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Conserved domains on  [gi|16132149|ref|NP_418748|]
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isoaspartyl dipeptidase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

isoaspartyl dipeptidase( domain architecture ID 10797681)

isoaspartyl dipeptidase catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 9-388 0e+00

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


:

Pssm-ID: 131030  Cd Length: 389  Bit Score: 643.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149     9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132149   320 DYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:TIGR01975 321 DGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
 
Name Accession Description Interval E-value
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 9-388 0e+00

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 643.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149     9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132149   320 DYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:TIGR01975 321 DGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 9-388 0e+00

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


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 635.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:cd01308   1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  89 LSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKC-AISD 167
Cdd:cd01308  81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEiAISD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 168 HRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARK 247
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 248 GGTIDITSSIDE------PVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDY 321
Cdd:cd01308 241 GGTIDLTSSIDPqfrkegEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149 322 DFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:cd01308 321 DIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-378 9.81e-15

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 75.00  E-value: 9.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   6 AAGFTLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEA---- 78
Cdd:COG1228   6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAvefe 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  79 --GPTTRTPEVA------LSRLTEAGVTSVVGLLGT-----DSISRHPESLLAKTRALNEE-GISawmLTGAYHVPSRti 144
Cdd:COG1228  86 agGGITPTVDLVnpadkrLRRALAAGVTTVRDLPGGplglrDAIIAGESKLLPGPRVLAAGpALS---LTGGAHARGP-- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 145 tGSVEKDV--AIIDRVIGVKcAISDHRSAAPDVYHLANMAAESRVGGLLggkpgvTVFH---MGDSKKALQ--------- 210
Cdd:COG1228 161 -EEARAALreLLAEGADYIK-VFAEGGAPDFSLEELRAILEAAHALGLP------VAAHahqADDIRLAVEagvdsiehg 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 211 -PIYD-----LLENCDVPiskLLPTHVnrnvpLFEQALEFARKGGTIDITSSIDEPVAPAegiARAVQAGIPLArvtLSS 284
Cdd:COG1228 233 tYLDDevadlLAEAGTVV---LVPTLS-----LFLALLEGAAAPVAAKARKVREAALANA---RRLHDAGVPVA---LGT 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 285 DGNGSQPffddegnlthigvAGFETLLEtVQVLVKdYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDADLLVMTPE- 362
Cdd:COG1228 299 DAGVGVP-------------PGRSLHRE-LALAVE-AGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDp 363

                       410       420
                ....*....|....*....|...
gi 16132149 363 -------LRIEQVYARGKLMVKD 378
Cdd:COG1228 364 lediaylEDVRAVMKDGRVVDRS 386
pyrC PRK09357
dihydroorotase; Validated
 10-71 1.41e-12

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 68.68  E-value: 1.41e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132149   10 TLLQGAHLYAPEDRGI-CDVLVANGKIIAVASNIPsdiVPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK09357   3 ILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIE---AEGAEVIDATGLVVAPGLVDLHVHL 62
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 59-375 9.30e-06

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: 47.11  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    59 ILCPGFIDQHVHLIGGGGEAGPTTRT--PEVALSRLTEA---GVTSVVGLLGTDSISRH-----PESLLAKTRALNEEGI 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEfaYEALRLGITTMlksGTTTVLDMGATTSTGIEalleaAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   129 SAWMLTGAYHVPSR-TITGSVEKDVAIIDRVIGVKCAISDHRSAAPD-VYHLANMAAESRVG--GLLGGKPGvTVFHM-- 202
Cdd:pfam01979  81 LDTDGELEGRKALReKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDeLKAALEEAKKYGLPvaIHALETKG-EVEDAia 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   203 --GDSKKALQPIYDLLENCDVPISKLLPTHvnrNVPL----FEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIp 276
Cdd:pfam01979 160 afGGGIEHGTHLEVAESGGLLDIIKLILAH---GVHLspteANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGV- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   277 laRVTLSSDGNGSQpffdDEGNLTHIGVAGFETlletvqVLVKDYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDAD 355
Cdd:pfam01979 236 --KVGLGTDGAGSG----NSLNMLEELRLALEL------QFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDAD 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 16132149   356 LLV-----------MTPELRIEQVYARGKLM 375
Cdd:pfam01979 304 LVVvdldplaaffgLKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 9-388 0e+00

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 643.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149     9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132149   320 DYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:TIGR01975 321 DGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 9-388 0e+00

