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Conserved domains on  [gi|530369028|ref|XP_005263643|]
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2-amino-3-carboxymuconate-6-semialdehyde decarboxylase isoform X1 [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 ...
1-283 1.62e-57

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 184.80  E-value: 1.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028   1 MKIDIHSHIlpkewPDLKKRFGY----GGWVQLQHHSKAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELA 76
Cdd:COG2159    2 MIIDVHTHL-----GTPEERLADmdeaGIDKAVLSPTPLADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028  77 VKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICS 156
Cdd:COG2159   77 VEELERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028 157 MIMGGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIG 233
Cdd:COG2159  144 LILSGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLG 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530369028 234 KDKVILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 283
Cdd:COG2159  205 ADRILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-283 1.62e-57

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 184.80  E-value: 1.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028   1 MKIDIHSHIlpkewPDLKKRFGY----GGWVQLQHHSKAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELA 76
Cdd:COG2159    2 MIIDVHTHL-----GTPEERLADmdeaGIDKAVLSPTPLADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028  77 VKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICS 156
Cdd:COG2159   77 VEELERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028 157 MIMGGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIG 233
Cdd:COG2159  144 LILSGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLG 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530369028 234 KDKVILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 283
Cdd:COG2159  205 ADRILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
3-281 4.88e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 148.45  E-value: 4.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028    3 IDIHSHILP-----KEWPDLKKRFGYGGWVQLQHHS------------KAKPEDTLNLCQLLNNDLASTVVSYPRRFVGL 65
Cdd:pfam04909   1 IDAHAHLWPdderiGFDPGGRLPFMKRRGYDPRDASpedllalgaalgVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028   66 GTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYAAAERLKCSLFVHPwdmqmdgrmakywlpwLV 144
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYEALEELGLPVDIHT----------------GF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028  145 GMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM---RP----DLCAqdnpmnpkkYLGSFYTDA 217
Cdd:pfam04909 145 GDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALALlarRPnvyvKLSG---------LYRDLYFDA 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530369028  218 LVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF----DEETKNKLKAGNALAFLGL 281
Cdd:pfam04909 216 PLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-283 1.62e-57

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 184.80  E-value: 1.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028   1 MKIDIHSHIlpkewPDLKKRFGY----GGWVQLQHHSKAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELA 76
Cdd:COG2159    2 MIIDVHTHL-----GTPEERLADmdeaGIDKAVLSPTPLADPELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028  77 VKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMqmdgrmakywlpwLVGMPAETTIAICS 156
Cdd:COG2159   77 VEELERAVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHPGTP-------------PGPPPGLDLYYAAP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028 157 MIMGGVFEKFPKLKVCFAHGGGAF-PFTVGRIshgfsmrpdlcAQDNPmnpkkylgSFYTD--ALVHDPLSLKLLTDVIG 233
Cdd:COG2159  144 LILSGVAERFPDLKFILAHGGGPWlPELLGRL-----------LKRLP--------NVYFDtsGVFPRPEALRELLETLG 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530369028 234 KDKVILGTDYPFPLGElEPGKLIESMEEFDEETKNKLKAGNALAFLGLER 283
Cdd:COG2159  205 ADRILFGSDYPHWDPP-EALEALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
3-281 4.88e-43

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 148.45  E-value: 4.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028    3 IDIHSHILP-----KEWPDLKKRFGYGGWVQLQHHS------------KAKPEDTLNLCQLLNNDLASTVVSYPRRFVGL 65
Cdd:pfam04909   1 IDAHAHLWPdderiGFDPGGRLPFMKRRGYDPRDASpedllalgaalgVARAVVVAASCRGANNRVAAEALARPGRFLGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028   66 GTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELF-PVYAAAERLKCSLFVHPwdmqmdgrmakywlpwLV 144
Cdd:pfam04909  81 VAVVPLDPEDAAAELERAVGEAGFRGVRLNPHPGGDPLLGDRLDrPIYEALEELGLPVDIHT----------------GF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530369028  145 GMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSM---RP----DLCAqdnpmnpkkYLGSFYTDA 217
Cdd:pfam04909 145 GDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAALALlarRPnvyvKLSG---------LYRDLYFDA 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530369028  218 LVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEF----DEETKNKLKAGNALAFLGL 281
Cdd:pfam04909 216 PLADRPYLARLLEAFGPDRILFGSDWPHPPLEISPDDGVLLDLPLllalSDEEREKILGGNAARLYGL 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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