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Conserved domains on  [gi|446490563|ref|WP_000568417|]
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MULTISPECIES: beta-aspartyl-peptidase [Enterobacteriaceae]

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: 639.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563    9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490563  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: 639.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563    9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490563  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: 632.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:cd01308    1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  89 LSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKC-AISD 167
Cdd:cd01308   81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEiAISD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 168 HRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARK 247
Cdd:cd01308  161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 248 GGTIDITSSIDE------PVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDY 321
Cdd:cd01308  241 GGTIDLTSSIDPqfrkegEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563 322 DFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFE 388
Cdd:cd01308  321 DIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-378 1.20e-14

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 74.61  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   6 AAGFTLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEA---- 78
Cdd:COG1228    6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAvefe 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  79 --GPTTRTPEVA------LSRLTEAGVTSVVGLLGT-----DSISRHPESLLAKTRALNEE-GISawmLTGAYHVPSRti 144
Cdd:COG1228   86 agGGITPTVDLVnpadkrLRRALAAGVTTVRDLPGGplglrDAIIAGESKLLPGPRVLAAGpALS---LTGGAHARGP-- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 145 tGSVEKDV--AIIDRVIGVKcAISDHRSAAPDVYHLANMAAESRVGGLLggkpgvTVFHMGDSKKALQPV---YDLLENC 219
Cdd:COG1228  161 -EEARAALreLLAEGADYIK-VFAEGGAPDFSLEELRAILEAAHALGLP------VAAHAHQADDIRLAVeagVDSIEHG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 220 dVPISK-------------LLPTHVnrnvpLFEQALEFARKGGTIDITSSIDEPVAPAegiARAVQAGIPLArvtLSSDG 286
Cdd:COG1228  233 -TYLDDevadllaeagtvvLVPTLS-----LFLALLEGAAAPVAAKARKVREAALANA---RRLHDAGVPVA---LGTDA 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 287 NGSQPffddegnlthigvAGFETLLEtVQVLVKdYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDADLLVMTPE--- 362
Cdd:COG1228  301 GVGVP-------------PGRSLHRE-LALAVE-AGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDple 365

                        410       420
                 ....*....|....*....|.
gi 446490563 363 -----LRIEQVYARGKLMVKD 378
Cdd:COG1228  366 diaylEDVRAVMKDGRVVDRS 386
pyrC PRK09357
dihydroorotase; Validated
 10-71 8.55e-13

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 69.07  E-value: 8.55e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446490563  10 TLLQGAHLYAPEDRGI-CDVLVANGKIIAVASNIPsdiVPDCTVVDLSGQILCPGFIDQHVHL 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 4.51e-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: 48.27  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   59 ILCPGFIDQHVHLIGGGGEAGPTTRT--PEVALSRLTEA---GVTSVVGLLGTDSISRH-----PESLLAKTRALNEEGI 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEfaYEALRLGITTMlksGTTTVLDMGATTSTGIEalleaAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  129 SAWMLTGAYHVPSR-TITGSVEKDVAIIDRVIGVKCAISDHRSAAPD-VYHLANMAAESRVG--GLLGGKPGvTVFHM-- 202
Cdd:pfam01979  81 LDTDGELEGRKALReKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDeLKAALEEAKKYGLPvaIHALETKG-EVEDAia 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  203 --GDSKKALQPVYDLLENCDVPISKLLPTHvnrNVPL----FEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIp 276
Cdd:pfam01979 160 afGGGIEHGTHLEVAESGGLLDIIKLILAH---GVHLspteANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGV- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  277 laRVTLSSDGNGSQpffdDEGNLTHIGVAGFETlletvqVLVKDYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDAD 355
Cdd:pfam01979 236 --KVGLGTDGAGSG----NSLNMLEELRLALEL------QFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDAD 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 446490563  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: 639.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563    9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPS--DIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE 86
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   87 VALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGV-KCAI 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  166 SDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  246 RKGGTIDITSSIDEP------VAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVK 319
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQfrkegeVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446490563  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: 632.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   9 FTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:cd01308    1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  89 LSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKC-AISD 167
Cdd:cd01308   81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEiAISD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 168 HRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARK 247
Cdd:cd01308  161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 248 GGTIDITSSIDE------PVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDY 321
Cdd:cd01308  241 GGTIDLTSSIDPqfrkegEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563 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 2.60e-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: 81.23  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  64 FIDQHVHLIGGGGE---------------AGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNE-EG 127
Cdd:cd01292    1 FIDTHVHLDGSALRgtrlnlelkeaeelsPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 128 ISAWMLTGAYHVP---SRTITGSVEKDVAIIDR--VIGVKCAISDHRSAAPDvYHLANMAAESRVGGLlggkpgVTVFHM 202
Cdd:cd01292   81 IRVVLGLGIPGVPaavDEDAEALLLELLRRGLElgAVGLKLAGPYTATGLSD-ESLRRVLEEARKLGL------PVVIHA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 203 GDSKKALQPVYDLLENCDVPiSKLLPTHVNRNVPLFEQALEFARKGGTID-ITSSIDE-PVAPAEGIARAVQAGIplaRV 280
Cdd:cd01292  154 GELPDPTRALEDLVALLRLG-GRVVIGHVSHLDPELLELLKEAGVSLEVCpLSNYLLGrDGEGAEALRRLLELGI---RV 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446490563 281 TLSSDGNGSQPFFDdegnlthigvagfetLLETVQVLVKD--YDFSISDALRPLTSSVA 337
Cdd:cd01292  230 TLGTDGPPHPLGTD---------------LLALLRLLLKVlrLGLSLEEALRLATINPA 273
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 6-378 1.20e-14