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


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 635.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:cd01308   1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  89 LSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKC-AISD 167
Cdd:cd01308  81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEiAISD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 168 HRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARK 247
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 248 GGTIDITSSIDE------PVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDY 321
Cdd:cd01308 241 GGTIDLTSSIDPqfrkegEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149 322 DFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:cd01308 321 DIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 64-337 1.50e-17

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 82.00  E-value: 1.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  64 FIDQHVHLIGGGGE---------------AGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNE-EG 127
Cdd:cd01292   1 FIDTHVHLDGSALRgtrlnlelkeaeelsPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 128 ISAWMLTGAYHVP---SRTITGSVEKDVAIIDR--VIGVKCAISDHRSAAPDvYHLANMAAESRVGGLlggkpgVTVFHM 202
Cdd:cd01292  81 IRVVLGLGIPGVPaavDEDAEALLLELLRRGLElgAVGLKLAGPYTATGLSD-ESLRRVLEEARKLGL------PVVIHA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 203 GDSKKALQPIYDLLENCDVPiSKLLPTHVNRNVPLFEQALEFARKGGTID-ITSSIDE-PVAPAEGIARAVQAGIplaRV 280
Cdd:cd01292 154 GELPDPTRALEDLVALLRLG-GRVVIGHVSHLDPELLELLKEAGVSLEVCpLSNYLLGrDGEGAEALRRLLELGI---RV 229

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16132149 281 TLSSDGNGSQPFFDdegnlthigvagfetLLETVQVLVKD--YDFSISDALRPLTSSVA 337
Cdd:cd01292 230 TLGTDGPPHPLGTD---------------LLALLRLLLKVlrLGLSLEEALRLATINPA 273
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-378 9.81e-15

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 75.00  E-value: 9.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   6 AAGFTLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEA---- 78
Cdd:COG1228   6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAvefe 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  79 --GPTTRTPEVA------LSRLTEAGVTSVVGLLGT-----DSISRHPESLLAKTRALNEE-GISawmLTGAYHVPSRti 144
Cdd:COG1228  86 agGGITPTVDLVnpadkrLRRALAAGVTTVRDLPGGplglrDAIIAGESKLLPGPRVLAAGpALS---LTGGAHARGP-- 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 145 tGSVEKDV--AIIDRVIGVKcAISDHRSAAPDVYHLANMAAESRVGGLLggkpgvTVFH---MGDSKKALQ--------- 210
Cdd:COG1228 161 -EEARAALreLLAEGADYIK-VFAEGGAPDFSLEELRAILEAAHALGLP------VAAHahqADDIRLAVEagvdsiehg 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 211 -PIYD-----LLENCDVPiskLLPTHVnrnvpLFEQALEFARKGGTIDITSSIDEPVAPAegiARAVQAGIPLArvtLSS 284
Cdd:COG1228 233 tYLDDevadlLAEAGTVV---LVPTLS-----LFLALLEGAAAPVAAKARKVREAALANA---RRLHDAGVPVA---LGT 298

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 285 DGNGSQPffddegnlthigvAGFETLLEtVQVLVKdYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDADLLVMTPE- 362
Cdd:COG1228 299 DAGVGVP-------------PGRSLHRE-LALAVE-AGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDp 363

                       410       420
                ....*....|....*....|...
gi 16132149 363 -------LRIEQVYARGKLMVKD 378
Cdd:COG1228 364 lediaylEDVRAVMKDGRVVDRS 386
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 11-101 3.27e-14

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: 73.59  E-value: 3.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHLigggGEAGPTTR-TPEVAl 89
Cdd:COG0044   1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAP--EAAEVIDATGLLVLPGLIDLHVHL----REPGLEHKeDIETG- 73

                        90
                ....*....|....*.
gi 16132149  90 srlTEA----GVTSVV 101
Cdd:COG0044  74 ---TRAaaagGVTTVV 86
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 27-362 7.76e-13

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 69.25  E-value: 7.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  27 DVLVANGKIIAVAsniPSDIVPNCTVVDLSGQILCPGFIDQHVHliggggEAGPTTRTPEVALSrlTEAGVTSVVglLGT 106
Cdd:cd01297  21 DVGIRDGRIAAIG---PILSTSAREVIDAAGLVVAPGFIDVHTH------YDGQVFWDPDLRPS--SRQGVTTVV--LGN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 107 DSISRHP---------ESLLAKTRALNEEGISAWMLTGAYhvpsrtiTGSVEKDVAIIDRVIGV-KCAISDH-------R 169
Cdd:cd01297  88 CGVSPAPanpddlarlIMLMEGLVALGEGLPWGWATFAEY-------LDALEARPPAVNVAALVgHAALRRAvmgldarE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 170 SAAPDVYHLANMAAESRVGGLLGGKPGVTVFH-MGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKG 248
Cdd:cd01297 161 ATEEELAKMRELLREALEAGALGISTGLAYAPrLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGRET 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 249 G---TIDITSSIDEPVAPAEG-----IARAVQAGIPLaRVTLSSDGNGS------------QPFFDDEG--NLTHIGVAG 306
Cdd:cd01297 241 GrpvHISHLKSAGAPNWGKIDrllalIEAARAEGLQV-TADVYPYGAGSeddvrrimahpvVMGGSDGGalGKPHPRSYG 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149 307 FETLLETVQvlVKDYD-FSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPE 362
Cdd:cd01297 320 DFTRVLGHY--VRERKlLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDPD 374
pyrC PRK09357
dihydroorotase; Validated
 10-71 1.41e-12

