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Conserved domains on  [gi|1734324461|ref|NP_001360068|]
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2-amino-3-carboxymuconate-6-semialdehyde decarboxylase [Caenorhabditis elegans]

Protein Classification

amidohydrolase family protein( domain architecture ID 10005476)

amidohydrolase family protein is a metallo-dependent hydrolase with a TIM barrel fold and a conserved metal binding site, involving four histidines and one aspartic acid residue; similar to 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (ACMSD), a metal-dependent enzyme that converts ACMS to alpha-aminomuconate semialdehyde (AMS)

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
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
66-343 1.93e-57

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 186.72  E-value: 1.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEEVKRCV 145
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 146 SM-GIKGFEVGSHVAEKSLDHRDFWPLYKICEELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNIL 224
Cdd:COG2159    85 EElGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 225 VLFPKLKLCFAHGGGAY-PQIRGRVshgwnvrpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLG 301
Cdd:COG2159   151 ERFPDLKFILAHGGGPWlPELLGRL--------------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFG 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1734324461 302 TDYPFPLGELEVgRVVEEYKPFSAKDREDLLWKNAVKMLDID 343
Cdd:COG2159   212 SDYPHWDPPEAL-EALEELPGLSEEDREKILGGNAARLLGLD 252
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
66-343 1.93e-57

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 186.72  E-value: 1.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEEVKRCV 145
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 146 SM-GIKGFEVGSHVAEKSLDHRDFWPLYKICEELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNIL 224
Cdd:COG2159    85 EElGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 225 VLFPKLKLCFAHGGGAY-PQIRGRVshgwnvrpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLG 301
Cdd:COG2159   151 ERFPDLKFILAHGGGPWlPELLGRL--------------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFG 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1734324461 302 TDYPFPLGELEVgRVVEEYKPFSAKDREDLLWKNAVKMLDID 343
Cdd:COG2159   212 SDYPHWDPPEAL-EALEELPGLSEEDREKILGGNAARLLGLD 252
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
57-342 1.60e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 151.92  E-value: 1.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461  57 LFRVVEPNCFDTETRIADMNRANVNVQCLS----TVPVMFSYWAKPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMN 132
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 133 DVQRAVEEVKRCV-SMGIKGFEVGSHVAEKSLDH-RDFWPLYKICEELSVVLFVHPwdmhmwdgrldkywmpwLVGMPSE 210
Cdd:pfam04909  87 DPEDAAAELERAVgEAGFRGVRLNPHPGGDPLLGdRLDRPIYEALEELGLPVDIHT-----------------GFGDRPE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 211 TAQAICSVLMGNILVLFPKLKLCFAHGGGAYPQIRGR-------VSHGWNVRPDLCAgkckvapnkLDGLLWTDSLVHDP 283
Cdd:pfam04909 150 DTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDdpaalalLARRPNVYVKLSG---------LYRDLYFDAPLADR 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734324461 284 KALELLINTVGKEHIVLGTDYPFPLGELEVGRVVEEYKPF----SAKDREDLLWKNAVKMLDI 342
Cdd:pfam04909 221 PYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
66-343 1.93e-57

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 186.72  E-value: 1.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEEVKRCV 145
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 146 SM-GIKGFEVGSHVAEKSLDHRDFWPLYKICEELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNIL 224
Cdd:COG2159    85 EElGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 225 VLFPKLKLCFAHGGGAY-PQIRGRVshgwnvrpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLG 301
Cdd:COG2159   151 ERFPDLKFILAHGGGPWlPELLGRL--------------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFG 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1734324461 302 TDYPFPLGELEVgRVVEEYKPFSAKDREDLLWKNAVKMLDID 343
Cdd:COG2159   212 SDYPHWDPPEAL-EALEELPGLSEEDREKILGGNAARLLGLD 252
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
57-342 1.60e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 151.92  E-value: 1.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461  57 LFRVVEPNCFDTETRIADMNRANVNVQCLS----TVPVMFSYWAKPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMN 132
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 133 DVQRAVEEVKRCV-SMGIKGFEVGSHVAEKSLDH-RDFWPLYKICEELSVVLFVHPwdmhmwdgrldkywmpwLVGMPSE 210
Cdd:pfam04909  87 DPEDAAAELERAVgEAGFRGVRLNPHPGGDPLLGdRLDRPIYEALEELGLPVDIHT-----------------GFGDRPE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734324461 211 TAQAICSVLMGNILVLFPKLKLCFAHGGGAYPQIRGR-------VSHGWNVRPDLCAgkckvapnkLDGLLWTDSLVHDP 283
Cdd:pfam04909 150 DTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDdpaalalLARRPNVYVKLSG---------LYRDLYFDAPLADR 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1734324461 284 KALELLINTVGKEHIVLGTDYPFPLGELEVGRVVEEYKPF----SAKDREDLLWKNAVKMLDI 342
Cdd:pfam04909 221 PYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 283
 
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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