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 74.61  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   6 AAGFTLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEA---- 78
Cdd:COG1228    6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAvefe 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  79 --GPTTRTPEVA------LSRLTEAGVTSVVGLLGT-----DSISRHPESLLAKTRALNEE-GISawmLTGAYHVPSRti 144
Cdd:COG1228   86 agGGITPTVDLVnpadkrLRRALAAGVTTVRDLPGGplglrDAIIAGESKLLPGPRVLAAGpALS---LTGGAHARGP-- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 145 tGSVEKDV--AIIDRVIGVKcAISDHRSAAPDVYHLANMAAESRVGGLLggkpgvTVFHMGDSKKALQPV---YDLLENC 219
Cdd:COG1228  161 -EEARAALreLLAEGADYIK-VFAEGGAPDFSLEELRAILEAAHALGLP------VAAHAHQADDIRLAVeagVDSIEHG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 220 dVPISK-------------LLPTHVnrnvpLFEQALEFARKGGTIDITSSIDEPVAPAegiARAVQAGIPLArvtLSSDG 286
Cdd:COG1228  233 -TYLDDevadllaeagtvvLVPTLS-----LFLALLEGAAAPVAAKARKVREAALANA---RRLHDAGVPVA---LGTDA 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 287 NGSQPffddegnlthigvAGFETLLEtVQVLVKdYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDADLLVMTPE--- 362
Cdd:COG1228  301 GVGVP-------------PGRSLHRE-LALAVE-AGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDple 365

                        410       420
                 ....*....|....*....|.
gi 446490563 363 -----LRIEQVYARGKLMVKD 378
Cdd:COG1228  366 diaylEDVRAVMKDGRVVDRS 386
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 11-101 2.22e-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: 73.97  E-value: 2.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHLigggGEAGPTTR-TPEVAl 89
Cdd:COG0044    1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAP--EAAEVIDATGLLVLPGLIDLHVHL----REPGLEHKeDIETG- 73

                         90
                 ....*....|....*.
gi 446490563  90 srlTEA----GVTSVV 101
Cdd:COG0044   74 ---TRAaaagGVTTVV 86
pyrC PRK09357
dihydroorotase; Validated
 10-71 8.55e-13

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 69.07  E-value: 8.55e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446490563  10 TLLQGAHLYAPEDRGI-CDVLVANGKIIAVASNIPsdiVPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK09357   3 ILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIE---AEGAEVIDATGLVVAPGLVDLHVHL 62
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 27-362 1.82e-12

