Reviewed, UniProtKB/Swiss-Prot Q51603 (CBDC_BURCE)

Names and origin

Protein names

Recommended name:
    2-halobenzoate 1,2-dioxygenase electron transfer component
Including 2 domains:
  Recommended name:
      Ferredoxin
  Recommended name:
      Ferredoxin--NAD(+) reductase
      EC=1.18.1.3

Gene names

Name:

cbdC

Encoded on

Plasmid pBAH1

Organism

Burkholderia cepacia (Pseudomonas cepacia)

Taxonomic identifier

292 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Molecular function	ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 339	339	2-halobenzoate 1,2-dioxygenase electron transfer component
Regions
	Domain	3 – 96	94	2Fe-2S ferredoxin-type
	Domain	103 – 203	101	FAD-binding FR-type
	Region	98 – 336	239	Ferredoxin-reductase
Sites
	Metal binding	40	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	80	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q51603-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 075DFCC7A9F9AE63	FASTA	339	37,265
	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79076 Genomic DNA. Translation: CAA55683.1.
3D structure databases
HSSP	HSSP built from PDB template 1KRH based on UniProtKB P07771.
ModBase	Search...
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR001709. FPN_cyt_redctse. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProDom	Q51603. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

CBDC_BURCE

Accession

Primary (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:	July 22, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)