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Conserved domains on  [gi|1184523206|ref|WP_085093215|]
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amidohydrolase family protein [Mycobacterium paraense]

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 ...
85-377 1.06e-38

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 140.12  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206  85 YNVDERIKDMNAGGILASICFPSFPGFAGRLfatedhdfsiSLVQAYNDWHIdEWCGAYPARFIPMAIPVIWDAEACAAE 164
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLADPELA----------ALARAANDWLA-ELVARYPDRFIGFATVDPQDPDAAVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 165 VRR-VSKKGVHALTFteNPAAMGYPsFHDEYWNPLWKALCDTNTVMNVHIGSSGRLAITAPDAPMDVMItlqpmnivqaa 243
Cdd:COG2159    80 LERaVEELGFRGVKL--HPAVGGFP-LDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLI----------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 244 adllWSRPIKEYPDLKIALSEGGTGWIPYFLERAdrtfemhsAWTHQNFggklpsdvfrehFLTCFISDKVGVALR---N 320
Cdd:COG2159   146 ----LSGVAERFPDLKFILAHGGGPWLPELLGRL--------LKRLPNV------------YFDTSGVFPRPEALRellE 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184523206 321 MIGIDNIAWEADYPHSDSMWPGApeelwDVLSLNNVPDDEINKMAYENAMRWYSFDP 377
Cdd:COG2159   202 TLGADRILFGSDYPHWDPPEALE-----ALEELPGLSEEDREKILGGNAARLLGLDA 253
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
85-377 1.06e-38

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 140.12  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206  85 YNVDERIKDMNAGGILASICFPSFPGFAGRLfatedhdfsiSLVQAYNDWHIdEWCGAYPARFIPMAIPVIWDAEACAAE 164
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLADPELA----------ALARAANDWLA-ELVARYPDRFIGFATVDPQDPDAAVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 165 VRR-VSKKGVHALTFteNPAAMGYPsFHDEYWNPLWKALCDTNTVMNVHIGSSGRLAITAPDAPMDVMItlqpmnivqaa 243
Cdd:COG2159    80 LERaVEELGFRGVKL--HPAVGGFP-LDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLI----------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 244 adllWSRPIKEYPDLKIALSEGGTGWIPYFLERAdrtfemhsAWTHQNFggklpsdvfrehFLTCFISDKVGVALR---N 320
Cdd:COG2159   146 ----LSGVAERFPDLKFILAHGGGPWLPELLGRL--------LKRLPNV------------YFDTSGVFPRPEALRellE 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184523206 321 MIGIDNIAWEADYPHSDSMWPGApeelwDVLSLNNVPDDEINKMAYENAMRWYSFDP 377
Cdd:COG2159   202 TLGADRILFGSDYPHWDPPEALE-----ALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
88-375 3.73e-32

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 123.41  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206  88 DERIKDMNAGGILASICFPSFPGFAGRLFATEDHDFSISLVQAYNDWHIDEWCGAYPARFIPMAIPVIWDAEACAAEVRR 167
Cdd:pfam04909  19 GGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 168 VSKKGVHALTFteNPAAMGYPSFHDEYWNPLWKALCDTNTVMNVHIGSSGRLAITAPDAPMDVmitlqpmnivqaaadll 247
Cdd:pfam04909  99 VGEAGFRGVRL--NPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAIQPLLL----------------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 248 wSRPIKEYPDLKIALSEGGTGWIPYFLERADrtfEMHSAWTHQNFGGKLPSDVFREHFLTCFISDKVGVALRNMIGIDNI 327
Cdd:pfam04909 160 -AGVARKFPDLKIVLDHGGGPWIPEGLDDPA---ALALLARRPNVYVKLSGLYRDLYFDAPLADRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1184523206 328 AWEADYPHSDSMWPGAPEELWDVLSLNNVPDDEINKMAYENAMRWYSF 375
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
85-377 1.06e-38

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 140.12  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206  85 YNVDERIKDMNAGGILASICFPSFPGFAGRLfatedhdfsiSLVQAYNDWHIdEWCGAYPARFIPMAIPVIWDAEACAAE 164
Cdd:COG2159    11 GTPEERLADMDEAGIDKAVLSPTPLADPELA----------ALARAANDWLA-ELVARYPDRFIGFATVDPQDPDAAVEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 165 VRR-VSKKGVHALTFteNPAAMGYPsFHDEYWNPLWKALCDTNTVMNVHIGSSGRLAITAPDAPMDVMItlqpmnivqaa 243
Cdd:COG2159    80 LERaVEELGFRGVKL--HPAVGGFP-LDDPRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLI----------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 244 adllWSRPIKEYPDLKIALSEGGTGWIPYFLERAdrtfemhsAWTHQNFggklpsdvfrehFLTCFISDKVGVALR---N 320
Cdd:COG2159   146 ----LSGVAERFPDLKFILAHGGGPWLPELLGRL--------LKRLPNV------------YFDTSGVFPRPEALRellE 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184523206 321 MIGIDNIAWEADYPHSDSMWPGApeelwDVLSLNNVPDDEINKMAYENAMRWYSFDP 377
Cdd:COG2159   202 TLGADRILFGSDYPHWDPPEALE-----ALEELPGLSEEDREKILGGNAARLLGLDA 253
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
88-375 3.73e-32

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 123.41  E-value: 3.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206  88 DERIKDMNAGGILASICFPSFPGFAGRLFATEDHDFSISLVQAYNDWHIDEWCGAYPARFIPMAIPVIWDAEACAAEVRR 167
Cdd:pfam04909  19 GGRLPFMKRRGYDPRDASPEDLLALGAALGVARAVVVAASCRGANNRVAAEALARPGRFLGGVAVVPLDPEDAAAELERA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 168 VSKKGVHALTFteNPAAMGYPSFHDEYWNPLWKALCDTNTVMNVHIGSSGRLAITAPDAPMDVmitlqpmnivqaaadll 247
Cdd:pfam04909  99 VGEAGFRGVRL--NPHPGGDPLLGDRLDRPIYEALEELGLPVDIHTGFGDRPEDTRAIQPLLL----------------- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523206 248 wSRPIKEYPDLKIALSEGGTGWIPYFLERADrtfEMHSAWTHQNFGGKLPSDVFREHFLTCFISDKVGVALRNMIGIDNI 327
Cdd:pfam04909 160 -AGVARKFPDLKIVLDHGGGPWIPEGLDDPA---ALALLARRPNVYVKLSGLYRDLYFDAPLADRPYLARLLEAFGPDRI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1184523206 328 AWEADYPHSDSMWPGAPEELWDVLSLNNVPDDEINKMAYENAMRWYSF 375
Cdd:pfam04909 236 LFGSDWPHPPLEISPDDGVLLDLPLLLALSDEEREKILGGNAARLYGL 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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