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 68.68  E-value: 1.41e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132149   10 TLLQGAHLYAPEDRGI-CDVLVANGKIIAVASNIPsdiVPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK09357   3 ILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIE---AEGAEVIDATGLVVAPGLVDLHVHL 62
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
11-360 2.28e-11

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 64.80  E-value: 2.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  11 LLQGAHLYAPED--RGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGptTRTPEVA 88
Cdd:COG3964   3 LIKGGRVIDPANgiDGVMDIAIKDGKIAAVAKDIDAA--EAKKVIDASGLYVTPGLIDLHTHVFPGGTDYG--VDPDGVG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  89 LSRlteaGVTSVV--GLLGTDSISRHPESLL--AKTRALNEEGISAW-MLTGAYHVPSRTItgSVEKDVAII----DRVI 159
Cdd:COG3964  79 VRS----GVTTVVdaGSAGAANFDGFRKYVIdpSKTRVLAFLNISGIgLVGGNELQDLDDI--DPDATAAAAeanpDFIV 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 160 GVKCAISDHRSAAPD--VYHLANMAAEsrvgglLGGKPgVTVfHMGDSKKALQPIYDLLENCDVpiskllPTHVNRNVP- 236
Cdd:COG3964 153 GIKVRASKGVVGDNGiePLKRAKEAAK------EAGLP-LMV-HIGNPPPPLDEVLDLLRPGDI------LTHCFNGKPn 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 237 --------LFEQALEfARKGGTI-DI---TSSIDEPVApaegiARAVQAGI-PlarVTLSSD---GNGSQPFFDdegnLT 300
Cdd:COG3964 219 gildedgkVRPSVRE-ARKRGVLfDVghgGASFSFKVA-----EPAIAQGFlP---DTISTDlhtRNMNGPVFD----LA 285

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 301 HIgvagFETLLETvqvlvkdyDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT 360
Cdd:COG3964 286 TV----MSKFLAL--------GMPLEEVIAAVTWNPARAIGLPELGTLSVGADADITIFD 333
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
28-95 8.31e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 63.28  E-value: 8.31e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132149  28 VLVANGKIIAVASN--IPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAG----PTTRTPEVALSRLTEA 95
Cdd:COG1574  30 VAVRDGRIVAVGSDaeVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLgvdlSGARSLDELLARLRAA 103
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
11-70 3.33e-10

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 61.02  E-value: 3.33e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149   11 LLQGAHLYAPED--RGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09237   2 LLRGGRVIDPANgiDGVIDIAIEDGKIAAVAGDIDGS--QAKKVIDLSGLYVSPGWIDLHVH 61
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
11-109 4.31e-10

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 60.88  E-value: 4.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  11 LLQGAHLYAPED-RGICDVLVANGKIIAVASNIPsdivPNCTVVDLSGQILCPGFIDQHVHliGGGGEAGPTTrTPEvAL 89
Cdd:COG1820   1 AITNARIFTGDGvLEDGALLIEDGRIAAIGPGAE----PDAEVIDLGGGYLAPGFIDLHVH--GGGGVDFMDG-TPE-AL 72

                        90       100
                ....*....|....*....|....
gi 16132149  90 SRLTEA----GVTSVVGLLGTDSI 109
Cdd:COG1820  73 RTIARAharhGTTSFLPTTITAPP 96
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 27-136 5.53e-10

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 60.53  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    27 DVLVANGKIIAVASNipsDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRlteAGVTSVVGLLGT 106
Cdd:TIGR00857   7 DILVEGGRIKKIGKL---RIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAH---GGFTTVADMPNT 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 16132149   107 DSISRHPESLLAKTRALNEEGISAWMLTGA 136
Cdd:TIGR00857  81 KPPIDTPETLEWKLQRLKKVSLVDVHLYGG 110
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 10-133 2.70e-09

