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Conserved domains on  [gi|109715856|ref|NP_612199|]
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2-amino-3-carboxymuconate-6-semialdehyde decarboxylase isoform 1 [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

 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 ...
49-332 3.87e-62

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 198.28  E-value: 3.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  49 VRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKpedtlnLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKE 128
Cdd:COG2159    6 VHTHLGTPEERLADMDEAGIDKAVLSPTPLADPELAA------LARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 129 MERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIM 208
Cdd:COG2159   80 LERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLIL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 209 GGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDK 285
Cdd:COG2159  147 SGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADR 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 109715856 286 VILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 332
Cdd:COG2159  208 ILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
49-332 3.87e-62

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 198.28  E-value: 3.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  49 VRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKpedtlnLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKE 128
Cdd:COG2159    6 VHTHLGTPEERLADMDEAGIDKAVLSPTPLADPELAA------LARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 129 MERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIM 208
Cdd:COG2159   80 LERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLIL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 209 GGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDK 285
Cdd:COG2159  147 SGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADR 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 109715856 286 VILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 332
Cdd:COG2159  208 ILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
45-330 7.69e-47

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 160.00  E-value: 7.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856   45 VFRVVRENCWDPEVRIREMDQKGVTVQALS----TVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQ 120
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  121 APELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYAAAERLKCSLFVHPwdmqmdgrmakywlpwLVGMPAET 199
Cdd:pfam04909  87 DPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYEALEELGLPVDIHT----------------GFGDRPED 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  200 TIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM---RP----DLCAqdnpmnpkkYLGSFYTDALVHDPL 272
Cdd:pfam04909 151 TRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALALlarRPnvyvKLSG---------LYRDLYFDAPLADRP 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109715856  273 SLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF----DEETKNKLKAGNALAFLGL 330
Cdd:pfam04909 222 YLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
49-332 3.87e-62

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 198.28  E-value: 3.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  49 VRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKpedtlnLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKE 128
Cdd:COG2159    6 VHTHLGTPEERLADMDEAGIDKAVLSPTPLADPELAA------LARAANDWLAELVARYPDRFIGFATVDPQDPDAAVEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 129 MERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICSMIM 208
Cdd:COG2159   80 LERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAPLIL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856 209 GGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIGKDK 285
Cdd:COG2159  147 SGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLGADR 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 109715856 286 VILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 332
Cdd:COG2159  208 ILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
45-330 7.69e-47

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 160.00  E-value: 7.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856   45 VFRVVRENCWDPEVRIREMDQKGVTVQALS----TVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQ 120
Cdd:pfam04909   7 LWPDDERIGFDPGGRLPFMKRRGYDPRDASpedlLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  121 APELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYAAAERLKCSLFVHPwdmqmdgrmakywlpwLVGMPAET 199
Cdd:pfam04909  87 DPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYEALEELGLPVDIHT----------------GFGDRPED 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109715856  200 TIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM---RP----DLCAqdnpmnpkkYLGSFYTDALVHDPL 272
Cdd:pfam04909 151 TRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALALlarRPnvyvKLSG---------LYRDLYFDAPLADRP 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109715856  273 SLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF----DEETKNKLKAGNALAFLGL 330
Cdd:pfam04909 222 YLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 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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