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: 68.09  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  27 DVLVANGKIIAVAsniPSDIVPDCTVVDLSGQILCPGFIDQHVHliggggEAGPTTRTPEVALSrlTEAGVTSVVglLGT 106
Cdd:cd01297   21 DVGIRDGRIAAIG---PILSTSAREVIDAAGLVVAPGFIDVHTH------YDGQVFWDPDLRPS--SRQGVTTVV--LGN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 107 DSISRHP---------ESLLAKTRALNEEGISAWMLTGAYhvpsrtiTGSVEKDVAIIDRVIGV-KCAISDH-------R 169
Cdd:cd01297   88 CGVSPAPanpddlarlIMLMEGLVALGEGLPWGWATFAEY-------LDALEARPPAVNVAALVgHAALRRAvmgldarE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 170 SAAPDVYHLANMAAESRVGGLLGGKPGVTVFH-MGDSKKALQPVYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKG 248
Cdd:cd01297  161 ATEEELAKMRELLREALEAGALGISTGLAYAPrLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGRET 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 249 G---TIDITSSIDEPVAPAEG-----IARAVQAGIPLaRVTLSSDGNGS------------QPFFDDEG--NLTHIGVAG 306
Cdd:cd01297  241 GrpvHISHLKSAGAPNWGKIDrllalIEAARAEGLQV-TADVYPYGAGSeddvrrimahpvVMGGSDGGalGKPHPRSYG 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563 307 FETLLETVQvlVKDYD-FSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPE 362
Cdd:cd01297  320 DFTRVLGHY--VRERKlLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFDPD 374
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
11-360 3.45e-11

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 64.03  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  11 LLQGAHLYAPED--RGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGptTRTPEVA 88
Cdd:COG3964    3 LIKGGRVIDPANgiDGVMDIAIKDGKIAAVAKDIDAA--EAKKVIDASGLYVTPGLIDLHTHVFPGGTDYG--VDPDGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  89 LSRlteaGVTSVV--GLLGTDSISRHPESLL--AKTRALNEEGISAW-MLTGAYHVPSRTItgSVEKDVAII----DRVI 159
Cdd:COG3964   79 VRS----GVTTVVdaGSAGAANFDGFRKYVIdpSKTRVLAFLNISGIgLVGGNELQDLDDI--DPDATAAAAeanpDFIV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 160 GVKCAISDHRSAAPD--VYHLANMAAEsrvgglLGGKPgVTVfHMGDSKKALQPVYDLLENCDVpiskllPTHVNRNVP- 236
Cdd:COG3964  153 GIKVRASKGVVGDNGiePLKRAKEAAK------EAGLP-LMV-HIGNPPPPLDEVLDLLRPGDI------LTHCFNGKPn 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 237 --------LFEQALEfARKGGTI-DI---TSSIDEPVApaegiARAVQAGI-PlarVTLSSD---GNGSQPFFDdegnLT 300
Cdd:COG3964  219 gildedgkVRPSVRE-ARKRGVLfDVghgGASFSFKVA-----EPAIAQGFlP---DTISTDlhtRNMNGPVFD----LA 285

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 301 HIgvagFETLLETvqvlvkdyDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT 360
Cdd:COG3964  286 TV----MSKFLAL--------GMPLEEVIAAVTWNPARAIGLPELGTLSVGADADITIFD 333
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
28-95 6.36e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 63.66  E-value: 6.36e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446490563  28 VLVANGKIIAVASN--IPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAG----PTTRTPEVALSRLTEA 95
Cdd:COG1574   30 VAVRDGRIVAVGSDaeVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLgvdlSGARSLDELLARLRAA 103
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
11-70 1.20e-10

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 62.56  E-value: 1.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  11 LLQGAHLYAPED--RGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09237   2 LLRGGRVIDPANgiDGVIDIAIEDGKIAAVAGDIDGS--QAKKVIDLSGLYVSPGWIDLHVH 61
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
11-109 2.23e-10

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 61.65  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  11 LLQGAHLYAPED-RGICDVLVANGKIIAVASNIPsdivPDCTVVDLSGQILCPGFIDQHVHliGGGGEAGPTTrTPEvAL 89
Cdd:COG1820    1 AITNARIFTGDGvLEDGALLIEDGRIAAIGPGAE----PDAEVIDLGGGYLAPGFIDLHVH--GGGGVDFMDG-TPE-AL 72

                         90       100
                 ....*....|....*....|....
gi 446490563  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 2.26e-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: 61.69  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   27 DVLVANGKIIAVASNipsDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRlteAGVTSVVGLLGT 106
Cdd:TIGR00857   7 DILVEGGRIKKIGKL---RIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAH---GGFTTVADMPNT 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 446490563  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 1.20e-09

