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Conserved domains on  [gi|838567150|gb|KLV51675|]
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hypothetical protein SK34_04466 [Citrobacter sp. MGH104]

Protein Classification

carboxymuconolactone decarboxylase family protein( domain architecture ID 10001777)

carboxymuconolactone decarboxylase (CMD) family protein similar to alkyl hydroperoxide reductase AhpD, which is required for the reduction of the AhpC active site cysteine residues to regenerate its enzyme activity; carboxymuconolactone d

CATH:  1.20.1290.10
Gene Ontology:  GO:0051920
PubMed:  9495744
SCOP:  4000771

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 45-156 1.32e-35

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


:

Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150  45 QKMLQQVDgKGGEAVVESLKDIAPDFARYLlEFPFGDIYARPGLDLRSREIATVAALTAMGnAAPQLKVHIGAALHVGLT 124
Cdd:COG0599    1 EEVLKEVE-EYVPRALEALAEFAPEFAEAF-EALFGDVWARGALDPKTRELITLAALAALG-CEPCLKAHVRAALNAGAT 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 838567150 125 QDEIVEVIMQMAVYAGFPAALNGLFAAKEVFA 156
Cdd:COG0599   78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 45-156 1.32e-35

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150  45 QKMLQQVDgKGGEAVVESLKDIAPDFARYLlEFPFGDIYARPGLDLRSREIATVAALTAMGnAAPQLKVHIGAALHVGLT 124
Cdd:COG0599    1 EEVLKEVE-EYVPRALEALAEFAPEFAEAF-EALFGDVWARGALDPKTRELITLAALAALG-CEPCLKAHVRAALNAGAT 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 838567150 125 QDEIVEVIMQMAVYAGFPAALNGLFAAKEVFA 156
Cdd:COG0599   78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
 37-157 1.61e-24

4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone decarboxylase, which catalyzes the third step in the catabolism of protocatechuate (and therefore the fourth step in the catabolism of para-hydroxybenzoate, of 3-hydroxybenzoate, of vanillate, etc.). Most members of this family are encoded within protocatechuate catabolism operons. This protein is sometimes found as a fusion protein with other enzymes of the pathway, as in Rhodococcus opacus, Streptomyces avermitilis, and Caulobacter crescentus. [Energy metabolism, Other]


Pssm-ID: 131478  Cd Length: 123  Bit Score: 91.74  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150   37 ESERFITGQKMLQQVDGKGG-EAVVESLKDIAPDFARYLLEFPFGDIYARPGLDLRSREIATVAALTAMGNAApQLKVHI 115
Cdd:TIGR02425   1 EQERYEQGMQVRRAVLGDAHvDRALAATTDFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDE-ELAMHV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 838567150  116 GAALHVGLTQDEIVEVIMQMAVYAGFPAALNGLFAAKEVFAS 157
Cdd:TIGR02425  80 RATANTGVTEDDIKEVLLHVAIYAGVPAANHAFALAKEALAE 121
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 68-153 3.08e-21

Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1.44 is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway. In these bifunctional proteins CMD represents the C-terminal domain, pfam00561 represents the N-terminal domain.


Pssm-ID: 460628 [Multi-domain]  Cd Length: 84  Bit Score: 81.97  E-value: 3.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150   68 PDFARYLLEFPFGDIYArPGLDLRSREIATVAALTAMGnAAPQLKVHIGAALHVGLTQDEIVEVIMQMAVYAGFPAALNG 147
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANG-CAYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAA 78


                  ....*.
gi 838567150  148 LFAAKE 153
Cdd:pfam02627  79 LAAAEE 84
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 45-156 1.32e-35

Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family [General function prediction only];


Pssm-ID: 440364  Cd Length: 114  Bit Score: 119.67  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150  45 QKMLQQVDgKGGEAVVESLKDIAPDFARYLlEFPFGDIYARPGLDLRSREIATVAALTAMGnAAPQLKVHIGAALHVGLT 124
Cdd:COG0599    1 EEVLKEVE-EYVPRALEALAEFAPEFAEAF-EALFGDVWARGALDPKTRELITLAALAALG-CEPCLKAHVRAALNAGAT 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 838567150 125 QDEIVEVIMQMAVYAGFPAALNGLFAAKEVFA 156
Cdd:COG0599   78 REEIAEALLVAAVYAGFPAALNALRAALEVLE 109
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
 37-157 1.61e-24

4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone decarboxylase, which catalyzes the third step in the catabolism of protocatechuate (and therefore the fourth step in the catabolism of para-hydroxybenzoate, of 3-hydroxybenzoate, of vanillate, etc.). Most members of this family are encoded within protocatechuate catabolism operons. This protein is sometimes found as a fusion protein with other enzymes of the pathway, as in Rhodococcus opacus, Streptomyces avermitilis, and Caulobacter crescentus. [Energy metabolism, Other]


Pssm-ID: 131478  Cd Length: 123  Bit Score: 91.74  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150   37 ESERFITGQKMLQQVDGKGG-EAVVESLKDIAPDFARYLLEFPFGDIYARPGLDLRSREIATVAALTAMGNAApQLKVHI 115
Cdd:TIGR02425   1 EQERYEQGMQVRRAVLGDAHvDRALAATTDFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDE-ELAMHV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 838567150  116 GAALHVGLTQDEIVEVIMQMAVYAGFPAALNGLFAAKEVFAS 157
Cdd:TIGR02425  80 RATANTGVTEDDIKEVLLHVAIYAGVPAANHAFALAKEALAE 121
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 68-153 3.08e-21

Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1.44 is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway. In these bifunctional proteins CMD represents the C-terminal domain, pfam00561 represents the N-terminal domain.


Pssm-ID: 460628 [Multi-domain]  Cd Length: 84  Bit Score: 81.97  E-value: 3.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838567150   68 PDFARYLLEFPFGDIYArPGLDLRSREIATVAALTAMGnAAPQLKVHIGAALHVGLTQDEIVEVIMQMAVYAGFPAALNG 147
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANG-CAYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAA 78


                  ....*.
gi 838567150  148 LFAAKE 153
Cdd:pfam02627  79 LAAAEE 84
 
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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