLTSINSDSNDLQ---RRLNTEAAKSVRYCGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNA 948
Cdd:cd01296   274 LIDAGVPVALGTDFNPGSsptSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDA 349
PRK06189 PRK06189
allantoinase; Provisional
 582-644 4.28e-06

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 50.47  E-value: 4.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494663131  582 NLHIRNATVWTADdqGVlENTDIIVRNGLIHRVGKDLSTPrGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK06189    4 DLIIRGGKVVTPE--GV-YRADIGIKNGKIAEIAPEISSP-AREIIDADGLYVFPGMIDVHVH 62
PRK08044 PRK08044
allantoinase AllB;
582-646 5.19e-06

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 50.24  E-value: 5.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494663131  582 NLHIRNATVwtaddqgVLEN----TDIIVRNGLIHRVGKDLSTPRgyTVIDATGMHITPGIIDEHSHIA 646
Cdd:PRK08044    4 DLIIKNGTV-------ILENearvVDIAVKGGKIAAIGQDLGDAK--EVMDASGLVVSPGMVDAHTHIS 63
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 45-102 6.68e-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: 49.91  E-value: 6.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 494663131   45 IAFTNATLVTEpgERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDA 102
Cdd:cd01314     1 LIIKNGTIVTA--DGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDP 56
PRK08204 PRK08204
hypothetical protein; Provisional
 585-675 7.67e-06

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 49.62  E-value: 7.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADDQ-GVLENTDIIVRNGLIHRVGKDLSTPrGYTVIDATGMHITPGIIDEHSHI--AISQGVNEGTEAITAE 661
Cdd:PRK08204    6 IRGGTVLTMDPAiGDLPRGDILIEGDRIAAVAPSIEAP-DAEVVDARGMIVMPGLVDTHRHTwqSVLRGIGADWTLQTYF 84

                          90
                  ....*....|....*...
gi 494663131  662 VRI----GDVVNPDDIHI 675
Cdd:PRK08204   85 REIhgnlGPMFRPEDVYI 102
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 585-668 1.13e-05

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: 48.93  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADDQGvleNTDIIVRNGLIHRVGKDLSTPRGY--TVIDATGMHITPGIIDEHSHIaISQGVNEGTEAITAEV 662
Cdd:cd01308     4 IKNAEVYAPEYLG---KKDILIAGGKILAIEDQLNLPGYEnvTVVDLHGKILVPGFIDQHVHI-IGGGGEGGPSTRTPEV 79


                  ....*.
gi 494663131  663 RIGDVV 668
Cdd:cd01308    80 TLSDLT 85
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 899-945 1.54e-05

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 48.43  E-value: 1.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 494663131  899 EAAK-SVRYCGMSENDALKMITLYPAMQLEIDEYVGSITAGKHADL-VF 945
Cdd:PRK11170  315 EAVRnLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLtAF 363
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 45-102 2.60e-05

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: 47.90  E-value: 2.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494663131   45 IAFTNATLVT--EPGERLENATLVMENGIIRSIERNNRAPN---GARVIDASGYTLYPGFVDA 102
Cdd:COG0402     2 LLIRGAWVLTmdPAGGVLEDGAVLVEDGRIAAVGPGAELPArypAAEVIDAGGKLVLPGLVNT 64
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
583-654 3.17e-05

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 47.88  E-value: 3.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494663131  583 LHIRNATVWtadD--QGV-LENTDIIVRNGlihRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAISQgVNEG 654
Cdd:COG1229     3 LIIKNGRVY---DpaNGIdGEVMDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTHIAGGK-VNVG 70
Amidohydro_3 pfam07969
Amidohydrolase family;
875-965 4.34e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.14  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   875 LMMEQGVLTSINSDSND--------LQRRLNTEAAKSVRYCGMSE----NDALKMITLYPAMQLEIDEYVGSITAGKHAD 942
Cdd:pfam07969  353 ELLNAGVKVALGSDAPVgpfdpwprIGAAVMRQTAGGGEVLGPDEelslEEALALYTSGPAKALGLEDRKGTLGVGKDAD 432

                           90       100
                   ....*....|....*....|....*....
gi 494663131   943 LVFWNAHPLS------AYAQVQETWIEGR 965
Cdd:pfam07969  433 LVVLDDDPLTvdppaiADIRVRLTVVDGR 461
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
575-646 8.32e-05

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 46.33  E-value: 8.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131  575 TSQPEQQNLHIRNATVWTADDQGVlENTDIIVRNGLIHRVGKDLS----TPRGYTVIDATGMHITPGIIDEHSHIA 646
Cdd:COG1574     2 KLAAAAADLLLTNGRIYTMDPAQP-VAEAVAVRDGRIVAVGSDAEvralAGPATEVIDLGGKTVLPGFIDAHVHLL 76
PRK09236 PRK09236
dihydroorotase; Reviewed
 44-101 1.50e-04