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


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 59.51  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLYAPE--DRGicDVLVANGKIIAVASNIpsDIVPDCTVVDLSGQILCPGFIDQHVHliGGGGEAGP--TTRTP 85
Cdd:cd00854    1 LIIKNARILTPGglEDG--AVLVEDGKIVAIGPED--ELEEADEIIDLKGQYLVPGFIDIHIH--GGGGADFMdgTAEAL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446490563  86 EVALSRLTEAGVTSVVGLLGTDSisrhPESL---LAKTRALNEEGISAWML 133
Cdd:cd00854   75 KTIAEALAKHGTTSFLPTTVTAP----PEEIakaLAAIAEAIAEGQGAEIL 121
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 11-71 1.58e-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: 56.10  E-value: 1.58e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446490563  11 LLQGAHLYApEDRGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01293    1 LLRNARLAD-GGTALVDIAIEDGRIAAIGPALAVP--PDAEEVDAKGRLVLPAFVDPHIHL 58
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 27-360 1.76e-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: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  27 DVLVANGKIIAVASNIPSDIvpDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGptTRTPEVALsrltEAGVTSVV--GLL 104
Cdd:cd01307    1 DVAIENGKIAAVGAALAAPA--ATQIVDAGGCYVSPGWIDLHVHVYQGGTRYG--DRPDMIGV----KSGVTTVVdaGSA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 105 GTDSI--SRHPESLLAKTRALNEEGISAWMLTGAYHVPsrtitgsvekDVAIIDRVIGVKCAisdhrSAAPDVYhlanMA 182
Cdd:cd01307   73 GADNIdgFRYTVIERSATRVYAFLNISRVGLVAQDELP----------DPDNIDEDAVVAAA-----REYPDVI----VG 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 183 AESRVGGLLGGKPGVTVFHMGD--SKKALQPVYdllencdvpiskllpTHVNRNVPLFEQALEFARKGgtiDI------- 253
Cdd:cd01307  134 LKARASKSVVGEWGIKPLELAKkiAKEADLPLM---------------VHIGSPPPILDEVVPLLRRG---DVlthcfng 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 254 --TSSIDEPVAPAEGIARAVQAGIPL-------------ARV---------TLSSDGNGSqpffddegNLTHIGVAGFET 309
Cdd:cd01307  196 kpNGIVDEEGEVLPLVRRARERGVIFdvghgtasfsfrvARAaiaagllpdTISSDIHGR--------NRTNGPVYALAT 267

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446490563 310 LLETVQVLvkdyDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT 360
Cdd:cd01307  268 TLSKLLAL----GMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFD 314
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 27-283 2.99e-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: 55.39  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  27 DVLVANGKIIAVASN--IPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGgeagpttrtpeVALSRLTEAGVTSVVGLL 104
Cdd:cd01300    1 AVAVRDGRIVAVGSDaeAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGG-----------LSLLWLDLSGVTSKEEAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 105 gtdsisrhpeSLLAKTRALNEEGisAWMLTGAYHvPSRtITGSVEKDVAIIDRVIGVKCAISDHRSaapdvYH--LANMA 182
Cdd:cd01300   70 ----------ARIREDAAAAPPG--EWILGFGWD-ESL-LGEGRYPTRAELDAVSPDRPVLLLRRD-----GHsaWVNSA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 183 AeSRVGGLLGGKPGVTVFHMGDsKKALQPVYDLLEN-CDVPISKLLPTHVNRNVPLFEQALEFARKGGtidITSSIDEPV 261
Cdd:cd01300  131 A-LRLAGITRDTPDPPGGEIVR-DADGEPTGVLVEAaAALVLEAVPPPTPEERRAALRAAARELASLG---VTTVHDAGG 205

                        250       260
                 ....*....|....*....|....*
gi 446490563 262 APAEGIA---RAVQAGIPLARVTLS 283
Cdd:cd01300  206 GAADDIEayrRLAAAGELTLRVRVA 230
PRK08204 PRK08204
hypothetical protein; Provisional
 10-130 3.53e-08

