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Conserved domains on  [gi|2075270921|ref|WP_219776060|]
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amidohydrolase family protein [Polymorphobacter sp. PAMC 29334]

Protein Classification

amidohydrolase( domain architecture ID 10007618)

metal-dependent amidohydrolase catalyzes the hydrolysis of amide bonds in target substrates

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];
27-296 6.29e-93

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


:

Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 276.32  E-value: 6.29e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  27 GAVDAHVHVFGPEAL-FPFSPKAKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIARSNGTARGVAVVD 105
Cdd:COG3618     1 GIIDAHHHVWDPDRGrYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 106 PAISD--AELARLHAGGIRGVRFNFLKRLVDHAPKDAFLALAQRIAPLGWHVVVYFEADLLTELTPFLAAIPTV-VVVDH 182
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLpVVIDH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 183 LGRPDIGQGpGGADISAFVALLDaQPHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERF-PDRVLWGTDWPHPNMEnniP 261
Cdd:COG3618   161 LGKPDIAAG-DDPWFAALLALAA-RPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA---P 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2075270921 262 DDGALVDVVPRIA--VSAQLQQKLLVANPDRLYWLDA 296
Cdd:COG3618   236 DYGELLDLLEELLpdLSEAERRAILGDNAARLYGLAA 272
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
27-296 6.29e-93

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 276.32  E-value: 6.29e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  27 GAVDAHVHVFGPEAL-FPFSPKAKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIARSNGTARGVAVVD 105
Cdd:COG3618     1 GIIDAHHHVWDPDRGrYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 106 PAISD--AELARLHAGGIRGVRFNFLKRLVDHAPKDAFLALAQRIAPLGWHVVVYFEADLLTELTPFLAAIPTV-VVVDH 182
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLpVVIDH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 183 LGRPDIGQGpGGADISAFVALLDaQPHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERF-PDRVLWGTDWPHPNMEnniP 261
Cdd:COG3618   161 LGKPDIAAG-DDPWFAALLALAA-RPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA---P 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2075270921 262 DDGALVDVVPRIA--VSAQLQQKLLVANPDRLYWLDA 296
Cdd:COG3618   236 DYGELLDLLEELLpdLSEAERRAILGDNAARLYGLAA 272
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
27-291 8.75e-90

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: 267.77  E-value: 8.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  27 GAVDAHVHVFGPEALFPFSPKaKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIArSNGTARGVAVVDP 106
Cdd:cd01311     1 GAVDAHMHVFDPGYPFPPAPE-KFTPYDPGIDDLRALRSTLGIDRVVIVQASIYGADNSNLLDALA-SNGKARGGATVDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 107 -AISDAELARLHAGGIRGVRFNFLKRLVDHapKDAFLALAQRIAPLGWHVVVYFEADLLTELTPFLAAIPTVVVVDHLGR 185
Cdd:cd01311    79 rTTTDAELKEMHDAGVRGVRFNFLFGGVDN--KDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 186 PDIGQGPGGADISAFVALLDAQpHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERFPDRVLWGTDWPHPNMENN--IPDD 263
Cdd:cd01311   157 PDVTKGVDGAEFAALLKLIEEG-NVWVKVSGPYRLSVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPRLREPdpMPDD 235
                         250       260
                  ....*....|....*....|....*...
gi 2075270921 264 GALVDVVPRIAVSAQLQQKLLVANPDRL 291
Cdd:cd01311   236 GALLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
29-292 2.93e-51

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 170.02  E-value: 2.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  29 VDAHVHV--------FGPEALFPFSPKAKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIARSNGTARG 100
Cdd:pfam04909   1 IDAHAHLwpdderigFDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 101 VAVVDP---AISDAELARLHAGGIRGVRFNFLKRLVDHAPKDAFLALAQRIAPLGWHVVVY---------FEADLLTELT 168
Cdd:pfam04909  81 VAVVPLdpeDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHtgfgdrpedTRAIQPLLLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 169 PFLAAIPTV-VVVDHLGRPDIgqgPGGADISAFVALLDAQPHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERFPDRVLW 247
Cdd:pfam04909 161 GVARKFPDLkIVLDHGGGPWI---PEGLDDPAALALLARRPNVYVKLSGLYRDLYFDAPLADRPYLARLLEAFGPDRILF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2075270921 248 GTDWPHPNMEnNIPDDGALVDVVPRIAVSAQLQQKLLVANPDRLY 292
Cdd:pfam04909 238 GSDWPHPPLE-ISPDDGVLLDLPLLLALSDEEREKILGGNAARLY 281
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
27-296 6.29e-93

