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Conserved domains on  [gi|501408044|ref|WP_012439610|]
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amidohydrolase [Xanthomonas campestris]

Protein Classification

amidohydrolase family protein( domain architecture ID 10007618)

amidohydrolase family protein similar to 2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase which catalyzes the hydrolysis of PDC to oxalomesaconic acid (OMA), and to Agrobacterium fabrum D-galactarolactone isomerase which catalyzes the isomerization of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone

CATH:  3.20.20.140
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016787
PubMed:  9144792
SCOP:  3000428

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
3-278 7.61e-71

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


:

Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 219.70  E-value: 7.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044   3 RVDAHLHFWHLGRGDYDWLtPELSALYRDFGPDDVSAALDAADVDSVVVVQAAATEAETCYLFELARDTPRIAGVVGWVD 82
Cdd:COG3618    2 IIDAHHHVWDPDRGRYPWL-PDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  83 FAAPDAPARIGALVRAGgglLKGLRPMVQDIADvQWLASPALDAAFDALIAHDLAFDALIRAAHVPALQARLQRHPGLRV 162
Cdd:COG3618   81 LDAPDAAAELARLAAAG---VRGVRFNLQGEPD-GWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 163 VVDHGGKPAIAAGEFvAWAAGIAALAQHPGVHCKLSGLLTEAARGATAQTLEPYVAHLFARFGAQRVLWGSDWPVLTQRA 242
Cdd:COG3618  157 VIDHLGKPDIAAGDD-PWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 501408044 243 DYAQWLQIAQQLVQQYADGHAAAVFGDNARTFYRLP 278
Cdd:COG3618  236 DYGELLDLLEELLPDLSEAERRAILGDNAARLYGLA 271
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
3-278 7.61e-71

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 219.70  E-value: 7.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044   3 RVDAHLHFWHLGRGDYDWLtPELSALYRDFGPDDVSAALDAADVDSVVVVQAAATEAETCYLFELARDTPRIAGVVGWVD 82
Cdd:COG3618    2 IIDAHHHVWDPDRGRYPWL-PDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  83 FAAPDAPARIGALVRAGgglLKGLRPMVQDIADvQWLASPALDAAFDALIAHDLAFDALIRAAHVPALQARLQRHPGLRV 162
Cdd:COG3618   81 LDAPDAAAELARLAAAG---VRGVRFNLQGEPD-GWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 163 VVDHGGKPAIAAGEFvAWAAGIAALAQHPGVHCKLSGLLTEAARGATAQTLEPYVAHLFARFGAQRVLWGSDWPVLTQRA 242
Cdd:COG3618  157 VIDHLGKPDIAAGDD-PWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 501408044 243 DYAQWLQIAQQLVQQYADGHAAAVFGDNARTFYRLP 278
Cdd:COG3618  236 DYGELLDLLEELLPDLSEAERRAILGDNAARLYGLA 271
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
4-277 1.75e-35

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 128.80  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044    4 VDAHLHFWHLGRGDYDW------LTPELSALYRDFGPDDVSAALDAADVDSVVVVQAAATEAETCYLFELARDTPRIAGV 77
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDpggrlpFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044   78 VGWVDFAAPDAPARIGALVRAGGglLKGLRPMVQDIADVqWLASPALDAAFDALIAHDLAFDALI---------RAAHVP 148
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEAG--FRGVRLNPHPGGDP-LLGDRLDRPIYEALEELGLPVDIHTgfgdrpedtRAIQPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  149 ALQARLQRHPGLRVVVDHGGKPAIAagEFVAWAAGIAALAQHPGVHCKLSGLLTeAARGATAQTLEPYVAHLFARFGAQR 228
Cdd:pfam04909 158 LLAGVARKFPDLKIVLDHGGGPWIP--EGLDDPAALALLARRPNVYVKLSGLYR-DLYFDAPLADRPYLARLLEAFGPDR 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 501408044  229 VLWGSDWPVLTQRADYAQWLQIAQQLVQQYADGHAAAVFGDNARTFYRL 277
Cdd:pfam04909 235 ILFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
138-236 7.84e-06

2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid (OMA) or its tautomer, 4-carboxy-2-hydroxymuconic acid (CHM). This reaction is part of the protocatechuate (PCA) 4,5-cleavage pathway. PCA is one of the most important intermediate metabolites in the bacterial pathways for various phenolic compounds, including lignin, which is the most abundant aromatic material in nature.