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


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 58.36  E-value: 2.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  10 TLLQGAHLYAPE--DRGicDVLVANGKIIAVASNIpsDIVPNCTVVDLSGQILCPGFIDQHVHliGGGGEAGP--TTRTP 85
Cdd:cd00854   1 LIIKNARILTPGglEDG--AVLVEDGKIVAIGPED--ELEEADEIIDLKGQYLVPGFIDIHIH--GGGGADFMdgTAEAL 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132149  86 EVALSRLTEAGVTSVVGLLGTDSisrhPESL---LAKTRALNEEGISAWML 133
Cdd:cd00854  75 KTIAEALAKHGTTSFLPTTVTAP----PEEIakaLAAIAEAIAEGQGAEIL 121
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 27-360 2.20e-08

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: 55.41  E-value: 2.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  27 DVLVANGKIIAVASNIPSDIvpNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGptTRTPEVALsrltEAGVTSVV--GLL 104
Cdd:cd01307   1 DVAIENGKIAAVGAALAAPA--ATQIVDAGGCYVSPGWIDLHVHVYQGGTRYG--DRPDMIGV----KSGVTTVVdaGSA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 105 GTDSI--SRHPESLLAKTRALNEEGISAWMLTGAYHVPsrtitgsvekDVAIIDRVIGVKCAisdhrSAAPDVYhlanMA 182
Cdd:cd01307  73 GADNIdgFRYTVIERSATRVYAFLNISRVGLVAQDELP----------DPDNIDEDAVVAAA-----REYPDVI----VG 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 183 AESRVGGLLGGKPGVTVFHMGdskKALQPIYDLlencdvPisklLPTHVNRNVPLFEQALEFARKGgtiDI--------- 253
Cdd:cd01307 134 LKARASKSVVGEWGIKPLELA---KKIAKEADL------P----LMVHIGSPPPILDEVVPLLRRG---DVlthcfngkp 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 254 TSSIDEPVAPAEGIARAVQAGIPL-------------ARV---------TLSSDGNGSqpffddegNLTHIGVAGFETLL 311
Cdd:cd01307 198 NGIVDEEGEVLPLVRRARERGVIFdvghgtasfsfrvARAaiaagllpdTISSDIHGR--------NRTNGPVYALATTL 269

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 16132149 312 ETVQVLvkdyDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT 360
Cdd:cd01307 270 SKLLAL----GMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFD 314
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 11-71 2.26e-08

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: 55.33  E-value: 2.26e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132149  11 LLQGAHLYApEDRGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01293   1 LLRNARLAD-GGTALVDIAIEDGRIAAIGPALAVP--PDAEEVDAKGRLVLPAFVDPHIHL 58
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 27-75 5.46e-08

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


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 54.62  E-value: 5.46e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132149  27 DVLVANGKIIAVASN--IPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGG 75
Cdd:cd01300   1 AVAVRDGRIVAVGSDaeAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGG 51
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 10-137 9.75e-08

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: 53.68  E-value: 9.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  10 TLLQGAHL--YAPEDRGI--CDVLVANGKIIAVASNI-PSDIVPNCTVVDLSGQILCPGFIDQHVH----LIGGGGEAGP 80
Cdd:COG0402   2 LLIRGAWVltMDPAGGVLedGAVLVEDGRIAAVGPGAeLPARYPAAEVIDAGGKLVLPGLVNTHTHlpqtLLRGLADDLP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149  81 -------------TTRTPE-------VALSRLTEAGVTSVVgllgtDSISRHPESLLAKTRALNEEGISAWMLTGAY 137
Cdd:COG0402  82 lldwleeyiwpleARLDPEdvyagalLALAEMLRSGTTTVA-----DFYYVHPESADALAEAAAEAGIRAVLGRGLM 153
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 10-71 1.06e-07

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: 53.38  E-value: 1.06e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149  10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01314   1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAP--GGVEVIDATGKYVLPGGIDPHTHL 60
PRK07369 PRK07369
dihydroorotase; Provisional
 10-137 1.10e-07

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 53.45  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   10 TLLQGAHLYAP---EDRgICDVLVANGKIIAVASNIPsDIVPNCTVVDLSGQILCPGFIDQHVHliggGGEAGPTTRTpe 86
Cdd:PRK07369   4 ELLQQVRVLDPvsnTDR-IADVLIEDGKIQAIEPHID-PIPPDTQIIDASGLILGPGLVDLYSH----SGEPGFEERE-- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16132149   87 vALSRLTEA----GVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAY 137
Cdd:PRK07369  76 -TLASLAAAaaagGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGAL 129
PRK08323 PRK08323
phenylhydantoinase; Validated
 10-71 1.41e-07

