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Conserved domains on  [gi|1231751501|emb|SNV91960|]
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4-carboxymuconolactone decarboxylase [Mycolicibacter terrae]

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 ...
 26-118 5.43e-19

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


:

Pssm-ID: 440364  Cd Length: 114  Bit Score: 76.53  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751501  26 EFFALTaDHLFGRIWTRPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFPLGSVLN 105
Cdd:COG0599    24 EFAEAF-EALFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAG-ATREEIAEALLVAAVYAGFPAALNAL 101

                          90
                  ....*....|...
gi 1231751501 106 SVVEQVIAKRSKA 118
Cdd:COG0599   102 RAALEVLEELGAA 114
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 26-118 5.43e-19

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


Pssm-ID: 440364  Cd Length: 114  Bit Score: 76.53  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751501  26 EFFALTaDHLFGRIWTRPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFPLGSVLN 105
Cdd:COG0599    24 EFAEAF-EALFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAG-ATREEIAEALLVAAVYAGFPAALNAL 101

                          90
                  ....*....|...
gi 1231751501 106 SVVEQVIAKRSKA 118
Cdd:COG0599   102 RAALEVLEELGAA 114
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
 22-116 1.33e-12

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: 60.53  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751501  22 DMPGEFFALTADHLFGRIWTRPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFPLG 101
Cdd:TIGR02425  30 DFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDEELAMHVRATANTG-VTEDDIKEVLLHVAIYAGVPAA 108

                          90
                  ....*....|....*
gi 1231751501 102 SVLNSVVEQVIAKRS 116
Cdd:TIGR02425 109 NHAFALAKEALAEMA 123
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 26-99 8.24e-08

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: 46.92  E-value: 8.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751501  26 EFFALTADHLFGRIWTrPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFP 99
Cdd:pfam02627   2 ELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGCAYCLDAHTRAALKAG-VTEEEIAEVLAWAAAYAGGP 73
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
 26-118 5.43e-19

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


Pssm-ID: 440364  Cd Length: 114  Bit Score: 76.53  E-value: 5.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751501  26 EFFALTaDHLFGRIWTRPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFPLGSVLN 105
Cdd:COG0599    24 EFAEAF-EALFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAG-ATREEIAEALLVAAVYAGFPAALNAL 101

                          90
                  ....*....|...
gi 1231751501 106 SVVEQVIAKRSKA 118
Cdd:COG0599   102 RAALEVLEELGAA 114
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
 22-116 1.33e-12

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: 60.53  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231751501  22 DMPGEFFALTADHLFGRIWTRPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFPLG 101
Cdd:TIGR02425  30 DFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDEELAMHVRATANTG-VTEDDIKEVLLHVAIYAGVPAA 108

                          90
                  ....*....|....*
gi 1231751501 102 SVLNSVVEQVIAKRS 116
Cdd:TIGR02425 109 NHAFALAKEALAEMA 123
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
 26-99 8.24e-08

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: 46.92  E-value: 8.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231751501  26 EFFALTADHLFGRIWTrPGLSMRDKRLITLAVVTALGQKDLAGIQVNAALHNGeMTEDELREMVIFITHYVGFP 99
Cdd:pfam02627   2 ELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGCAYCLDAHTRAALKAG-VTEEEIAEVLAWAAAYAGGP 73
 
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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