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 55.01  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLY----APEDRGICDVLVANGKIIAVASNIPsdiVPDCTVVDLSGQILCPGFIDQHVH-----LIGGGGEAGP 80
Cdd:PRK08204   4 TLIRGGTVLtmdpAIGDLPRGDILIEGDRIAAVAPSIE---APDAEVVDARGMIVMPGLVDTHRHtwqsvLRGIGADWTL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  81 TT------------RTPE--------VALSRLtEAGVTSVVgllgtD--SISRHPESLLAKTRALNEEGISA 130
Cdd:PRK08204  81 QTyfreihgnlgpmFRPEdvyianllGALEAL-DAGVTTLL-----DwsHINNSPEHADAAIRGLAEAGIRA 146
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 10-137 4.67e-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: 54.45  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHL--YAPEDRGI--CDVLVANGKIIAVASNI-PSDIVPDCTVVDLSGQILCPGFIDQHVH----LIGGGGEAGP 80
Cdd:COG0402    2 LLIRGAWVltMDPAGGVLedGAVLVEDGRIAAVGPGAeLPARYPAAEVIDAGGKLVLPGLVNTHTHlpqtLLRGLADDLP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563  81 -------------TTRTPE-------VALSRLTEAGVTSVVgllgtDSISRHPESLLAKTRALNEEGISAWMLTGAY 137
Cdd:COG0402   82 lldwleeyiwpleARLDPEdvyagalLALAEMLRSGTTTVA-----DFYYVHPESADALAEAAAEAGIRAVLGRGLM 153
PRK07369 PRK07369
dihydroorotase; Provisional
 10-137 5.88e-08

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 54.22  E-value: 5.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLYAP---EDRgICDVLVANGKIIAVASNIPsDIVPDCTVVDLSGQILCPGFIDQHVHliggGGEAGPTTRTpe 86
Cdd:PRK07369   4 ELLQQVRVLDPvsnTDR-IADVLIEDGKIQAIEPHID-PIPPDTQIIDASGLILGPGLVDLYSH----SGEPGFEERE-- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446490563  87 vALSRLTEA----GVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAY 137
Cdd:PRK07369  76 -TLASLAAAaaagGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGAL 129
PRK08323 PRK08323
phenylhydantoinase; Validated
 10-71 1.30e-07

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 53.25  E-value: 1.30e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNipsdivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK08323   3 TLIKNGTVVTADDTYKADVLIEDGKIAAIGAN------LGDEVIDATGKYVMPGGIDPHTHM 58
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 10-71 1.49e-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: 52.99  E-value: 1.49e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01314    1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAP--GGVEVIDATGKYVLPGGIDPHTHL 60
PRK05985 PRK05985
cytosine deaminase; Provisional
 26-71 1.55e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 53.01  E-value: 1.55e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446490563  26 CDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK05985  17 VDILIRDGRIAAIGPALAAP--PGAEVEDGGGALALPGLVDGHIHL 60
PRK09228 PRK09228
guanine deaminase; Provisional
 28-77 5.31e-07

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 51.34  E-value: 5.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563  28 VLVANGKIIAV--ASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHL-----IGGGGE 77
Cdd:PRK09228  34 LLVEDGRIVAAgpYAELRAQLPADAEVTDYRGKLILPGFIDTHIHYpqtdmIASYGE 90
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 10-110 6.95e-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: 6.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLY----APEDRGicDVLVANGKIIAVASNIPsdiVPDCTVVDLSGQILCPGFIDQHVHligGGGEAgptTRTP 85
Cdd:COG3653    4 LLIRGGTVVdgtgAPPFRA--DVAIKGGRIVAVGDLAA---AEAARVIDATGLVVAPGFIDIHTH---YDLQL---LWDP 72

                         90       100
                 ....*....|....*....|....*
gi 446490563  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 1.12e-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: 50.28  E-value: 1.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446490563  10 TLLQGAHLYAPEDRGI---CDVLVANGKIIAVASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:cd01298    1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
PRK09236 PRK09236
dihydroorotase; Reviewed
 26-70 1.13e-06