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 45.63  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 494663131   44 LIafTNATLVTEpGERLEnATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVD 101
Cdd:PRK09236    5 LI--KNARIVNE-GKIFE-GDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMID 58
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
585-645 1.83e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 45.48  E-value: 1.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNAT---VWTaddqGVLENTDIIVRNGLIHRVGKdlSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:COG1001     9 IKNGRlvnVFT----GEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI 66
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 47-102 1.86e-04

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 45.36  E-value: 1.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   47 FTNATLVTEPGERleNATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDA 102
Cdd:cd01315     4 IKNGRVVTPDGVR--EADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDT 57
PRK07203 PRK07203
putative aminohydrolase SsnA;
585-652 2.04e-04

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 44.93  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNATVWTADDQ-GVLENTDIIVRNGLIHRVGK--DLSTP-RGYTVIDATGMHITPGIIDEHSHI--AISQGVN 652
Cdd:PRK07203    4 IGNGTAITRDPAkPVIEDGAIAIEGNVIVEIGTtdELKAKyPDAEFIDAKGKLIMPGLINSHNHIysGLARGMM 77
PRK09061 PRK09061
D-glutamate deacylase; Validated
 603-644 2.80e-04

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 44.69  E-value: 2.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 494663131  603 DIIVRNGLIHRVGKDLSTPRgyTVIDATGMHITPGIIDEHSH 644
Cdd:PRK09061   40 DVGIKGGKIAAVGTAAIEGD--RTIDATGLVVAPGFIDLHAH 79
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 604-645 3.04e-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: 44.17  E-value: 3.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 494663131  604 IIVRNGLIHRVGK----DLSTPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:cd01296     1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
PRK05985 PRK05985
cytosine deaminase; Provisional
 43-117 3.10e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 44.54  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   43 NLIAFTNATLVTepGERLEnatLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDAY-----SNYGVE-QPGQPAP 116
Cdd:PRK05985    2 TDLLFRNVRPAG--GAAVD---ILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHihldkTFWGDPwYPNEPGP 76


                  .
gi 494663131  117 R 117
Cdd:PRK05985   77 S 77
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 585-672 3.92e-04

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629 [Multi-domain]  Cd Length: 541  Bit Score: 44.33  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADDQGVLENTDIIVRNGlihRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHIAisqgvnegteaiTAEVRI 664
Cdd:cd01304     1 IKNGTVYDPLNGINGEKMDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSHIA------------GGKVNV 65


                  ....*...
gi 494663131  665 GDVVNPDD 672
Cdd:cd01304    66 GRILRPED 73
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
585-644 5.33e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.83  E-value: 5.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADDQGVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK07228    5 IKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
373-431 6.24e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 43.55  E-value: 6.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494663131  373 NIRKAVAHGLSSDNALAALTTVPAQIAGVANQsGKLAAGYRGDIVVSRgDL--------FADGEIVS 431
Cdd:COG1001   275 VVRRAIELGLDPVTAIQMATLNAAEHFGLKDL-GAIAPGRRADIVLLD-DLedfkvekvYADGKLVA 339
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
914-991 6.37e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 43.36  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  914 ALKMITLYPAMQLEIDEYVGSITAGKHADLVFWNA---------HPLS--AYA----QVQETWIEGRKYfdraddLAARE 978
Cdd:PRK09045  345 ALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLsgletqpvyDPVSqlVYAagreQVSHVWVAGKQL------LDDRE 418

                          90
                  ....*....|...
gi 494663131  979 AVELERQALIQKV 991
Cdd:PRK09045  419 LTTLDEAELLARA 431
pyrC PRK09357
dihydroorotase; Validated
 45-101 8.17e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 43.26  E-value: 8.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 494663131   45 IAFTNATLVTEPGErLENATLVMENGIIRSIERNNrAPNGARVIDASGYTLYPGFVD 101
Cdd:PRK09357    3 ILIKNGRVIDPKGL-DEVADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVD 57
PRK09059 PRK09059
dihydroorotase; Validated
 45-102 1.07e-03

