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Q51603 (CBDC_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-halobenzoate 1,2-dioxygenase electron transfer component

Including the following 2 domains:

  1. Ferredoxin
  2. Ferredoxin--NAD(+) reductase
    EC=1.18.1.3
Gene names
Name:cbdC
Encoded onPlasmid pBAH1
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron transfer component of 2-halobenzoate 1,2-dioxygenase system.

Catalytic activity

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactor

Binds 1 FAD per subunit By similarity.

Binds 1 2Fe-2S cluster per subunit By similarity.

Pathway

Xenobiotic degradation; benzoate degradation via CoA ligation.

Subunit structure

Monomer. It is part of 2-halobenzoate dioxygenase two component enzyme system. The other component is a dioxygenase component consisting of 3 large (CbdA) subunits and 3 small (CbdB) subunits.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3393392-halobenzoate 1,2-dioxygenase electron transfer component
PRO_0000167656

Regions

Domain3 – 96942Fe-2S ferredoxin-type
Domain103 – 203101FAD-binding FR-type
Region98 – 336239Ferredoxin-reductase

Sites

Metal binding401Iron-sulfur (2Fe-2S) By similarity
Metal binding451Iron-sulfur (2Fe-2S) By similarity
Metal binding481Iron-sulfur (2Fe-2S) By similarity
Metal binding801Iron-sulfur (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q51603 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 075DFCC7A9F9AE63

FASTA33937,265
        10         20         30         40         50         60 
MLHSIALRFE DDVTYFITSS EHETVADAAY QHGIRIPLDC RNGVCGTCKG FCEHGEYDGG 

        70         80         90        100        110        120 
DYIEDALSAD EAREGFVLPC QMQARTDCVV RILASSSACQ VKKSTMTGQM TEIDRGSSST 

       130        140        150        160        170        180 
LQFTLAIDPS SKVDFLPGQY AQLRIPGTTE SRAYSYSSMP GSSHVTFLVR DVPNGKMSGY 

       190        200        210        220        230        240 
LRNQATITET FTFDGPYGAF YLREPVRPIL MLAGGTGLAP FLSMLQYMAG LQRNDLPSVR 

       250        260        270        280        290        300 
LVYGVNRDDD LVGLDKLDEL ATQLSGFSYI TTVVDKDSAQ LRRGYVTQQI TNDDMNGGDV 

       310        320        330 
DIYVCGPPPM VEAVRSWLAA EKLNPVNFYF EKFAPTVGN 

« Hide

References

[1]"Cloning, nucleotide sequence, and expression of the plasmid-encoded genes for the two-component 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS."
Haak B., Fetzner S., Lingens F.
J. Bacteriol. 177:667-675(1995) [PubMed: 7530709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 2CBS.
[2]"Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a two-component enzyme system from Pseudomonas cepacia 2CBS."
Fetzner S., Mueller R., Lingens F.
J. Bacteriol. 174:279-290(1992) [PubMed: 1370284] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19, CHARACTERIZATION.
Strain: 2CBS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79076 Genomic DNA. Translation: CAA55683.1.

3D structure databases

ProteinModelPortalQ51603.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14765.

Family and domain databases

InterProIPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_ferredoxin-type.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001041. Ferredoxin.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMSSF54292. Ferredoxin. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBDC_BURCE
AccessionPrimary (citable) accession number: Q51603
Secondary accession number(s): O08068
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families