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Protein

2-halobenzoate 1,2-dioxygenase electron transfer component

Gene

cbdC

Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity

Pathwayi: benzoate degradation via CoA ligation

This protein is involved in the pathway benzoate degradation via CoA ligation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway benzoate degradation via CoA ligation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi45 – 451Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi48 – 481Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi80 – 801Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14765.
UniPathwayiUPA00233.

Names & Taxonomyi

Protein namesi
Recommended name:
2-halobenzoate 1,2-dioxygenase electron transfer component
Including the following 2 domains:
Ferredoxin
Ferredoxin--NAD(+) reductase (EC:1.18.1.3)
Gene namesi
Name:cbdC
Encoded oniPlasmid pBAH10 Publication
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3393392-halobenzoate 1,2-dioxygenase electron transfer componentPRO_0000167656Add
BLAST

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ51603.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 96942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini103 – 203101FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 336239Ferredoxin-reductaseAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q51603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHSIALRFE DDVTYFITSS EHETVADAAY QHGIRIPLDC RNGVCGTCKG
60 70 80 90 100
FCEHGEYDGG DYIEDALSAD EAREGFVLPC QMQARTDCVV RILASSSACQ
110 120 130 140 150
VKKSTMTGQM TEIDRGSSST LQFTLAIDPS SKVDFLPGQY AQLRIPGTTE
160 170 180 190 200
SRAYSYSSMP GSSHVTFLVR DVPNGKMSGY LRNQATITET FTFDGPYGAF
210 220 230 240 250
YLREPVRPIL MLAGGTGLAP FLSMLQYMAG LQRNDLPSVR LVYGVNRDDD
260 270 280 290 300
LVGLDKLDEL ATQLSGFSYI TTVVDKDSAQ LRRGYVTQQI TNDDMNGGDV
310 320 330
DIYVCGPPPM VEAVRSWLAA EKLNPVNFYF EKFAPTVGN
Length:339
Mass (Da):37,265
Last modified:November 1, 1996 - v1
Checksum:i075DFCC7A9F9AE63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79076 Genomic DNA. Translation: CAA55683.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79076 Genomic DNA. Translation: CAA55683.1.

3D structure databases

ProteinModelPortaliQ51603.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00233.
BioCyciMetaCyc:MONOMER-14765.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19, CHARACTERIZATION.
    Strain: 2CBS.

Entry informationi

Entry nameiCBDC_BURCE
AccessioniPrimary (citable) accession number: Q51603
Secondary accession number(s): O08068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.