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 42.71  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131   45 IAFTNATLVtEPGERL-ENATLVMENGIIRSIER---NNRAPNGARVIDASGYTLYPGFVDA 102
Cdd:PRK09059    5 ILLANARII-DPSRGLdEIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDA 65
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 585-644 1.24e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 42.48  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATVWTADDQGVLEnTDIIVRNGLIHRVGKDLSTPRGyTVIDATGMHITPGIIDEHSH 644
Cdd:PRK08393    5 IKNGYVIYGENLKVIR-ADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTH 62
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 585-644 1.26e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 42.53  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494663131  585 IRNATVWTADDQG-VLENTDIIVRNGLIHRVGKDLSTPRGY-TVIDATGMHITPGIIDEHSH 644
Cdd:PRK08203    6 KNPLAIVTMDAARrEIADGGLVVEGGRIVEVGPGGALPQPAdEVFDARGHVVTPGLVNTHHH 67
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 46-101 1.46e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 42.27  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   46 AFTNATLVTEpGERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVD 101
Cdd:PRK11170    3 ALTNGRIYTG-HEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFID 57
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 350-426 1.58e-03

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: 41.90  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  350 LAEAGVEFAF---TLHGIDKTADFWPNIRKAVAHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVSRGDLFAD 426
Cdd:cd01299   259 AHKAGVKIAFgtdAGFPVPPHGWNARELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDPLED 338
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 585-648 1.63e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 42.04  E-value: 1.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNATVWTADdQGVLENTDIIVRNGLIHRVGKDLSTpRGYTVIDATGMHITPGIIDEHSHIAIS 648
Cdd:PRK06038    6 IKNAYVLTMD-AGDLKKGSVVIEDGTITEVSESTPG-DADTVIDAKGSVVMPGLVNTHTHAAMT 67
PRK12394 PRK12394
metallo-dependent hydrolase;
603-671 1.64e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 42.05  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  603 DIIVRNGLI-----HRVGK-----------DLS---TPRGYTVIDATGMHITPGIIDEHSHIaisqgVNEGTEaitaevr 663
Cdd:PRK12394    4 DILITNGHIidparNINEInnlriindiivDADkypVASETRIIHADGCIVTPGLIDYHAHV-----FYDGTE------- 71


                  ....*...
gi 494663131  664 IGdvVNPD 671
Cdd:PRK12394   72 GG--VRPD 77
PRK09059 PRK09059
dihydroorotase; Validated
 600-645 1.92e-03

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 41.94  E-value: 1.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 494663131  600 ENTDIIVRNGLIHRVGKDL---STPRGYTVIDATGMHITPGIIDEHSHI 645
Cdd:PRK09059   21 EIGTVLIEDGVIVAAGKGAgnqGAPEGAEIVDCAGKAVAPGLVDARVFV 69
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 587-661 2.01e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 41.88  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  587 NATVWTADDqgVLENTDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDehshiaiSQ-----GV--NEGTEAIT 659
Cdd:PRK11170    6 NGRIYTGHE--VLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFID-------LQlngcgGVqfNDTAEAIS 76


                  ..
gi 494663131  660 AE 661
Cdd:PRK11170   77 VE 78
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 47-102 2.04e-03

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: 41.85  E-value: 2.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   47 FTNATLVTEPGERlenATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDA 102
Cdd:cd01293     2 LRNARLADGGTAL---VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDP 54
PRK05985 PRK05985
cytosine deaminase; Provisional
 585-644 2.31e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 41.46  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  585 IRNATvwTADDQGVlentDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSH 644
Cdd:PRK05985    6 FRNVR--PAGGAAV----DILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIH 59
PLN02942 PLN02942
dihydropyrimidinase
 58-113 3.10e-03

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 41.37  E-value: 3.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131   58 ERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDAYSNYGVEQPGQ 113
Cdd:PLN02942   18 HHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGT 73
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 352-437 3.23e-03

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: 40.95  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   352 EAGVEFAFtlhGID-----KTADFWPNIRKAV------AHGLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVSR 420
Cdd:pfam01979  232 EDGVKVGL---GTDgagsgNSLNMLEELRLALelqfdpEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVD 308

                           90       100
                   ....*....|....*....|....
gi 494663131   421 GDLFA-------DGEIVSVWLQGE 437
Cdd:pfam01979  309 LDPLAaffglkpDGNVKKVIVKGK 332
Amidohydro_3 pfam07969
Amidohydrolase family;
341-437 4.26e-03

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 40.98  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   341 ERAPSNPAV--LAEAGVEFAFTLHGIDKTADFWPNIRKAVAH-------------GLSSDNALAALTTVPAQIAGVANQS 405
Cdd:pfam07969  343 ERARGLTPVkeLLNAGVKVALGSDAPVGPFDPWPRIGAAVMRqtagggevlgpdeELSLEEALALYTSGPAKALGLEDRK 422

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 494663131   406 GKLAAGYRGDIVVSRGDLF-------ADGEIVSVWLQGE 437
Cdd:pfam07969  423 GTLGVGKDADLVVLDDDPLtvdppaiADIRVRLTVVDGR 461
PRK02382 PRK02382
dihydroorotase; Provisional
 47-114 4.54e-03

