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Conserved domains on  [gi|1997926598|ref|WP_206362043|]
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amidohydrolase [Sphingomonas montana]

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

 Zoom to residue level

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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];
46-311 5.94e-62

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


:

Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 197.74  E-value: 5.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  46 GAWDCHTHIYGPFD-RFPLPSDAAYTPDAAPFVALQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAASGGRYRGIGLID 124
Cdd:COG3618     1 GIIDAHHHVWDPDRgRYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 125 AATTD--AQLQALHDGGLRGIRFNLMSHLPGSRDPAMLRRMAERVHGLGWHVLVH---GEMSVLVPVLEQWStlATPLVI 199
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLvdpRQLPALAPLLARLP--DLPVVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 200 DHMARPDLTKAvDQAQLAALVRQLRHPGRWIKLSGVDRaMHGAPAPWPQAVAHTRMLLAAA-PDRAIWGTDWPHPNITgp 278
Cdd:COG3618   159 DHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYR-ESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA-- 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1997926598 279 vPDEAALLGFIFDVCG--TDDSVRQVLVDNPARLY 311
Cdd:COG3618   235 -PDYGELLDLLEELLPdlSEAERRAILGDNAARLY 268
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
46-311 5.94e-62

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 197.74  E-value: 5.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  46 GAWDCHTHIYGPFD-RFPLPSDAAYTPDAAPFVALQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAASGGRYRGIGLID 124
Cdd:COG3618     1 GIIDAHHHVWDPDRgRYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 125 AATTD--AQLQALHDGGLRGIRFNLMSHLPGSRDPAMLRRMAERVHGLGWHVLVH---GEMSVLVPVLEQWStlATPLVI 199
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLvdpRQLPALAPLLARLP--DLPVVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 200 DHMARPDLTKAvDQAQLAALVRQLRHPGRWIKLSGVDRaMHGAPAPWPQAVAHTRMLLAAA-PDRAIWGTDWPHPNITgp 278
Cdd:COG3618   159 DHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYR-ESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA-- 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1997926598 279 vPDEAALLGFIFDVCG--TDDSVRQVLVDNPARLY 311
Cdd:COG3618   235 -PDYGELLDLLEELLPdlSEAERRAILGDNAARLY 268
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
46-310 1.32e-61

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: 196.51  E-value: 1.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  46 GAWDCHTHIYGPfdRFPLPSDAAYTPDAAPFVA-LQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAaSGGRYRGIGLID 124
Cdd:cd01311     1 GAVDAHMHVFDP--GYPFPPAPEKFTPYDPGIDdLRALRSTLGIDRVVIVQASIYGADNSNLLDALA-SNGKARGGATVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 125 -AATTDAQLQALHDGGLRGIRFNLMShlPGSRDPAMLRRMAERVHGLGWHVLVHGEMSVLVPVLEQWSTLATPLVIDHMA 203
Cdd:cd01311    78 pRTTTDAELKEMHDAGVRGVRFNFLF--GGVDNKDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 204 RPDLTKAVDQAQLAALVRQLRHPGRWIKLSGVDRaMHGAPAPWPQAVAHTRMLLAAAPDRAIWGTDWPHPNI--TGPVPD 281
Cdd:cd01311   156 RPDVTKGVDGAEFAALLKLIEEGNVWVKVSGPYR-LSVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPRLrePDPMPD 234
                         250       260
                  ....*....|....*....|....*....
gi 1997926598 282 EAALLGFIFDVCGTDDSVRQVLVDNPARL 310
Cdd:cd01311   235 DGALLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
49-311 6.60e-38

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 135.74  E-value: 6.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  49 DCHTHIY--------GPFDRFPLPSDAAYTPDAAPFVALQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAASGGRYRGI 120
Cdd:pfam04909   2 DAHAHLWpdderigfDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 121 GLID---AATTDAQLQALHDGGLRGIRFNLMSHLPGSRDPAMLRRMAERVHGLGWHVLVHGEMSVLVPVLEQWSTLA--- 194
Cdd:pfam04909  82 AVVPldpEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAIQPLLlag 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 195 -------TPLVIDHMARPDLTKAVDQAQLAALVRqlRHPGRWIKLSGVDRAMHGAPAPWPQAVAhTRMLLAAAPDRAIWG 267
Cdd:pfam04909 162 varkfpdLKIVLDHGGGPWIPEGLDDPAALALLA--RRPNVYVKLSGLYRDLYFDAPLADRPYL-ARLLEAFGPDRILFG 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1997926598 268 TDWPHPNITGPvPDEAALLGFIFDVCGTDDSVRQVLVDNPARLY 311
Cdd:pfam04909 239 SDWPHPPLEIS-PDDGVLLDLPLLLALSDEEREKILGGNAARLY 281
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
46-311 5.94e-62

