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Conserved domains on  [gi|71995655|ref|NP_001022935|]
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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 ...
66-392 9.32e-48

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 163.23  E-value: 9.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEifgkri 145
Cdd:COG2159  11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVE------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 146 fffeiwspakkspeEVKRCVSM-GIKGFEVGSHVAEKSLDHRDFWPLYKLtesfklstimpgfceffenwglttktpgiC 224
Cdd:COG2159  79 --------------ELERAVEElGFRGVKLHPAVGGFPLDDPRLDPLYEA-----------------------------A 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 225 EELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNILVLFPKLKLCFAHGGGAY-PQIRGRVshgwnv 303
Cdd:COG2159 116 AELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVAERFPDLKFILAHGGGPWlPELLGRL------ 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 304 rpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLGTDYPFPLGELEVgRVVEEYKPFSAKDREDLL 381
Cdd:COG2159 176 --------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPPEAL-EALEELPGLSEEDREKIL 241
                       330
                ....*....|.
gi 71995655 382 WKNAVKMLDID 392
Cdd:COG2159 242 GGNAARLLGLD 252
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
66-392 9.32e-48

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 163.23  E-value: 9.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEifgkri 145
Cdd:COG2159  11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVE------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 146 fffeiwspakkspeEVKRCVSM-GIKGFEVGSHVAEKSLDHRDFWPLYKLtesfklstimpgfceffenwglttktpgiC 224
Cdd:COG2159  79 --------------ELERAVEElGFRGVKLHPAVGGFPLDDPRLDPLYEA-----------------------------A 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 225 EELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNILVLFPKLKLCFAHGGGAY-PQIRGRVshgwnv 303
Cdd:COG2159 116 AELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVAERFPDLKFILAHGGGPWlPELLGRL------ 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 304 rpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLGTDYPFPLGELEVgRVVEEYKPFSAKDREDLL 381
Cdd:COG2159 176 --------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPPEAL-EALEELPGLSEEDREKIL 241
                       330
                ....*....|.
gi 71995655 382 WKNAVKMLDID 392
Cdd:COG2159 242 GGNAARLLGLD 252
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
57-391 2.29e-34

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 128.80  E-value: 2.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655    57 LFRVVEPNCFDTETRIADMNRANVNVQCLS----TVPVMFSYWAKPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMN 132
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   133 DVQRAVEifgkrifffeiwspakkspeEVKRCV-SMGIKGFEVGSHVAEKSLDHRDFWplykltesfklstimpgfCEFF 211
Cdd:pfam04909  87 DPEDAAA--------------------ELERAVgEAGFRGVRLNPHPGGDPLLGDRLD------------------RPIY 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   212 EnwglttktpgICEELSVVLFVHPwdmhmwdgrldkywmpwLVGMPSETAQAICSVLMGNILVLFPKLKLCFAHGGGAYP 291
Cdd:pfam04909 129 E----------ALEELGLPVDIHT-----------------GFGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWI 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   292 QIRGR-------VSHGWNVRPDLCAgkckvapnkLDGLLWTDSLVHDPKALELLINTVGKEHIVLGTDYPFPLGELEVGR 364
Cdd:pfam04909 182 PEGLDdpaalalLARRPNVYVKLSG---------LYRDLYFDAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDD 252
                         330       340       350
                  ....*....|....*....|....*....|.
gi 71995655   365 VVEEYKPF----SAKDREDLLWKNAVKMLDI 391
Cdd:pfam04909 253 GVLLDLPLllalSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
66-392 9.32e-48

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 163.23  E-value: 9.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655  66 FDTETRIADMNRANVNVQCLSTVPVMfsywakPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEifgkri 145
Cdd:COG2159  11 GTPEERLADMDEAGIDKAVLSPTPLA------DPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVE------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 146 fffeiwspakkspeEVKRCVSM-GIKGFEVGSHVAEKSLDHRDFWPLYKLtesfklstimpgfceffenwglttktpgiC 224
Cdd:COG2159  79 --------------ELERAVEElGFRGVKLHPAVGGFPLDDPRLDPLYEA-----------------------------A 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 225 EELSVVLFVHPWDMHMWDGRLDKYWMpwlvgmpsetaqaiCSVLMGNILVLFPKLKLCFAHGGGAY-PQIRGRVshgwnv 303
Cdd:COG2159 116 AELGLPVLVHPGTPPGPPPGLDLYYA--------------APLILSGVAERFPDLKFILAHGGGPWlPELLGRL------ 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655 304 rpdlcagkCKVAPNkldglLWTD--SLVHDPKALELLINTVGKEHIVLGTDYPFPLGELEVgRVVEEYKPFSAKDREDLL 381
Cdd:COG2159 176 --------LKRLPN-----VYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPPEAL-EALEELPGLSEEDREKIL 241
                       330
                ....*....|.
gi 71995655 382 WKNAVKMLDID 392
Cdd:COG2159 242 GGNAARLLGLD 252
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
57-391 2.29e-34

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 128.80  E-value: 2.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655    57 LFRVVEPNCFDTETRIADMNRANVNVQCLS----TVPVMFSYWAKPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMN 132
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   133 DVQRAVEifgkrifffeiwspakkspeEVKRCV-SMGIKGFEVGSHVAEKSLDHRDFWplykltesfklstimpgfCEFF 211
Cdd:pfam04909  87 DPEDAAA--------------------ELERAVgEAGFRGVRLNPHPGGDPLLGDRLD------------------RPIY 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   212 EnwglttktpgICEELSVVLFVHPwdmhmwdgrldkywmpwLVGMPSETAQAICSVLMGNILVLFPKLKLCFAHGGGAYP 291
Cdd:pfam04909 129 E----------ALEELGLPVDIHT-----------------GFGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWI 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995655   292 QIRGR-------VSHGWNVRPDLCAgkckvapnkLDGLLWTDSLVHDPKALELLINTVGKEHIVLGTDYPFPLGELEVGR 364
Cdd:pfam04909 182 PEGLDdpaalalLARRPNVYVKLSG---------LYRDLYFDAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDD 252
                         330       340       350
                  ....*....|....*....|....*....|.
gi 71995655   365 VVEEYKPF----SAKDREDLLWKNAVKMLDI 391
Cdd:pfam04909 253 GVLLDLPLllalSDEEREKILGGNAARLYGL 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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