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Conserved domains on  [gi|495339056|ref|WP_008063790|]
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amidohydrolase [Pseudomonas sp. GM78]

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];
7-276 4.78e-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: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   7 PKIDCHNHLFDPA--RFPYRTDTIYAPagqEVATLEQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQGEGRFKGI 84
Cdd:COG3618    1 GIIDAHHHVWDPDrgRYPWLPDRSYPP---RDATPEDYLALLDALGVDRAVLVQA-SFYGADNRYLLDAAARHPDRLRGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  85 AVVEHAIG--LDELAALKEQGVVGVAFNPALEGLASMN--GVAGLFGRLAELDLFAQIQVQGNQLVELLGLIESTAP-RL 159
Cdd:COG3618   77 AWVDLDAPdaAAELARLAAAGVRGVRFNLQGEPDGWLLdpAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDlPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 160 LIDHCGRPEARAGvGQPGFQALLGLAGSGRACVKISGMHKFAAHDHFQEQAGAYVRELLRAFGADACVWGSDWPFIREQS 239
Cdd:COG3618  157 VIDHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 495339056 240 rlDYGPLLKLAEQLMA--DASVRRKVMWDTPRRLFGFGE 276
Cdd:COG3618  236 --DYGELLDLLEELLPdlSEAERRAILGDNAARLYGLAA 272
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
7-276 4.78e-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: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   7 PKIDCHNHLFDPA--RFPYRTDTIYAPagqEVATLEQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQGEGRFKGI 84
Cdd:COG3618    1 GIIDAHHHVWDPDrgRYPWLPDRSYPP---RDATPEDYLALLDALGVDRAVLVQA-SFYGADNRYLLDAAARHPDRLRGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  85 AVVEHAIG--LDELAALKEQGVVGVAFNPALEGLASMN--GVAGLFGRLAELDLFAQIQVQGNQLVELLGLIESTAP-RL 159
Cdd:COG3618   77 AWVDLDAPdaAAELARLAAAGVRGVRFNLQGEPDGWLLdpAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDlPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 160 LIDHCGRPEARAGvGQPGFQALLGLAGSGRACVKISGMHKFAAHDHFQEQAGAYVRELLRAFGADACVWGSDWPFIREQS 239
Cdd:COG3618  157 VIDHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 495339056 240 rlDYGPLLKLAEQLMA--DASVRRKVMWDTPRRLFGFGE 276
Cdd:COG3618  236 --DYGELLDLLEELLPdlSEAERRAILGDNAARLYGLAA 272
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
10-271 1.64e-43

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: 148.75  E-value: 1.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  10 DCHNHLFDPARFPYRTDTIYAPAGQEVAtleQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQgEGRFKGIAVV-E 88
Cdd:cd01311    4 DAHMHVFDPGYPFPPAPEKFTPYDPGID---DLRALRSTLGIDRVVIVQA-SIYGADNSNLLDALAS-NGKARGGATVdP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  89 HAIGLDELAALKEQGVVGVAFNPALEGLASMNGVAGLFGRLAELDLFAQIQVQGNQLVELLGLIESTAPRLLIDHCGRPE 168
Cdd:cd01311   79 RTTTDAELKEMHDAGVRGVRFNFLFGGVDNKDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGRPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 169 ARAGVGQPGFQALLGLAGSGRACVKISGMHKFAAHDHFQEQAGAYVRELLRAfGADACVWGSDWPFIREQS---RLDYGP 245
Cdd:cd01311  159 VTKGVDGAEFAALLKLIEEGNVWVKVSGPYRLSVKQEAYADVIAFARQIVAA-APDRLVWGTDWPHPRLREpdpMPDDGA 237
                        250       260
                 ....*....|....*....|....*.
gi 495339056 246 LLKLAEQLMADASVRRKVMWDTPRRL 271
Cdd:cd01311  238 LLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
9-274 1.54e-33

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 123.41  E-value: 1.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056    9 IDCHNHLFDPARFPYRTDTIYAPAGQE------VATLEQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQGEGRFK 82
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDPGGRLPFMKRrgydprDASPEDLLALGAALGVARAVVVAA-SCRGANNRVAAEALARPGRFLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   83 GIAVVEHAI--GLDEL-AALKEQGVVGVAFNPALEGLASMNGVAG--LFGRLAELDLFAQIQVQGN---------QLVEL 148
Cdd:pfam04909  80 GVAVVPLDPedAAAELeRAVGEAGFRGVRLNPHPGGDPLLGDRLDrpIYEALEELGLPVDIHTGFGdrpedtraiQPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  149 LGLIEStAPRL--LIDHCGRPEARAGVGQPGFQALLGLAGSGRacVKISGMHKFAAHDHFQEqAGAYVRELLRAFGADAC 226
Cdd:pfam04909 160 AGVARK-FPDLkiVLDHGGGPWIPEGLDDPAALALLARRPNVY--VKLSGLYRDLYFDAPLA-DRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 495339056  227 VWGSDWPFIREQSRLDYGPLLKLAEQLMADASVRRKVMWDTPRRLFGF 274
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
7-276 4.78e-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: 4.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   7 PKIDCHNHLFDPA--RFPYRTDTIYAPagqEVATLEQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQGEGRFKGI 84
Cdd:COG3618    1 GIIDAHHHVWDPDrgRYPWLPDRSYPP---RDATPEDYLALLDALGVDRAVLVQA-SFYGADNRYLLDAAARHPDRLRGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  85 AVVEHAIG--LDELAALKEQGVVGVAFNPALEGLASMN--GVAGLFGRLAELDLFAQIQVQGNQLVELLGLIESTAP-RL 159
Cdd:COG3618   77 AWVDLDAPdaAAELARLAAAGVRGVRFNLQGEPDGWLLdpAFRRGLARLAELGLHFDLLVDPRQLPALAPLLARLPDlPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 160 LIDHCGRPEARAGvGQPGFQALLGLAGSGRACVKISGMHKFAAHDHFQEQAGAYVRELLRAFGADACVWGSDWPFIREQS 239
Cdd:COG3618  157 VIDHLGKPDIAAG-DDPWFAALLALAARPNVWVKLSGLYRESDAGWPYADLRPYARALLEAFGPDRLMWGSDWPVTLLAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 495339056 240 rlDYGPLLKLAEQLMA--DASVRRKVMWDTPRRLFGFGE 276
Cdd:COG3618  236 --DYGELLDLLEELLPdlSEAERRAILGDNAARLYGLAA 272
PDC_hydrolase cd01311
2-pyrone-4,6-dicarboxylic acid (PDC) hydrolase hydrolyzes PDC to yield 4-oxalomesaconic acid ...
10-271 1.64e-43

