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Conserved domains on  [gi|983312218|ref|WP_060497603|]
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MULTISPECIES: amidohydrolase [Pseudomonas]

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];
11-277 1.89e-84

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


:

Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 253.98  E-value: 1.89e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  11 AIDTHAHVFSR---RLNLASERRYAPsYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRGVVM-- 85
Cdd:COG3618    2 IIDAHHHVWDPdrgRYPWLPDRSYPP-RDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWvd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  86 LERDVERETLDEMARLGVKGVRLNLMGQALPDLTGAQWRPLLERIGEQGWHLELHRQVADIPALVRALEPY-GLDIVVDH 164
Cdd:COG3618   81 LDAPDAAAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLpDLPVVIDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 165 FGRPDARRGlGQPGFAELLTLGGRGKVWVKVSGIYRLEGS---PEQNLAFARQALctleAHYGAERLMWGSDWPHTQHes 241
Cdd:COG3618  161 LGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAgwpYADLRPYARALL----EAFGPDRLMWGSDWPVTLL-- 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 983312218 242 AVGFSTALEQFEAL--GCSAELRRALLVDTARALFGFE 277
Cdd:COG3618  234 APDYGELLDLLEELlpDLSEAERRAILGDNAARLYGLA 271
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
11-277 1.89e-84

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 253.98  E-value: 1.89e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  11 AIDTHAHVFSR---RLNLASERRYAPsYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRGVVM-- 85
Cdd:COG3618    2 IIDAHHHVWDPdrgRYPWLPDRSYPP-RDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWvd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  86 LERDVERETLDEMARLGVKGVRLNLMGQALPDLTGAQWRPLLERIGEQGWHLELHRQVADIPALVRALEPY-GLDIVVDH 164
Cdd:COG3618   81 LDAPDAAAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLpDLPVVIDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 165 FGRPDARRGlGQPGFAELLTLGGRGKVWVKVSGIYRLEGS---PEQNLAFARQALctleAHYGAERLMWGSDWPHTQHes 241
Cdd:COG3618  161 LGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAgwpYADLRPYARALL----EAFGPDRLMWGSDWPVTLL-- 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 983312218 242 AVGFSTALEQFEAL--GCSAELRRALLVDTARALFGFE 277
Cdd:COG3618  234 APDYGELLDLLEELlpDLSEAERRAILGDNAARLYGLA 271
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
12-276 2.33e-52

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 172.33  E-value: 2.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218   12 IDTHAHVFSRRLNLASE---------RRYAPSYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRG 82
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDpggrlpfmkRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218   83 VVMLERDVErETLDEMAR----LGVKGVRLNLMGQALPDLTGAQWRPLLERIGEQGWHLELH---------RQVADIPAL 149
Cdd:pfam04909  81 VAVVPLDPE-DAAAELERavgeAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHtgfgdrpedTRAIQPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  150 VRALEPY-GLDIVVDHFGRPDARRGLGQPGFAELLtlGGRGKVWVKVSGIYRLegSPEQNLAFARQALCTLEAHYGAERL 228
Cdd:pfam04909 160 AGVARKFpDLKIVLDHGGGPWIPEGLDDPAALALL--ARRPNVYVKLSGLYRD--LYFDAPLADRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 983312218  229 MWGSDWPHTQHESAVGFSTALEQFEALGCSAELRRALLVDTARALFGF 276
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
11-268 1.27e-51

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: 169.55  E-value: 1.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  11 AIDTHAHVFSRRLNLASERRYAPSYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRGVVMLERDV 90
Cdd:cd01311    2 AVDAHMHVFDPGYPFPPAPEKFTPYDPGIDDLRALRSTLGIDRVVIVQASIYGADNSNLLDALASNGKARGGATVDPRTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  91 ERETLDEMARLGVKGVRLNLM--GQALPDLTGAqwrpLLERIGEQGWHLELHRQVADIPALVRALEPYGLDIVVDHFGRP 168
Cdd:cd01311   82 TDAELKEMHDAGVRGVRFNFLfgGVDNKDELDE----IAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGRP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 169 DARRGLGQPGFAELLTLGGRGKVWVKVSGIYRLegSPEQNLAFARQALCTLEAHYGAERLMWGSDWPHT--QHESAVGFS 246
Cdd:cd01311  158 DVTKGVDGAEFAALLKLIEEGNVWVKVSGPYRL--SVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPrlREPDPMPDD 235
                        250       260
                 ....*....|....*....|...
gi 983312218 247 TALEQFEALGCS-AELRRALLVD 268
Cdd:cd01311  236 GALLRLIPSWAPdAQLQRKNLVD 258
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
11-277 1.89e-84