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 40.79  E-value: 4.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494663131   47 FTNATLV---TEPGERLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVDAYSNYgvEQPGQP 114
Cdd:PRK02382    1 MRDALLKdgrVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHF--REPGYT 69
PRK12393 PRK12393
amidohydrolase; Provisional
 581-662 5.18e-03

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 40.44  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  581 QNLHIRNAT-VWT--ADDQGVLENTDIIVRNGLIHRVGKDLSTPrGYTVIDATGMHITPGIIDEHSHI------AISQGV 651
Cdd:PRK12393    2 PSLLIRNAAaIMTglPGDAARLGGPDIRIRDGRIAAIGALTPLP-GERVIDATDCVVYPGWVNTHHHLfqsllkGVPAGI 80

                          90
                  ....*....|.
gi 494663131  652 NEGTEAITAEV 662
Cdd:PRK12393   81 NQSLTAWLAAV 91
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 48-102 6.17e-03

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: 40.26  E-value: 6.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 494663131   48 TNATLVT-EPGERLENATLVMENGIIRSIERNNRAPN--GARVIDASGYTLYPGFVDA 102
Cdd:cd01298     4 RNGTIVTtDPRRVLEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNT 61
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 584-684 6.18e-03

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: 40.31  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131  584 HIRNATVWTADDQGVlentDIIVRNGLIHRVGKDLSTPRGYTVIDATGMHITPGIIDEHSHI----------AISQGVNe 653
Cdd:cd01293     1 LLRNARLADGGTALV----DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktftggrwpNNSGGTL- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 494663131  654 gTEAITAEVRIGDVVNPDDI------HIYRSLAGGAT 684
Cdd:cd01293    76 -LEAIIAWEERKLLLTAEDVkeraerALELAIAHGTT 111
PRK07575 PRK07575
dihydroorotase; Provisional
 49-101 6.83e-03

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 40.04  E-value: 6.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494663131   49 NATLVTEPGErLENATLVMENGIIRSIERNNRAPNGARVIDASGYTLYPGFVD 101
Cdd:PRK07575    9 NARILLPSGE-LLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVID 60
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 381-436 7.15e-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: 39.87  E-value: 7.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494663131  381 GLSSDNALAALTTVPAQIAGVANQSGKLAAGYRGDIVVsrgdLFADGEIVSVWLQG 436
Cdd:cd00854   323 GCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVV----LDDDLNVKATWING 374
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 585-648 7.79e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 39.87  E-value: 7.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494663131  585 IRNATVWTADDQGVLENTDIIVRNGLIHRVGKDlsTPRGYTVIDATGMHITPGIIDEHSHIAIS 648
Cdd:PRK06380    5 IKNAWIVTQNEKREILQGNVYIEGNKIVYVGDV--NEEADYIIDATGKVVMPGLINTHAHVGMT 66
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 585-643 8.29e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 39.78  E-value: 8.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 494663131  585 IRNATVWTADDqgvLENTDIIVRNGLIHRVGKDLSTPRGytVIDATGMHITPGIIDEHS 643
Cdd:PRK15446    6 LSNARLVLPDE---VVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
ureC PRK13308
urease subunit alpha; Reviewed
 919-946 8.42e-03

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 40.08  E-value: 8.42e-03
                          10        20
                  ....*....|....*....|....*...
gi 494663131  919 TLYPAMQLEIDEYVGSITAGKHADLVFW 946
Cdd:PRK13308  410 TINPAITFGIDDHIGSLEPGKLADIVLW 437
ureC PRK13207
urease subunit alpha; Reviewed
 918-947 9.43e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 39.78  E-value: 9.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 494663131  918 ITLYPAMQLEIDEYVGSITAGKHADLVFWN 947
Cdd:PRK13207  408 YTINPAIAHGISHEVGSVEVGKLADLVLWK 437
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 600-648 9.44e-03

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: 39.70  E-value: 9.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 494663131   600 ENTDIIVRNGLIHRVGK--DLSTPRGYTVIDATGMHITPGIIDEHSHIAIS 648
Cdd:TIGR01224    2 EDAVILIHGGKIVWIGQlaALPGEEATEIIDCGGGLVTPGLVDPHTHLVFA 52
PRK07203 PRK07203
putative aminohydrolase SsnA;
49-116 9.85e-03

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 39.53  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494663131   49 NATLVTEPGER--LENATLVMENGIIRSI----ERNNRAPNgARVIDASGYTLYPGFVDA----YSNY--GVEQPGQPAP 116
Cdd:PRK07203    6 NGTAITRDPAKpvIEDGAIAIEGNVIVEIgttdELKAKYPD-AEFIDAKGKLIMPGLINShnhiYSGLarGMMANIPPPP 84
 
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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