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 53.25  E-value: 1.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149   10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNipsdivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK08323   3 TLIKNGTVVTADDTYKADVLIEDGKIAAIGAN------LGDEVIDATGKYVMPGGIDPHTHM 58
PRK05985 PRK05985
cytosine deaminase; Provisional
 26-71 1.71e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 52.63  E-value: 1.71e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 16132149   26 CDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK05985  17 VDILIRDGRIAAIGPALAAP--PGAEVEDGGGALALPGLVDGHIHL 60
PRK08204 PRK08204
hypothetical protein; Provisional
 10-130 2.15e-07

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 52.70  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   10 TLLQGAHLY----APEDRGICDVLVANGKIIAVASNIPsdiVPNCTVVDLSGQILCPGFIDQHVH-----LIGGGGEAGP 80
Cdd:PRK08204   4 TLIRGGTVLtmdpAIGDLPRGDILIEGDRIAAVAPSIE---APDAEVVDARGMIVMPGLVDTHRHtwqsvLRGIGADWTL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149   81 TT------------RTPE--------VALSRLtEAGVTSVVgllgtD--SISRHPESLLAKTRALNEEGISA 130
Cdd:PRK08204  81 QTyfreihgnlgpmFRPEdvyianllGALEAL-DAGVTTLL-----DwsHINNSPEHADAAIRGLAEAGIRA 146
PRK09236 PRK09236
dihydroorotase; Reviewed
 26-70 5.85e-07

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 51.02  E-value: 5.85e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16132149   26 CDVLVANGKIIAVASNIPSdiVPNCTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09236  20 GDVLIENGRIAKIASSISA--KSADTVIDAAGRYLLPGMIDDQVH 62
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 10-110 7.07e-07

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 50.94  E-value: 7.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  10 TLLQGAHLY----APEDRGicDVLVANGKIIAVASNIPsdiVPNCTVVDLSGQILCPGFIDQHVHligGGGEAgptTRTP 85
Cdd:COG3653   4 LLIRGGTVVdgtgAPPFRA--DVAIKGGRIVAVGDLAA---AEAARVIDATGLVVAPGFIDIHTH---YDLQL---LWDP 72

                        90       100
                ....*....|....*....|....*
gi 16132149  86 EvALSRLTEaGVTSVVglLGTDSIS 110
Cdd:COG3653  73 R-LEPSLRQ-GVTTVV--MGNCGVS 93
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 10-71 1.46e-06

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: 49.89  E-value: 1.46e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132149  10 TLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01298   1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 50-107 1.66e-06

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: 49.60  E-value: 1.66e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132149  50 CTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE-----VALSRLT---EAGVTSVVGLLGTD 107
Cdd:cd01299   1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVeyrtiRATRQARaalRAGFTTVRDAGGAD 66
PRK09228 PRK09228
guanine deaminase; Provisional
 28-77 1.66e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 49.80  E-value: 1.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149   28 VLVANGKIIAV--ASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHL-----IGGGGE 77
Cdd:PRK09228  34 LLVEDGRIVAAgpYAELRAQLPADAEVTDYRGKLILPGFIDTHIHYpqtdmIASYGE 90
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 28-75 6.39e-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: 47.64  E-value: 6.39e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16132149  28 VLVANGKIIAV--ASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGG 75
Cdd:cd01296   1 IAIRDGRIAAVgpAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
PRK07572 PRK07572
cytosine deaminase; Validated
 11-71 7.93e-06

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 47.71  E-value: 7.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132149   11 LLQGAHLyaPEDRGICDVLVANGKIIAVASNIPSdivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07572   5 IVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQA---EAAEEIDAAGRLVSPPFVDPHFHM 60
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 59-375 9.30e-06