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 197.74  E-value: 5.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  46 GAWDCHTHIYGPFD-RFPLPSDAAYTPDAAPFVALQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAASGGRYRGIGLID 124
Cdd:COG3618     1 GIIDAHHHVWDPDRgRYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 125 AATTD--AQLQALHDGGLRGIRFNLMSHLPGSRDPAMLRRMAERVHGLGWHVLVH---GEMSVLVPVLEQWStlATPLVI 199
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLvdpRQLPALAPLLARLP--DLPVVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 200 DHMARPDLTKAvDQAQLAALVRQLRHPGRWIKLSGVDRaMHGAPAPWPQAVAHTRMLLAAA-PDRAIWGTDWPHPNITgp 278
Cdd:COG3618   159 DHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYR-ESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA-- 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1997926598 279 vPDEAALLGFIFDVCG--TDDSVRQVLVDNPARLY 311
Cdd:COG3618   235 -PDYGELLDLLEELLPdlSEAERRAILGDNAARLY 268
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
46-310 1.32e-61

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: 196.51  E-value: 1.32e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  46 GAWDCHTHIYGPfdRFPLPSDAAYTPDAAPFVA-LQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAaSGGRYRGIGLID 124
Cdd:cd01311     1 GAVDAHMHVFDP--GYPFPPAPEKFTPYDPGIDdLRALRSTLGIDRVVIVQASIYGADNSNLLDALA-SNGKARGGATVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 125 -AATTDAQLQALHDGGLRGIRFNLMShlPGSRDPAMLRRMAERVHGLGWHVLVHGEMSVLVPVLEQWSTLATPLVIDHMA 203
Cdd:cd01311    78 pRTTTDAELKEMHDAGVRGVRFNFLF--GGVDNKDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 204 RPDLTKAVDQAQLAALVRQLRHPGRWIKLSGVDRaMHGAPAPWPQAVAHTRMLLAAAPDRAIWGTDWPHPNI--TGPVPD 281
Cdd:cd01311   156 RPDVTKGVDGAEFAALLKLIEEGNVWVKVSGPYR-LSVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPRLrePDPMPD 234
                         250       260
                  ....*....|....*....|....*....
gi 1997926598 282 EAALLGFIFDVCGTDDSVRQVLVDNPARL 310
Cdd:cd01311   235 DGALLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
49-311 6.60e-38

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 135.74  E-value: 6.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598  49 DCHTHIY--------GPFDRFPLPSDAAYTPDAAPFVALQAAHAALGIEHGVLVQAAPYGTNHAAIIEAIAASGGRYRGI 120
Cdd:pfam04909   2 DAHAHLWpdderigfDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 121 GLID---AATTDAQLQALHDGGLRGIRFNLMSHLPGSRDPAMLRRMAERVHGLGWHVLVHGEMSVLVPVLEQWSTLA--- 194
Cdd:pfam04909  82 AVVPldpEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAIQPLLlag 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 195 -------TPLVIDHMARPDLTKAVDQAQLAALVRqlRHPGRWIKLSGVDRAMHGAPAPWPQAVAhTRMLLAAAPDRAIWG 267
Cdd:pfam04909 162 varkfpdLKIVLDHGGGPWIPEGLDDPAALALLA--RRPNVYVKLSGLYRDLYFDAPLADRPYL-ARLLEAFGPDRILFG 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1997926598 268 TDWPHPNITGPvPDEAALLGFIFDVCGTDDSVRQVLVDNPARLY 311
Cdd:pfam04909 239 SDWPHPPLEIS-PDDGVLLDLPLLLALSDEEREKILGGNAARLY 281
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
115-311 5.50e-07

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 49.98  E-value: 5.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 115 GRYRGIGLIDAATTDAQLQALH----DGGLRGIRFNLMSHLPGSRDPAmLRRMAERVHGLGWHVLVH-GEMSVLVPVLEQ 189
Cdd:COG2159    60 DRFIGFATVDPQDPDAAVEELEraveELGFRGVKLHPAVGGFPLDDPR-LDPLYEAAAELGLPVLVHpGTPPGPPPGLDL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997926598 190 WstLATPLVIDHMAR--PDLTkavdqaqlaaLVrqLRHPGRWIKLSGVDRAM------HGAPAPWPQAVAHTRMLLAAA- 260
Cdd:COG2159   139 Y--YAAPLILSGVAErfPDLK----------FI--LAHGGGPWLPELLGRLLkrlpnvYFDTSGVFPRPEALRELLETLg 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1997926598 261 PDRAIWGTDWPHPNITGPVPDEAALLGFifdvcgTDDSVRQVLVDNPARLY 311
Cdd:COG2159   205 ADRILFGSDYPHWDPPEALEALEELPGL------SEEDREKILGGNAARLL 249
 
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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