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Conserved domains on  [gi|1567971815|gb|RYD93261|]
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MAG: amidohydrolase, partial [Sphingomonadales bacterium]

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 ...
1-173 1.97e-22

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


:

Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 90.04  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815   1 DPLFAAIEEAELPICFHVGewfrdgygghgTTIMVAFGGFRKNLGELIFGGIFDRHPKLQAVFLEADINWVPGALQTAsm 80
Cdd:COG2159   109 DPLYEAAAELGLPVLVHPG-----------TPPGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPWLPELLGRL-- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815  81 gyecyyemlnpkIKHHPRHYWhnnCFAAFTFDPVGLR-LLDIVGADRVLWSADYPHVEstygyGWDAIKAV--VDAVGED 157
Cdd:COG2159   176 ------------LKRLPNVYF---DTSGVFPRPEALReLLETLGADRILFGSDYPHWD-----PPEALEALeeLPGLSEE 235
                         170
                  ....*....|....*.
gi 1567971815 158 DARAILGGNAIKLFKL 173
Cdd:COG2159   236 DREKILGGNAARLLGL 251
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-173 1.97e-22

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 90.04  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815   1 DPLFAAIEEAELPICFHVGewfrdgygghgTTIMVAFGGFRKNLGELIFGGIFDRHPKLQAVFLEADINWVPGALQTAsm 80
Cdd:COG2159   109 DPLYEAAAELGLPVLVHPG-----------TPPGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPWLPELLGRL-- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815  81 gyecyyemlnpkIKHHPRHYWhnnCFAAFTFDPVGLR-LLDIVGADRVLWSADYPHVEstygyGWDAIKAV--VDAVGED 157
Cdd:COG2159   176 ------------LKRLPNVYF---DTSGVFPRPEALReLLETLGADRILFGSDYPHWD-----PPEALEALeeLPGLSEE 235
                         170
                  ....*....|....*.
gi 1567971815 158 DARAILGGNAIKLFKL 173
Cdd:COG2159   236 DREKILGGNAARLLGL 251
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
1-173 1.35e-18

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 80.27  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815   1 DPLFAAIEEAELPICFHVGEWFRDGYGGHgttIMVafggfrknlgeLIFGGIFDRHPKLQAVFLEADINWVPGALQTASM 80
Cdd:pfam04909 125 RPIYEALEELGLPVDIHTGFGDRPEDTRA---IQP-----------LLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAA 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815  81 GYECY-YEMLNPKIKHHPRHYWHNNCFAAFtfdPVGLRLLDIVGADRVLWSADYPHV--ESTYGYGWDAIKAVVDAVGED 157
Cdd:pfam04909 191 LALLArRPNVYVKLSGLYRDLYFDAPLADR---PYLARLLEAFGPDRILFGSDWPHPplEISPDDGVLLDLPLLLALSDE 267
                         170
                  ....*....|....*.
gi 1567971815 158 DARAILGGNAIKLFKL 173
Cdd:pfam04909 268 EREKILGGNAARLYGL 283
 
Name Accession Description Interval E-value
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
1-173 1.97e-22

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


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 90.04  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815   1 DPLFAAIEEAELPICFHVGewfrdgygghgTTIMVAFGGFRKNLGELIFGGIFDRHPKLQAVFLEADINWVPGALQTAsm 80
Cdd:COG2159   109 DPLYEAAAELGLPVLVHPG-----------TPPGPPPGLDLYYAAPLILSGVAERFPDLKFILAHGGGPWLPELLGRL-- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815  81 gyecyyemlnpkIKHHPRHYWhnnCFAAFTFDPVGLR-LLDIVGADRVLWSADYPHVEstygyGWDAIKAV--VDAVGED 157
Cdd:COG2159   176 ------------LKRLPNVYF---DTSGVFPRPEALReLLETLGADRILFGSDYPHWD-----PPEALEALeeLPGLSEE 235
                         170
                  ....*....|....*.
gi 1567971815 158 DARAILGGNAIKLFKL 173
Cdd:COG2159   236 DREKILGGNAARLLGL 251
Amidohydro_2 pfam04909
Amidohydrolase; These proteins are amidohydrolases that are related to pfam01979.
1-173 1.35e-18

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


Pssm-ID: 428190 [Multi-domain]  Cd Length: 283  Bit Score: 80.27  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815   1 DPLFAAIEEAELPICFHVGEWFRDGYGGHgttIMVafggfrknlgeLIFGGIFDRHPKLQAVFLEADINWVPGALQTASM 80
Cdd:pfam04909 125 RPIYEALEELGLPVDIHTGFGDRPEDTRA---IQP-----------LLLAGVARKFPDLKIVLDHGGGPWIPEGLDDPAA 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567971815  81 GYECY-YEMLNPKIKHHPRHYWHNNCFAAFtfdPVGLRLLDIVGADRVLWSADYPHV--ESTYGYGWDAIKAVVDAVGED 157
Cdd:pfam04909 191 LALLArRPNVYVKLSGLYRDLYFDAPLADR---PYLARLLEAFGPDRILFGSDWPHPplEISPDDGVLLDLPLLLALSDE 267
                         170
                  ....*....|....*.
gi 1567971815 158 DARAILGGNAIKLFKL 173
Cdd:pfam04909 268 EREKILGGNAARLYGL 283
COG3618 COG3618
Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];
113-173 7.49e-10

Predicted metal-dependent hydrolase, TIM-barrel fold [General function prediction only];


Pssm-ID: 442836 [Multi-domain]  Cd Length: 272  Bit Score: 55.99  E-value: 7.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1567971815 113 PVGLRLLDIVGADRVLWSADYPHV--ESTYGYGWDAIKAVVDAVGEDDARAILGGNAIKLFKL 173
Cdd:COG3618   208 PYARALLEAFGPDRLMWGSDWPVTllAPDYGELLDLLEELLPDLSEAERRAILGDNAARLYGL 270
 
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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