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: 47.11  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149    59 ILCPGFIDQHVHLIGGGGEAGPTTRT--PEVALSRLTEA---GVTSVVGLLGTDSISRH-----PESLLAKTRALNEEGI 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEfaYEALRLGITTMlksGTTTVLDMGATTSTGIEalleaAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   129 SAWMLTGAYHVPSR-TITGSVEKDVAIIDRVIGVKCAISDHRSAAPD-VYHLANMAAESRVG--GLLGGKPGvTVFHM-- 202
Cdd:pfam01979  81 LDTDGELEGRKALReKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDeLKAALEEAKKYGLPvaIHALETKG-EVEDAia 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   203 --GDSKKALQPIYDLLENCDVPISKLLPTHvnrNVPL----FEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIp 276
Cdd:pfam01979 160 afGGGIEHGTHLEVAESGGLLDIIKLILAH---GVHLspteANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGV- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   277 laRVTLSSDGNGSQpffdDEGNLTHIGVAGFETlletvqVLVKDYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDAD 355
Cdd:pfam01979 236 --KVGLGTDGAGSG----NSLNMLEELRLALEL------QFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDAD 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 16132149   356 LLV-----------MTPELRIEQVYARGKLM 375
Cdd:pfam01979 304 LVVvdldplaaffgLKPDGNVKKVIVKGKIV 334
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
27-70 1.23e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 47.02  E-value: 1.23e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 16132149  27 DVLVANGKIIAVASNIPSDIvpncTVVDLSGQILCPGFIDQHVH 70
Cdd:COG1001  26 DIAIAGGRIAGVGDYIGEAT----EVIDAAGRYLVPGFIDGHVH 65
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 28-77 1.41e-05

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 46.86  E-value: 1.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16132149    28 VLVANGKIIAV--ASNIPSDIVPNCTVVDLSGQILCPGFIDQHVH-----LIGGGGE 77
Cdd:TIGR02967   9 LVVENGRIVAVgdYAELKETLPAGVEIDDYRGHLIMPGFIDTHIHypqteMIASYGE 65
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 32-109 1.56e-05

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: 46.54  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  32 NGKIIAVASNIpsDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTR---------TPEV-----------ALSR 91
Cdd:cd01309   1 DGKIVAVGAEI--TTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSdaneetdpvTPHVraidginpddeAFKR 78

                        90
                ....*....|....*...
gi 16132149  92 LTEAGVTSVVGLLGTDSI 109
Cdd:cd01309  79 ARAGGVTTVQVLPGSANL 96
PRK09059 PRK09059
dihydroorotase; Validated
 10-109 2.04e-05

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 46.18  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   10 TLLQGAHLYAPEDR--GICDVLVANGKIIAVASNIPSDIVPNCT-VVDLSGQILCPGFIDQHVHLigggGEAGPTTRTPE 86
Cdd:PRK09059   5 ILLANARIIDPSRGldEIGTVLIEDGVIVAAGKGAGNQGAPEGAeIVDCAGKAVAPGLVDARVFV----GEPGAEHRETI 80

                         90       100
                 ....*....|....*....|....
gi 16132149   87 VALSRLTEA-GVTSVVGLLGTDSI 109
Cdd:PRK09059  81 ASASRAAAAgGVTSIIMMPDTDPV 104
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 28-76 3.03e-05

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 45.74  E-value: 3.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16132149   28 VLVANGKIIAV--ASNIPSDIvpncTVVDLSGQILCPGFIDqhVHLIGGGG 76
Cdd:PRK11170  21 VVIADGLIEAVcpVAELPPGI----EQRDLNGAILSPGFID--LQLNGCGG 65
PLN02942 PLN02942
dihydropyrimidinase
 11-71 3.27e-05

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 45.60  E-value: 3.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132149   11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIpsDIVPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PLN02942   8 LIKGGTVVNAHHQELADVYVEDGIIVAVAPNL--KVPDDVRVIDATGKFVMPGGIDPHTHL 66
PRK07575 PRK07575
dihydroorotase; Provisional
 10-119 4.61e-05

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 45.05  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   10 TLLQGAHLYAPE-DRGICDVLVANGKIIAVASNIPSDivPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:PRK07575   5 LLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISAT--AVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 16132149   89 LSRlteAGVTSVVGLLGTDSISRHPESLLAK 119
Cdd:PRK07575  83 CAK---GGVTSFLEMPNTKPLTTTQAALDDK 110
PRK02382 PRK02382
dihydroorotase; Provisional
 11-107 5.14e-05

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 45.03  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPncTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPevalS 90
Cdd:PRK02382   5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE--EVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTG----S 78

                         90
                 ....*....|....*...
gi 16132149   91 RLTEA-GVTSVVGLLGTD 107
Cdd:PRK02382  79 RSAAAgGVTTVVDQPNTD 96
PRK12394 PRK12394
metallo-dependent hydrolase;
11-101 6.48e-05

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 44.75  E-value: 6.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   11 LLQGAHLYAPE--DRGICDVLVANGKIIAvASNIPSDIVPncTVVDLSGQILCPGFIDQHVHLIGGGGEAGPttrTPEVA 88
Cdd:PRK12394   6 LITNGHIIDPArnINEINNLRIINDIIVD-ADKYPVASET--RIIHADGCIVTPGLIDYHAHVFYDGTEGGV---RPDMY 79