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 50.25  E-value: 1.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446490563  26 CDVLVANGKIIAVASNIPSdiVPDCTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09236  20 GDVLIENGRIAKIASSISA--KSADTVIDAAGRYLLPGMIDDQVH 62
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 50-107 1.83e-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: 49.21  E-value: 1.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446490563  50 CTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPE-----VALSRLT---EAGVTSVVGLLGTD 107
Cdd:cd01299    1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVeyrtiRATRQARaalRAGFTTVRDAGGAD 66
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 59-375 4.51e-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: 48.27  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563   59 ILCPGFIDQHVHLIGGGGEAGPTTRT--PEVALSRLTEA---GVTSVVGLLGTDSISRH-----PESLLAKTRALNEEGI 128
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEfaYEALRLGITTMlksGTTTVLDMGATTSTGIEalleaAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  129 SAWMLTGAYHVPSR-TITGSVEKDVAIIDRVIGVKCAISDHRSAAPD-VYHLANMAAESRVG--GLLGGKPGvTVFHM-- 202
Cdd:pfam01979  81 LDTDGELEGRKALReKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDeLKAALEEAKKYGLPvaIHALETKG-EVEDAia 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  203 --GDSKKALQPVYDLLENCDVPISKLLPTHvnrNVPL----FEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIp 276
Cdd:pfam01979 160 afGGGIEHGTHLEVAESGGLLDIIKLILAH---GVHLspteANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGV- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  277 laRVTLSSDGNGSQpffdDEGNLTHIGVAGFETlletvqVLVKDYDFSISDALRPLTSSVAGFLNLTGK-GEILPGNDAD 355
Cdd:pfam01979 236 --KVGLGTDGAGSG----NSLNMLEELRLALEL------QFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDAD 303

                         330       340       350
                  ....*....|....*....|....*....|.
gi 446490563  356 LLV-----------MTPELRIEQVYARGKLM 375
Cdd:pfam01979 304 LVVvdldplaaffgLKPDGNVKKVIVKGKIV 334
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 32-109 4.62e-06

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: 48.08  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  32 NGKIIAVASNIpsDIVPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTR---------TPEV-----------ALSR 91
Cdd:cd01309    1 DGKIVAVGAEI--TTPADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSdaneetdpvTPHVraidginpddeAFKR 78

                         90
                 ....*....|....*...
gi 446490563  92 LTEAGVTSVVGLLGTDSI 109
Cdd:cd01309   79 ARAGGVTTVQVLPGSANL 96
PRK09059 PRK09059
dihydroorotase; Validated
 10-109 5.83e-06

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 48.11  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLYAPEDR--GICDVLVANGKIIAVASNIPSDIVPDCT-VVDLSGQILCPGFIDQHVHLigggGEAGPTTRTPE 86
Cdd:PRK09059   5 ILLANARIIDPSRGldEIGTVLIEDGVIVAAGKGAGNQGAPEGAeIVDCAGKAVAPGLVDARVFV----GEPGAEHRETI 80

                         90       100
                 ....*....|....*....|....
gi 446490563  87 VALSRLTEA-GVTSVVGLLGTDSI 109
Cdd:PRK09059  81 ASASRAAAAgGVTSIIMMPDTDPV 104
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 28-77 5.91e-06

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: 48.02  E-value: 5.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446490563   28 VLVANGKIIAV--ASNIPSDIVPDCTVVDLSGQILCPGFIDQHVH-----LIGGGGE 77
Cdd:TIGR02967   9 LVVENGRIVAVgdYAELKETLPAGVEIDDYRGHLIMPGFIDTHIHypqteMIASYGE 65
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 28-75 7.37e-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: 7.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446490563  28 VLVANGKIIAV--ASNIPSDIVPDCTVVDLSGQILCPGFIDQHVHLIGGG 75
Cdd:cd01296    1 IAIRDGRIAAVgpAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
PRK07572 PRK07572
cytosine deaminase; Validated
 11-71 9.05e-06

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 47.32  E-value: 9.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446490563  11 LLQGAHLyaPEDRGICDVLVANGKIIAVASNIPSdivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07572   5 IVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQA---EAAEEIDAAGRLVSPPFVDPHFHM 60
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
27-70 1.33e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 47.02  E-value: 1.33e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446490563  27 DVLVANGKIIAVASNIPSDIvpdcTVVDLSGQILCPGFIDQHVH 70
Cdd:COG1001   26 DIAIAGGRIAGVGDYIGEAT----EVIDAAGRYLVPGFIDGHVH 65
PLN02942 PLN02942
dihydropyrimidinase
 11-71 1.42e-05