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: 148.75  E-value: 1.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  10 DCHNHLFDPARFPYRTDTIYAPAGQEVAtleQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQgEGRFKGIAVV-E 88
Cdd:cd01311    4 DAHMHVFDPGYPFPPAPEKFTPYDPGID---DLRALRSTLGIDRVVIVQA-SIYGADNSNLLDALAS-NGKARGGATVdP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  89 HAIGLDELAALKEQGVVGVAFNPALEGLASMNGVAGLFGRLAELDLFAQIQVQGNQLVELLGLIESTAPRLLIDHCGRPE 168
Cdd:cd01311   79 RTTTDAELKEMHDAGVRGVRFNFLFGGVDNKDELDEIAKRAAELGWHVQVYFDAVDLPALLPFLQKLPVAVVIDHFGRPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 169 ARAGVGQPGFQALLGLAGSGRACVKISGMHKFAAHDHFQEQAGAYVRELLRAfGADACVWGSDWPFIREQS---RLDYGP 245
Cdd:cd01311  159 VTKGVDGAEFAALLKLIEEGNVWVKVSGPYRLSVKQEAYADVIAFARQIVAA-APDRLVWGTDWPHPRLREpdpMPDDGA 237
                        250       260
                 ....*....|....*....|....*.
gi 495339056 246 LLKLAEQLMADASVRRKVMWDTPRRL 271
Cdd:cd01311  238 LLRLIPSWAPDAQLQRKNLVDNPARL 263
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
9-274 1.54e-33

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 123.41  E-value: 1.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056    9 IDCHNHLFDPARFPYRTDTIYAPAGQE------VATLEQFGRVMDAYGVQHALLVGPtSGYRTDNRCLLHALAQGEGRFK 82
Cdd:pfam04909   1 IDAHAHLWPDDERIGFDPGGRLPFMKRrgydprDASPEDLLALGAALGVARAVVVAA-SCRGANNRVAAEALARPGRFLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   83 GIAVVEHAI--GLDEL-AALKEQGVVGVAFNPALEGLASMNGVAG--LFGRLAELDLFAQIQVQGN---------QLVEL 148
Cdd:pfam04909  80 GVAVVPLDPedAAAELeRAVGEAGFRGVRLNPHPGGDPLLGDRLDrpIYEALEELGLPVDIHTGFGdrpedtraiQPLLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  149 LGLIEStAPRL--LIDHCGRPEARAGVGQPGFQALLGLAGSGRacVKISGMHKFAAHDHFQEqAGAYVRELLRAFGADAC 226
Cdd:pfam04909 160 AGVARK-FPDLkiVLDHGGGPWIPEGLDDPAALALLARRPNVY--VKLSGLYRDLYFDAPLA-DRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 495339056  227 VWGSDWPFIREQSRLDYGPLLKLAEQLMADASVRRKVMWDTPRRLFGF 274
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
7-274 6.72e-14

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 69.62  E-value: 6.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056   7 PKIDCHNHLFDParfpyrtdtiyapagqevatlEQFGRVMDAYGVQHALLVGPTSGY-------RTDNRCLLHALAQGEG 79
Cdd:COG2159    2 MIIDVHTHLGTP---------------------EERLADMDEAGIDKAVLSPTPLADpelaalaRAANDWLAELVARYPD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056  80 RFKGIAVV-----EHAIglDELA-ALKEQGVVGVAFNPALEGLaSMN--GVAGLFGRLAELDLFAQIQVQGNQLVELLGL 151
Cdd:COG2159   61 RFIGFATVdpqdpDAAV--EELErAVEELGFRGVKLHPAVGGF-PLDdpRLDPLYEAAAELGLPVLVHPGTPPGPPPGLD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495339056 152 IESTAPRLLIDHCGR-PEAR---AGVGQPGFQALLglagsGRACVK-------ISGMHKFAahdhfqeqagAYVRELLRA 220
Cdd:COG2159  138 LYYAAPLILSGVAERfPDLKfilAHGGGPWLPELL-----GRLLKRlpnvyfdTSGVFPRP----------EALRELLET 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495339056 221 FGADACVWGSDWPFIreqsrlDYGPLLKLAEQLMA-DASVRRKVMWDTPRRLFGF 274
Cdd:COG2159  203 LGADRILFGSDYPHW------DPPEALEALEELPGlSEEDREKILGGNAARLLGL 251
 
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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