                         90
                 ....*....|...
gi 16132149   89 lsrLTEAGVTSVV 101
Cdd:PRK12394  80 ---MPPNGVTTVV 89
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
27-71 1.08e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 44.22  E-value: 1.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16132149   27 DVLVANGKIIAVASNIPSDIVPNctVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07228  23 DVLIEDDRIAAVGDRLDLEDYDD--HIDATGKVVIPGLIQGHIHL 65
PRK06846 PRK06846
putative deaminase; Validated
 24-71 1.72e-04

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 43.46  E-value: 1.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 16132149   24 GICDVLVANGKIIAVasnIPSDIVPNCTV--VDLSGQILCPGFIDQHVHL 71
Cdd:PRK06846  30 ALCTLEIQDGKIVAI---RPNKQVPDATLptYDANGLLMLPAFREMHIHL 76
PRK07583 PRK07583
cytosine deaminase;
27-71 2.32e-04

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 43.05  E-value: 2.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 16132149   27 DVLVANGKIIAVAsniPSDIVP-NCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07583  42 DIEIADGKIAAIL---PAGGAPdELPAVDLKGRMVWPCFVDMHTHL 84
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
327-384 3.22e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 42.78  E-value: 3.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 327 DALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT--PELRIEQVYARGKLMVKDGKACVK 384
Cdd:COG1001 288 TAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDdlEDFKVEKVYADGKLVAEDGKLLVD 347
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 27-77 3.39e-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: 42.66  E-value: 3.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132149  27 DVLVANGKIIAVASNIPSdiVPNCTVVDLSGQILCPGFIDQHVHLIGGGGE 77
Cdd:cd01315  19 DIAVKGGKIAAIGPDIAN--TEAEEVIDAGGLVVMPGLIDTHVHINEPGRT 67
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 303-362 4.13e-04

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643 [Multi-domain]  Cd Length: 361  Bit Score: 41.94  E-value: 4.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 303 GVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPE 362
Cdd:cd01318 267 GIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKNKGRIAEGYDADLTVVDLK 326
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 27-70 5.03e-04

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 42.10  E-value: 5.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 16132149   27 DVLVANGKIIAVASNI--PSDivpncTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK08393  22 DVLIEGNKIVEVKRNInkPAD-----TVIDASGSVVSPGFINAHTH 62
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 10-71 6.35e-04

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 41.61  E-value: 6.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149   10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPsdivPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK13404   6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG----PGAREIDATGRLVLPGGVDSHCHI 63
PRK07627 PRK07627
dihydroorotase; Provisional
 27-125 6.71e-04

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 41.59  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   27 DVLVANGKIIAVASnIPSDIVPNCTVvDLSGQILCPGFIDQHVHLIGGGGEAGPTTrtpEVALSRLTEAGVTSVVGLLGT 106
Cdd:PRK07627  22 DLYVAAGKIAAIGQ-APAGFNADKTI-DASGLIVCPGLVDLSARLREPGYEYKATL---ESEMAAAVAGGVTSLVCPPDT 96

                         90       100
                 ....*....|....*....|..
gi 16132149  107 DSISRHP---ESLLAKTRALNE 125
Cdd:PRK07627  97 DPVLDEPglvEMLKFRARNLNQ 118
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 52-362 7.41e-04

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 41.45  E-value: 7.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  52 VVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRlteAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAW 131
Cdd:cd01317   4 VIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAA---GGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 132 MLTGA------------------YHVPSRTITGSVEKDVAIIDRVI----GVKCAISDHrsaaPDVYHLAN--MAAESRV 187
Cdd:cd01317  81 LPIGAltkglkgeelteigelleAGAVGFSDDGKPIQDAELLRRALeyaaMLDLPIIVH----PEDPSLAGggVMNEGKV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 188 GGLLGGKpgvtvfhmGDSKKALQpiyDLLENcDVPISKLLPTHVN-------RNVPLFEQAlefarKGGTIDITSSI--- 257
Cdd:cd01317 157 ASRLGLP--------GIPPEAET---IMVAR-DLELAEATGARVHfqhlstaRSLELIRKA-----KAKGLPVTAEVtph 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149 258 ----DEP----------VAP-------AEGIARAVQAGIPlarVTLSSDgngSQPFFDDEGNL----THIGVAGFETLLE 312
Cdd:cd01317 220 hlllDDEalesydtnakVNPplrseedREALIEALKDGTI---DAIASD---HAPHTDEEKDLpfaeAPPGIIGLETALP 293

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 16132149 313 -TVQVLVKDYDFSISDALRPLTSSVAGFLNLTGkGEILPGNDADLLVMTPE 362
Cdd:cd01317 294 lLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFDPD 343
PLN02795 PLN02795
allantoinase
 28-366 1.03e-03