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 46.76  E-value: 1.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446490563  11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIpsDIVPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PLN02942   8 LIKGGTVVNAHHQELADVYVEDGIIVAVAPNL--KVPDDVRVIDATGKFVMPGGIDPHTHL 66
PRK07575 PRK07575
dihydroorotase; Provisional
 10-119 2.79e-05

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 45.82  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  10 TLLQGAHLYAPE-DRGICDVLVANGKIIAVASNIPSDivPDCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVA 88
Cdd:PRK07575   5 LLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISAT--AVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRA 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446490563  89 LSRlteAGVTSVVGLLGTDSISRHPESLLAK 119
Cdd:PRK07575  83 CAK---GGVTSFLEMPNTKPLTTTQAALDDK 110
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 28-76 2.85e-05

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 45.74  E-value: 2.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446490563  28 VLVANGKIIAV--ASNIPSDIvpdcTVVDLSGQILCPGFIDqhVHLIGGGG 76
Cdd:PRK11170  21 VVIADGLIEAVcpVAELPPGI----EQRDLNGAILSPGFID--LQLNGCGG 65
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
27-71 4.03e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 45.38  E-value: 4.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446490563  27 DVLVANGKIIAVASNIPSDIVPDctVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07228  23 DVLIEDDRIAAVGDRLDLEDYDD--HIDATGKVVIPGLIQGHIHL 65
PRK02382 PRK02382
dihydroorotase; Provisional
 11-107 5.52e-05

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 45.03  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPDctVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPevalS 90
Cdd:PRK02382   5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEE--VIDARGMLLLPGGIDVHVHFREPGYTHKETWYTG----S 78

                         90
                 ....*....|....*...
gi 446490563  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 446490563  11 LLQGAHLYAPE--DRGICDVLVANGKIIAvASNIPSDIVPdcTVVDLSGQILCPGFIDQHVHLIGGGGEAGPttrTPEVA 88
Cdd:PRK12394   6 LITNGHIIDPArnINEINNLRIINDIIVD-ADKYPVASET--RIIHADGCIVTPGLIDYHAHVFYDGTEGGV---RPDMY 79

                         90
                 ....*....|...
gi 446490563  89 lsrLTEAGVTSVV 101
Cdd:PRK12394  80 ---MPPNGVTTVV 89
PRK06846 PRK06846
putative deaminase; Validated
 24-71 9.18e-05

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 44.23  E-value: 9.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446490563  24 GICDVLVANGKIIAVasnIPSDIVPDCTV--VDLSGQILCPGFIDQHVHL 71
Cdd:PRK06846  30 ALCTLEIQDGKIVAI---RPNKQVPDATLptYDANGLLMLPAFREMHIHL 76
PRK07583 PRK07583
cytosine deaminase;
27-71 1.01e-04

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 44.20  E-value: 1.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446490563  27 DVLVANGKIIAVAsniPSDIVPDCT-VVDLSGQILCPGFIDQHVHL 71
Cdd:PRK07583  42 DIEIADGKIAAIL---PAGGAPDELpAVDLKGRMVWPCFVDMHTHL 84
PRK09061 PRK09061
D-glutamate deacylase; Validated
 10-70 3.16e-04

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 42.76  E-value: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446490563  10 TLLQGAHLYAPEDR--GICDVLVANGKIIAVASNIpsdIVPDcTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK09061  21 LVIRNGRVVDPETGldAVRDVGIKGGKIAAVGTAA---IEGD-RTIDATGLVVAPGFIDLHAH 79
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
327-384 3.37e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 42.78  E-value: 3.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 327 DALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT--PELRIEQVYARGKLMVKDGKACVK 384
Cdd:COG1001  288 TAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDdlEDFKVEKVYADGKLVAEDGKLLVD 347
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 28-70 3.53e-04

