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Conserved domains on  [gi|51872137|gb|AAU12178|]
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uracil-5-carboxylate decarboxylase [Neurospora crassa]

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 ...
78-390 4.93e-23

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 96.97  E-value: 4.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137  78 HYSSLNQKMHFMETHEIDISVVSlANPWLDFlsasEAGPIAESINADFSRMCEEKCGRLFFFAALPLTAPRDVIlASIAH 157
Cdd:COG2159   9 HLGTPEERLADMDEAGIDKAVLS-PTPLADP----ELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAV-EELER 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 158 VSNLPYCRGVILGTSGLGKGLDDPDLLPVFHALADAKLMIFLHPhyglpnevwgprakenyGHVLPLALGFPMEttiAVT 237
Cdd:COG2159  83 AVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHP-----------------GTPPGPPPGLDLY---YAA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 238 RMYLAGVFDQVPKLNMLLAHSGGT-LPFLAGRIescilhdghlhsaAGTKPKktiwevlssqIYLD--AVVYSDVGLKAA 314
Cdd:COG2159 143 PLILSGVAERFPDLKFILAHGGGPwLPELLGRL-------------LKRLPN----------VYFDtsGVFPRPEALREL 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51872137 315 VQASGPEgheRLMFGTDHPFFPPlgSDEEGEWESVTWNGAAVRKAfgaedgedseegkkvrgVMGANAVRVLNLRR 390
Cdd:COG2159 200 LETLGAD---RILFGSDYPHWDP--PEALEALEELPGLSEEDREK-----------------ILGGNAARLLGLDA 253
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
78-390 4.93e-23

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 96.97  E-value: 4.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137  78 HYSSLNQKMHFMETHEIDISVVSlANPWLDFlsasEAGPIAESINADFSRMCEEKCGRLFFFAALPLTAPRDVIlASIAH 157
Cdd:COG2159   9 HLGTPEERLADMDEAGIDKAVLS-PTPLADP----ELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAV-EELER 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 158 VSNLPYCRGVILGTSGLGKGLDDPDLLPVFHALADAKLMIFLHPhyglpnevwgprakenyGHVLPLALGFPMEttiAVT 237
Cdd:COG2159  83 AVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHP-----------------GTPPGPPPGLDLY---YAA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 238 RMYLAGVFDQVPKLNMLLAHSGGT-LPFLAGRIescilhdghlhsaAGTKPKktiwevlssqIYLD--AVVYSDVGLKAA 314
Cdd:COG2159 143 PLILSGVAERFPDLKFILAHGGGPwLPELLGRL-------------LKRLPN----------VYFDtsGVFPRPEALREL 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51872137 315 VQASGPEgheRLMFGTDHPFFPPlgSDEEGEWESVTWNGAAVRKAfgaedgedseegkkvrgVMGANAVRVLNLRR 390
Cdd:COG2159 200 LETLGAD---RILFGSDYPHWDP--PEALEALEELPGLSEEDREK-----------------ILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
106-388 2.43e-15

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 75.65  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   106 LDFLSASEAGPIAESINADFSRMCEEKCGRLFFFAALPLTAPRDVILASIAHVSNLpYCRGVILGTS-GLGKGLDDPDLL 184
Cdd:pfam04909  47 LGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERAVGEA-GFRGVRLNPHpGGDPLLGDRLDR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   185 PVFHALADAKLMIFLHPHyglpnevwgprakenyghvlplaLGFPMETTIAVTRMYLAGVFDQVPKLNMLLAHSGGTLPF 264
Cdd:pfam04909 126 PIYEALEELGLPVDIHTG-----------------------FGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   265 LAGRIEScilHDGHLHSAAGTKPKKTIWEVLSsqiYLDAVVYSDVGLKAAVQASGPeghERLMFGTDHPFFPPlgsdeeg 344
Cdd:pfam04909 183 EGLDDPA---ALALLARRPNVYVKLSGLYRDL---YFDAPLADRPYLARLLEAFGP---DRILFGSDWPHPPL------- 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 51872137   345 EWESVTWNGAAVRKAFGAEDGEdseegkkVRGVMGANAVRVLNL 388
Cdd:pfam04909 247 EISPDDGVLLDLPLLLALSDEE-------REKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
78-390 4.93e-23

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 96.97  E-value: 4.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137  78 HYSSLNQKMHFMETHEIDISVVSlANPWLDFlsasEAGPIAESINADFSRMCEEKCGRLFFFAALPLTAPRDVIlASIAH 157
Cdd:COG2159   9 HLGTPEERLADMDEAGIDKAVLS-PTPLADP----ELAALARAANDWLAELVARYPDRFIGFATVDPQDPDAAV-EELER 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 158 VSNLPYCRGVILGTSGLGKGLDDPDLLPVFHALADAKLMIFLHPhyglpnevwgprakenyGHVLPLALGFPMEttiAVT 237
Cdd:COG2159  83 AVEELGFRGVKLHPAVGGFPLDDPRLDPLYEAAAELGLPVLVHP-----------------GTPPGPPPGLDLY---YAA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137 238 RMYLAGVFDQVPKLNMLLAHSGGT-LPFLAGRIescilhdghlhsaAGTKPKktiwevlssqIYLD--AVVYSDVGLKAA 314
Cdd:COG2159 143 PLILSGVAERFPDLKFILAHGGGPwLPELLGRL-------------LKRLPN----------VYFDtsGVFPRPEALREL 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51872137 315 VQASGPEgheRLMFGTDHPFFPPlgSDEEGEWESVTWNGAAVRKAfgaedgedseegkkvrgVMGANAVRVLNLRR 390
Cdd:COG2159 200 LETLGAD---RILFGSDYPHWDP--PEALEALEELPGLSEEDREK-----------------ILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
106-388 2.43e-15

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 75.65  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   106 LDFLSASEAGPIAESINADFSRMCEEKCGRLFFFAALPLTAPRDVILASIAHVSNLpYCRGVILGTS-GLGKGLDDPDLL 184
Cdd:pfam04909  47 LGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERAVGEA-GFRGVRLNPHpGGDPLLGDRLDR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   185 PVFHALADAKLMIFLHPHyglpnevwgprakenyghvlplaLGFPMETTIAVTRMYLAGVFDQVPKLNMLLAHSGGTLPF 264
Cdd:pfam04909 126 PIYEALEELGLPVDIHTG-----------------------FGDRPEDTRAIQPLLLAGVARKFPDLKIVLDHGGGPWIP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51872137   265 LAGRIEScilHDGHLHSAAGTKPKKTIWEVLSsqiYLDAVVYSDVGLKAAVQASGPeghERLMFGTDHPFFPPlgsdeeg 344
Cdd:pfam04909 183 EGLDDPA---ALALLARRPNVYVKLSGLYRDL---YFDAPLADRPYLARLLEAFGP---DRILFGSDWPHPPL------- 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 51872137   345 EWESVTWNGAAVRKAFGAEDGEdseegkkVRGVMGANAVRVLNL 388
Cdd:pfam04909 247 EISPDDGVLLDLPLLLALSDEE-------REKILGGNAARLYGL 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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