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Conserved domains on  [gi|518516655|ref|WP_019686862|]
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MULTISPECIES: carboxymuconolactone decarboxylase family protein [Paenibacillus]

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 ...
7-111 4.16e-33

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


:

Pssm-ID: 440364  Cd Length: 114  Bit Score: 111.20  E-value: 4.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   7 RSSVRETIGDLAPAFVSYTEEvLFGDVWRRSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLA 86
Cdd:COG0599   11 VPRALEALAEFAPEFAEAFEA-LFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAGATREEIAEALLVAA 89
                         90       100
                 ....*....|....*....|....*
gi 518516655  87 FYVGWPRAASAVQVAKDVFCKEKER 111
Cdd:COG0599   90 VYAGFPAALNALRAALEVLEELGAA 114
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
7-111 4.16e-33

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


Pssm-ID: 440364  Cd Length: 114  Bit Score: 111.20  E-value: 4.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   7 RSSVRETIGDLAPAFVSYTEEvLFGDVWRRSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLA 86
Cdd:COG0599   11 VPRALEALAEFAPEFAEAFEA-LFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAGATREEIAEALLVAA 89
                         90       100
                 ....*....|....*....|....*
gi 518516655  87 FYVGWPRAASAVQVAKDVFCKEKER 111
Cdd:COG0599   90 VYAGFPAALNALRAALEVLEELGAA 114
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
19-103 5.41e-23

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: 84.67  E-value: 5.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   19 PAFVSYTEEVLFGDVWRrSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLAFYVGWPRAASAV 98
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGCAYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAAL 79

                  ....*
gi 518516655   99 QVAKD 103
Cdd:pfam02627  80 AAAEE 84
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
16-105 4.65e-18

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: 73.25  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   16 DLAPAFVSYTEEVLFGDVWRRSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLAFYVGWPRAA 95
Cdd:TIGR02425  30 DFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDEELAMHVRATANTGVTEDDIKEVLLHVAIYAGVPAAN 109
                          90
                  ....*....|
gi 518516655   96 SAVQVAKDVF 105
Cdd:TIGR02425 110 HAFALAKEAL 119
 
Name Accession Description Interval E-value
YurZ COG0599
Uncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone ...
7-111 4.16e-33

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


Pssm-ID: 440364  Cd Length: 114  Bit Score: 111.20  E-value: 4.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   7 RSSVRETIGDLAPAFVSYTEEvLFGDVWRRSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLA 86
Cdd:COG0599   11 VPRALEALAEFAPEFAEAFEA-LFGDVWARGALDPKTRELITLAALAALGCEPCLKAHVRAALNAGATREEIAEALLVAA 89
                         90       100
                 ....*....|....*....|....*
gi 518516655  87 FYVGWPRAASAVQVAKDVFCKEKER 111
Cdd:COG0599   90 VYAGFPAALNALRAALEVLEELGAA 114
CMD pfam02627
Carboxymuconolactone decarboxylase family; Carboxymuconolactone decarboxylase (CMD) EC:4.1.1. ...
19-103 5.41e-23

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: 84.67  E-value: 5.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   19 PAFVSYTEEVLFGDVWRrSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLAFYVGWPRAASAV 98
Cdd:pfam02627   1 PELLAALTALAFGLLWD-GGLDPKTRELIALAVSAANGCAYCLDAHTRAALKAGVTEEEIAEVLAWAAAYAGGPAARAAL 79

                  ....*
gi 518516655   99 QVAKD 103
Cdd:pfam02627  80 AAAEE 84
decarb_PcaC TIGR02425
4-carboxymuconolactone decarboxylase; Members of this family are 4-carboxymuconolactone ...
16-105 4.65e-18

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: 73.25  E-value: 4.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518516655   16 DLAPAFVSYTEEVLFGDVWRRSELSLRERSLITVATLVAGEHVNQLPYHLNLAKENGISEEELIEVITQLAFYVGWPRAA 95
Cdd:TIGR02425  30 DFDQPFQELITEYAWGTVWTRPGLTKRERSLVTIALLAALGRDEELAMHVRATANTGVTEDDIKEVLLHVAIYAGVPAAN 109
                          90
                  ....*....|
gi 518516655   96 SAVQVAKDVF 105
Cdd:TIGR02425 110 HAFALAKEAL 119
 
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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