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: 42.26  E-value: 3.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446490563  28 VLVANGKIIAV--ASNIPSDIVPDCTVVDLSGQILCPGFIDQHVH 70
Cdd:cd01303   29 IVVVDGNIIAAgaAETLKRAAKPGARVIDSPNQFILPGFIDTHIH 73
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 27-77 4.15e-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: 42.28  E-value: 4.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446490563  27 DVLVANGKIIAVASNIPSdiVPDCTVVDLSGQILCPGFIDQHVHLIGGGGE 77
Cdd:cd01315   19 DIAVKGGKIAAIGPDIAN--TEAEEVIDAGGLVVMPGLIDTHVHINEPGRT 67
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 303-362 4.20e-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: 4.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 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 446490563  27 DVLVANGKIIAVASNI--PSDivpdcTVVDLSGQILCPGFIDQHVH 70
Cdd:PRK08393  22 DVLIEGNKIVEVKRNInkPAD-----TVIDASGSVVSPGFINAHTH 62
PRK07627 PRK07627
dihydroorotase; Provisional
 27-125 5.34e-04

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 41.97  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  27 DVLVANGKIIAVASnIPSDIVPDCTVvDLSGQILCPGFIDQHVHLIGGGGEAGPTTrtpEVALSRLTEAGVTSVVGLLGT 106
Cdd:PRK07627  22 DLYVAAGKIAAIGQ-APAGFNADKTI-DASGLIVCPGLVDLSARLREPGYEYKATL---ESEMAAAVAGGVTSLVCPPDT 96

                         90       100
                 ....*....|....*....|..
gi 446490563 107 DSISRHP---ESLLAKTRALNE 125
Cdd:PRK07627  97 DPVLDEPglvEMLKFRARNLNQ 118
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 52-362 7.88e-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: 41.07  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  52 VVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRlteAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAW 131
Cdd:cd01317    4 VIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAA---GGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 132 MLTGA------------------YHVPSRTITGSVEKDVAIIDRVI----GVKCAISDHrsaaPDVYHLAN--MAAESRV 187
Cdd:cd01317   81 LPIGAltkglkgeelteigelleAGAVGFSDDGKPIQDAELLRRALeyaaMLDLPIIVH----PEDPSLAGggVMNEGKV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 188 GGLLGGKpgvtvfhmGDSKKALQpvyDLLENcDVPISKLLPTHVN-------RNVPLFEQAlefarKGGTIDITSSI--- 257
Cdd:cd01317  157 ASRLGLP--------GIPPEAET---IMVAR-DLELAEATGARVHfqhlstaRSLELIRKA-----KAKGLPVTAEVtph 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563 258 ----DEP----------VAP-------AEGIARAVQAGIPlarVTLSSDgngSQPFFDDEGNL----THIGVAGFETLLE 312
Cdd:cd01317  220 hlllDDEalesydtnakVNPplrseedREALIEALKDGTI---DAIASD---HAPHTDEEKDLpfaeAPPGIIGLETALP 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446490563 313 -TVQVLVKDYDFSISDALRPLTSSVAGFLNLTGkGEILPGNDADLLVMTPE 362
Cdd:cd01317  294 lLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFDPD 343
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 10-71 8.25e-04

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 41.22  E-value: 8.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPsdivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK13404   6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG----PGAREIDATGRLVLPGGVDSHCHI 63
PRK06189 PRK06189
allantoinase; Provisional
 11-71 1.02e-03

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 40.84  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446490563  11 LLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSdivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK06189   6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISS---PAREIIDADGLYVFPGMIDVHVHF 63
Amidohydro_3 pfam07969
Amidohydrolase family;
52-75 3.27e-03

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 39.44  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|....
gi 446490563   52 VVDLSGQILCPGFIDQHVHLIGGG 75
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGG 25
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
 27-71 5.31e-03

adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130246 [Multi-domain]  Cd Length: 552  Bit Score: 38.99  E-value: 5.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446490563   27 DVLVANGKIIAVASNipsdivPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:TIGR01178  21 DIAIANGHIAGVGKY------NGVKVIDALGEYAVPGFIDAHIHI 59
PRK09060 PRK09060
dihydroorotase; Validated
 10-71 5.39e-03

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 38.75  E-value: 5.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446490563  10 TLLQGAHLYAPEDRGICDVLVANGKIIAVASnipSDIVPDCTVVDLSGQILCPGFIDQHVHL 71
Cdd:PRK09060   7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD---LSGASAGEVIDCRGLHVLPGVIDSQVHF 65
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 27-86 9.14e-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: 9.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446490563  27 DVLVANGKIIAVASNIPSDivpdcTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRtPE 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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