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 253.98  E-value: 1.89e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  11 AIDTHAHVFSR---RLNLASERRYAPsYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRGVVM-- 85
Cdd:COG3618    2 IIDAHHHVWDPdrgRYPWLPDRSYPP-RDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWvd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  86 LERDVERETLDEMARLGVKGVRLNLMGQALPDLTGAQWRPLLERIGEQGWHLELHRQVADIPALVRALEPY-GLDIVVDH 164
Cdd:COG3618   81 LDAPDAAAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLpDLPVVIDH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 165 FGRPDARRGlGQPGFAELLTLGGRGKVWVKVSGIYRLEGS---PEQNLAFARQALctleAHYGAERLMWGSDWPHTQHes 241
Cdd:COG3618  161 LGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAgwpYADLRPYARALL----EAFGPDRLMWGSDWPVTLL-- 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 983312218 242 AVGFSTALEQFEAL--GCSAELRRALLVDTARALFGFE 277
Cdd:COG3618  234 APDYGELLDLLEELlpDLSEAERRAILGDNAARLYGLA 271
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
12-276 2.33e-52

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 172.33  E-value: 2.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218   12 IDTHAHVFSRRLNLASE---------RRYAPSYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRG 82
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDpggrlpfmkRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218   83 VVMLERDVErETLDEMAR----LGVKGVRLNLMGQALPDLTGAQWRPLLERIGEQGWHLELH---------RQVADIPAL 149
Cdd:pfam04909  81 VAVVPLDPE-DAAAELERavgeAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHtgfgdrpedTRAIQPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  150 VRALEPY-GLDIVVDHFGRPDARRGLGQPGFAELLtlGGRGKVWVKVSGIYRLegSPEQNLAFARQALCTLEAHYGAERL 228
Cdd:pfam04909 160 AGVARKFpDLKIVLDHGGGPWIPEGLDDPAALALL--ARRPNVYVKLSGLYRD--LYFDAPLADRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 983312218  229 MWGSDWPHTQHESAVGFSTALEQFEALGCSAELRRALLVDTARALFGF 276
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
11-268 1.27e-51

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: 169.55  E-value: 1.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  11 AIDTHAHVFSRRLNLASERRYAPSYDAPLGDYLGQLLAHGFSHGVLVQPSFLGTDNRYLLNALQTVPGQLRGVVMLERDV 90
Cdd:cd01311    2 AVDAHMHVFDPGYPFPPAPEKFTPYDPGIDDLRALRSTLGIDRVVIVQASIYGADNSNLLDALASNGKARGGATVDPRTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  91 ERETLDEMARLGVKGVRLNLM--GQALPDLTGAqwrpLLERIGEQGWHLELHRQVADIPALVRALEPYGLDIVVDHFGRP 168
Cdd:cd01311   82 TDAELKEMHDAGVRGVRFNFLfgGVDNKDELDE----IAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGRP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 169 DARRGLGQPGFAELLTLGGRGKVWVKVSGIYRLegSPEQNLAFARQALCTLEAHYGAERLMWGSDWPHT--QHESAVGFS 246
Cdd:cd01311  158 DVTKGVDGAEFAALLKLIEEGNVWVKVSGPYRL--SVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPrlREPDPMPDD 235
                        250       260
                 ....*....|....*....|...
gi 983312218 247 TALEQFEALGCS-AELRRALLVD 268
Cdd:cd01311  236 GALLRLIPSWAPdAQLQRKNLVD 258
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
12-277 2.41e-15

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 73.48  E-value: 2.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  12 IDTHAHVFSrrlnlaserryapsydapLGDYLGQLLAHGFSHGVLVQPSFLGTD--------NRYLLNALQTVPGQLRGV 83
Cdd:COG2159    4 IDVHTHLGT------------------PEERLADMDEAGIDKAVLSPTPLADPElaalaraaNDWLAELVARYPDRFIGF 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218  84 VMLERDVERETLDEMAR----LGVKGVRLNLMGQAlPDLTGAQWRPLLERIGEQGWHLELHrqVADIPALVRALEPY--- 156
Cdd:COG2159   66 ATVDPQDPDAAVEELERaveeLGFRGVKLHPAVGG-FPLDDPRLDPLYEAAAELGLPVLVH--PGTPPGPPPGLDLYyaa 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983312218 157 ------------GLDIVVDHFGRPDARRGLGqpgfaELLTLGGRgkVWVKVSGIYrlegspeqnlaFARQALCTLEAHYG 224
Cdd:COG2159  143 plilsgvaerfpDLKFILAHGGGPWLPELLG-----RLLKRLPN--VYFDTSGVF-----------PRPEALRELLETLG 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983312218 225 AERLMWGSDWPHTQHESAVGFstaLEQFEALgcSAELRRALLVDTARALFGFE 277
Cdd:COG2159  205 ADRILFGSDYPHWDPPEALEA---LEELPGL--SEEDREKILGGNAARLLGLD 252
 
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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