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Conserved domains on  [gi|2462570040|ref|XP_054196476|]
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2-amino-3-carboxymuconate-6-semialdehyde decarboxylase isoform X2 [Homo sapiens]

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

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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 ...
12-274 1.84e-56

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 181.72  E-value: 1.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  12 AGIQKFVLEKWTkkAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNE 91
Cdd:COG2159    23 AGIDKAVLSPTP--LADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAVEELGFRGVKLHPAVGG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  92 WDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAF 171
Cdd:COG2159   101 FPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 172 -PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGElEPGKLIE 248
Cdd:COG2159   168 lPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPP-EALEALE 227
                         250       260
                  ....*....|....*....|....*.
gi 2462570040 249 SMEEFDEETKNKLKAGNALAFLGLER 274
Cdd:COG2159   228 ELPGLSEEDREKILGGNAARLLGLDA 253
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
12-274 1.84e-56

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 181.72  E-value: 1.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  12 AGIQKFVLEKWTkkAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNE 91
Cdd:COG2159    23 AGIDKAVLSPTP--LADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAVEELGFRGVKLHPAVGG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  92 WDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAF 171
Cdd:COG2159   101 FPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 172 -PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGElEPGKLIE 248
Cdd:COG2159   168 lPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPP-EALEALE 227
                         250       260
                  ....*....|....*....|....*.
gi 2462570040 249 SMEEFDEETKNKLKAGNALAFLGLER 274
Cdd:COG2159   228 ELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
26-272 1.50e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 149.60  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  26 AKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYA 104
Cdd:pfam04909  50 ARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 105 AAERLKCSLFVHPwdmqmdgrmakywlpwLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM 184
Cdd:pfam04909 130 ALEELGLPVDIHT----------------GFGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALAL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 185 ---RP----DLCAqdnpmnpkkYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF---- 253
Cdd:pfam04909 194 larRPnvyvKLSG---------LYRDLYFDAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllal 264
                         250
                  ....*....|....*....
gi 2462570040 254 DEETKNKLKAGNALAFLGL 272
Cdd:pfam04909 265 SDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
12-274 1.84e-56

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 181.72  E-value: 1.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  12 AGIQKFVLEKWTkkAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNE 91
Cdd:COG2159    23 AGIDKAVLSPTP--LADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEELERAVEELGFRGVKLHPAVGG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  92 WDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAF 171
Cdd:COG2159   101 FPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPW 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 172 -PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGElEPGKLIE 248
Cdd:COG2159   168 lPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADRILFGSDYPHWDPP-EALEALE 227
                         250       260
                  ....*....|....*....|....*.
gi 2462570040 249 SMEEFDEETKNKLKAGNALAFLGLER 274
Cdd:COG2159   228 ELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
26-272 1.50e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 149.60  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040  26 AKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYA 104
Cdd:pfam04909  50 ARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 105 AAERLKCSLFVHPwdmqmdgrmakywlpwLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM 184
Cdd:pfam04909 130 ALEELGLPVDIHT----------------GFGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALAL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462570040 185 ---RP----DLCAqdnpmnpkkYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF---- 253
Cdd:pfam04909 194 larRPnvyvKLSG---------LYRDLYFDAPLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllal 264
                         250
                  ....*....|....*....
gi 2462570040 254 DEETKNKLKAGNALAFLGL 272
Cdd:pfam04909 265 SDEEREKILGGNAARLYGL 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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