Pssm-ID: 238636  Cd Length: 263  Bit Score: 46.28  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 138 FDALIRAAHVPALQARlqrhpGLRVVVDHGGKPAIAAGEFVAWAAGIAALAQHPGVHCKLSGLLTEAARGATAQTLEPyV 217
Cdd:cd01311  130 FDAVDLPALLPFLQKL-----PVAVVIDHFGRPDVTKGVDGAEFAALLKLIEEGNVWVKVSGPYRLSVKQEAYADVIA-F 203
                         90
                 ....*....|....*....
gi 501408044 218 AHLFARFGAQRVLWGSDWP 236
Cdd:cd01311  204 ARQIVAAAPDRLVWGTDWP 222
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
3-278 7.61e-71

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 219.70  E-value: 7.61e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044   3 RVDAHLHFWHLGRGDYDWLtPELSALYRDFGPDDVSAALDAADVDSVVVVQAAATEAETCYLFELARDTPRIAGVVGWVD 82
Cdd:COG3618    2 IIDAHHHVWDPDRGRYPWL-PDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  83 FAAPDAPARIGALVRAGgglLKGLRPMVQDIADvQWLASPALDAAFDALIAHDLAFDALIRAAHVPALQARLQRHPGLRV 162
Cdd:COG3618   81 LDAPDAAAELARLAAAG---VRGVRFNLQGEPD-GWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 163 VVDHGGKPAIAAGEFvAWAAGIAALAQHPGVHCKLSGLLTEAARGATAQTLEPYVAHLFARFGAQRVLWGSDWPVLTQRA 242
Cdd:COG3618  157 VIDHLGKPDIAAGDD-PWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 501408044 243 DYAQWLQIAQQLVQQYADGHAAAVFGDNARTFYRLP 278
Cdd:COG3618  236 DYGELLDLLEELLPDLSEAERRAILGDNAARLYGLA 271
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
4-277 1.75e-35

Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 128.80  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044    4 VDAHLHFWHLGRGDYDW------LTPELSALYRDFGPDDVSAALDAADVDSVVVVQAAATEAETCYLFELARDTPRIAGV 77
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDpggrlpFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044   78 VGWVDFAAPDAPARIGALVRAGGglLKGLRPMVQDIADVqWLASPALDAAFDALIAHDLAFDALI---------RAAHVP 148
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEAG--FRGVRLNPHPGGDP-LLGDRLDRPIYEALEELGLPVDIHTgfgdrpedtRAIQPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  149 ALQARLQRHPGLRVVVDHGGKPAIAagEFVAWAAGIAALAQHPGVHCKLSGLLTeAARGATAQTLEPYVAHLFARFGAQR 228
Cdd:pfam04909 158 LLAGVARKFPDLKIVLDHGGGPWIP--EGLDDPAALALLARRPNVYVKLSGLYR-DLYFDAPLADRPYLARLLEAFGPDR 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 501408044  229 VLWGSDWPVLTQRADYAQWLQIAQQLVQQYADGHAAAVFGDNARTFYRL 277
Cdd:pfam04909 235 ILFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
63-279 2.05e-10

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 59.61  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044  63 YLFELARDTP-RIAGVVGwVDFAAPDAPAR-IGALVRAGGglLKG--LRPMVQDIAdvqwLASPALDAAFDALIAHDL-- 136
Cdd:COG2159   50 WLAELVARYPdRFIGFAT-VDPQDPDAAVEeLERAVEELG--FRGvkLHPAVGGFP----LDDPRLDPLYEAAAELGLpv 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 137 ----------AFDALIRAAHVPALQARLQRHPGLRVVVDHGGKPAIAagefvawAAGIAALAQHPGVHCKLSGllteaar 206
Cdd:COG2159  123 lvhpgtppgpPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPWLP-------ELLGRLLKRLPNVYFDTSG------- 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501408044 207 gatAQTLEPYVAHLFARFGAQRVLWGSDWPVltqrADYAQWLQIAQQLvQQYADGHAAAVFGDNARTFYRLPR 279
Cdd:COG2159  189 ---VFPRPEALRELLETLGADRILFGSDYPH----WDPPEALEALEEL-PGLSEEDREKILGGNAARLLGLDA 253
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
138-236 7.84e-06

2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid (OMA) or its tautomer, 4-carboxy-2-hydroxymuconic acid (CHM). This reaction is part of the protocatechuate (PCA) 4,5-cleavage pathway. PCA is one of the most important intermediate metabolites in the bacterial pathways for various phenolic compounds, including lignin, which is the most abundant aromatic material in nature.


Pssm-ID: 238636  Cd Length: 263  Bit Score: 46.28  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501408044 138 FDALIRAAHVPALQARlqrhpGLRVVVDHGGKPAIAAGEFVAWAAGIAALAQHPGVHCKLSGLLTEAARGATAQTLEPyV 217
Cdd:cd01311  130 FDAVDLPALLPFLQKL-----PVAVVIDHFGRPDVTKGVDGAEFAALLKLIEEGNVWVKVSGPYRLSVKQEAYADVIA-F 203
                         90
                 ....*....|....*....
gi 501408044 218 AHLFARFGAQRVLWGSDWP 236
Cdd:cd01311  204 ARQIVAAAPDRLVWGTDWP 222
 
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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