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 40.91  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   28 VLVANGKIIAV--ASNIPSDiVPNCTVVDLSGQILCPGFIDQHVHLIGGGGE--AGPTTRTPEVALsrlteAGVTSVVGL 103
Cdd:PLN02795  64 VEVEGGRIVSVtkEEEAPKS-QKKPHVLDYGNAVVMPGLIDVHVHLNEPGRTewEGFPTGTKAAAA-----GGITTLVDM 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  104 -LGTDSISRHPESLLAKTRALNEEgisAWMLTG--AYHVPSRTITGSVEKdvAIIDR-VIGVK---C------------- 163
Cdd:PLN02795 138 pLNSFPSTTSVETLELKIEAAKGK---LYVDVGfwGGLVPENAHNASVLE--ELLDAgALGLKsfmCpsgindfpmttat 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  164 --------------------------AISDHRSAAPDVY--HLA---------------NMAAESRVGGLLGGKPgVTVF 200
Cdd:PLN02795 213 hikaalpvlakygrpllvhaevvspvESDSRLDADPRSYstYLKsrppsweqeairqllEVAKDTRPGGVAEGAH-VHIV 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  201 HMGDSKKALQPIYDL--------LENC---------DVPISKLL-----PTHVNRNVPLFEQALefarKGGTIDITSSID 258
Cdd:PLN02795 292 HLSDAESSLELIKEAkakgdsvtVETCphylafsaeEIPDGDTRykcapPIRDAANRELLWKAL----LDGDIDMLSSDH 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  259 EPVAPAegiaravqagiplarVTLSSDGNgsqpFFDDEGnlthiGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAG 338
Cdd:PLN02795 368 SPSPPD---------------LKLLEEGN----FLRAWG-----GISSLQFVLPATWTAGRAYGLTLEQLARWWSERPAK 423

                        410       420
                 ....*....|....*....|....*...
gi 16132149  339 FLNLTGKGEILPGNDADLLVMTPELRIE 366
Cdd:PLN02795 424 LAGLDSKGAIAPGKDADIVVWDPEAEFV 451
PRK09061 PRK09061
D-glutamate deacylase; Validated
 10-70 1.06e-03

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 41.22  E-value: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132149   10 TLLQGAHLYAPEDR--GICDVLVANGKIIAVASN-IPSDivpncTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09061  21 LVIRNGRVVDPETGldAVRDVGIKGGKIAAVGTAaIEGD-----RTIDATGLVVAPGFIDLHAH 79
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 28-70 1.57e-03

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 40.34  E-value: 1.57e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 16132149  28 VLVANGKIIAV--ASNIPSDIVPNCTVVDLSGQILCPGFIDQHVH 70
Cdd:cd01303  29 IVVVDGNIIAAgaAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
PRK06189 PRK06189
allantoinase; Provisional
 11-71 1.88e-03

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 40.07  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132149   11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPnctVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK06189   6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPARE---IIDADGLYVFPGMIDVHVHF 63
Amidohydro_3 pfam07969
Amidohydrolase family;
52-75 3.11e-03

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 39.44  E-value: 3.11e-03
                          10        20
                  ....*....|....*....|....
gi 16132149    52 VVDLSGQILCPGFIDQHVHLIGGG 75
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGG 25
PRK09060 PRK09060
dihydroorotase; Validated
 10-71 4.68e-03

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 38.75  E-value: 4.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132149   10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASnipSDIVPNCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK09060   7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD---LSGASAGEVIDCRGLHVLPGVIDSQVHF 65
ureC PRK13207
urease subunit alpha; Reviewed
 24-102 6.33e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 38.62  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149   24 GI--CDVLVANGKIIAV--ASNiPsDIVPNCT--------VVDLSGQILCPGFIDQHVHLIggggeagpTTRTPEVALSr 91
Cdd:PRK13207  81 GIvkADIGIKDGRIVAIgkAGN-P-DIQDGVDiiigpgteVIAGEGLIVTAGGIDTHIHFI--------CPQQIEEALA- 149

                         90
                 ....*....|.
gi 16132149   92 lteAGVTSVVG 102
Cdd:PRK13207 150 ---SGVTTMIG 157
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 27-86 8.90e-03

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: 38.16  E-value: 8.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132149  27 DVLVANGKIIAVASNIPSDivpncTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRtPE 86
Cdd:cd01304  19 DIFIRDGKIVESSSGAKPA-----KVIDASGKVVMAGGVDMHSHIAGGKVNVGRILR-PE 72
 
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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