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


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 276.32  E-value: 6.29e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  27 GAVDAHVHVFGPEAL-FPFSPKAKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIARSNGTARGVAVVD 105
Cdd:COG3618     1 GIIDAHHHVWDPDRGrYPWLPDRSYPPRDATPEDYLALLDALGVDRAVLVQASFYGADNRYLLDAAARHPDRLRGVAWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 106 PAISD--AELARLHAGGIRGVRFNFLKRLVDHAPKDAFLALAQRIAPLGWHVVVYFEADLLTELTPFLAAIPTV-VVVDH 182
Cdd:COG3618    81 LDAPDaaAELARLAAAGVRGVRFNLQGEPDGWLLDPAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDLpVVIDH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 183 LGRPDIGQGpGGADISAFVALLDaQPHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERF-PDRVLWGTDWPHPNMEnniP 261
Cdd:COG3618   161 LGKPDIAAG-DDPWFAALLALAA-RPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFgPDRLMWGSDWPVTLLA---P 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2075270921 262 DDGALVDVVPRIA--VSAQLQQKLLVANPDRLYWLDA 296
Cdd:COG3618   236 DYGELLDLLEELLpdLSEAERRAILGDNAARLYGLAA 272
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
27-291 8.75e-90

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: 267.77  E-value: 8.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  27 GAVDAHVHVFGPEALFPFSPKaKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIArSNGTARGVAVVDP 106
Cdd:cd01311     1 GAVDAHMHVFDPGYPFPPAPE-KFTPYDPGIDDLRALRSTLGIDRVVIVQASIYGADNSNLLDALA-SNGKARGGATVDP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 107 -AISDAELARLHAGGIRGVRFNFLKRLVDHapKDAFLALAQRIAPLGWHVVVYFEADLLTELTPFLAAIPTVVVVDHLGR 185
Cdd:cd01311    79 rTTTDAELKEMHDAGVRGVRFNFLFGGVDN--KDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 186 PDIGQGPGGADISAFVALLDAQpHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERFPDRVLWGTDWPHPNMENN--IPDD 263
Cdd:cd01311   157 PDVTKGVDGAEFAALLKLIEEG-NVWVKVSGPYRLSVKQEAYADVIAFARQIVAAAPDRLVWGTDWPHPRLREPdpMPDD 235
                         250       260
                  ....*....|....*....|....*...
gi 2075270921 264 GALVDVVPRIAVSAQLQQKLLVANPDRL 291
Cdd:cd01311   236 GALLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
29-292 2.93e-51

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 170.02  E-value: 2.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  29 VDAHVHV--------FGPEALFPFSPKAKYLPQDATPEMLFALRDSLGFARNVIVQASCHGTDNAATLDGIARSNGTARG 100
Cdd:pfam04909   1 IDAHAHLwpdderigFDPGGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 101 VAVVDP---AISDAELARLHAGGIRGVRFNFLKRLVDHAPKDAFLALAQRIAPLGWHVVVY---------FEADLLTELT 168
Cdd:pfam04909  81 VAVVPLdpeDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDRPIYEALEELGLPVDIHtgfgdrpedTRAIQPLLLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 169 PFLAAIPTV-VVVDHLGRPDIgqgPGGADISAFVALLDAQPHVWAKVSGADRLSVTGAPYDDFVAVVRPVVERFPDRVLW 247
Cdd:pfam04909 161 GVARKFPDLkIVLDHGGGPWI---PEGLDDPAALALLARRPNVYVKLSGLYRDLYFDAPLADRPYLARLLEAFGPDRILF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2075270921 248 GTDWPHPNMEnNIPDDGALVDVVPRIAVSAQLQQKLLVANPDRLY 292
Cdd:pfam04909 238 GSDWPHPPLE-ISPDDGVLLDLPLLLALSDEEREKILGGNAARLY 281
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
26-296 5.84e-08

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 52.67  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  26 PGAVDAHVHVFgpealfpfspkakylpqdaTPEMLFALRDSLGFARNVIVQASCHGTD--------NAATLDGIARSNGT 97
Cdd:COG2159     1 MMIIDVHTHLG-------------------TPEERLADMDEAGIDKAVLSPTPLADPElaalaraaNDWLAELVARYPDR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921  98 ARGVAVVDPAISDA---ELARLHA-GGIRGVRFNFLKRLVD-HAPK-DAFLALAQR----------IAPLGWHVVVYFEA 161
Cdd:COG2159    62 FIGFATVDPQDPDAaveELERAVEeLGFRGVKLHPAVGGFPlDDPRlDPLYEAAAElglpvlvhpgTPPGPPPGLDLYYA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075270921 162 DLLtELTPFLAAIPTV-VVVDHLGRPDIGQgpggadisAFVALLDAQPHVWakvsgadrlsVTGAPYDDFVAVVRPVVER 240
Cdd:COG2159   142 APL-ILSGVAERFPDLkFILAHGGGPWLPE--------LLGRLLKRLPNVY----------FDTSGVFPRPEALRELLET 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2075270921 241 F-PDRVLWGTDWPHPNMENNIpddgALVDVVPRIavSAQLQQKLLVANPDRLYWLDA 296
Cdd:COG2159   203 LgADRILFGSDYPHWDPPEAL----EALEELPGL--SEEDREKILGGNAARLLGLDA 253
 
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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