Reviewed, UniProtKB/Swiss-Prot Q51601 (CBDA_BURCE)

Names and origin

Protein names

Recommended name:
    2-halobenzoate 1,2-dioxygenase large subunit
    EC=1.14.12.13
Alternative name(s):
    2-chlorobenzoate 1,2-dioxygenase

Gene names

Name:

cbdA

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	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of 2-halobenzoate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into 2-halobenzoate to form catechol.
Catalytic activity	2-chlorobenzoate + NADH + O2 = catechol + chloride + NAD+ + CO2.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 1 Fe2+ ion per subunit By similarity.
Pathway	Xenobiotic degradation; benzoate degradation via CoA ligation.
Subunit structure	Heterohexamer of 3 large (CbdA) subunits and 3 small (CbdB) subunits. The heterohexamer is part of 2-halobenzoate dioxygenase two component enzyme system. The other component is a NADH:acceptor reductase (CdbC).
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 2-chlorobenzoate 1,2-dioxygenase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 465	464	2-halobenzoate 1,2-dioxygenase large subunit		PRO_0000085051
Regions
	Domain	56 – 154	99	Rieske
Sites
	Metal binding	98	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	100	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	118	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	121	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	227	1	Iron By similarity
	Metal binding	232	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q51601-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 08747DF6FB8D30DC	FASTA	465	52,478
	10 20 30 40 50 60 MSTPLIAGTG PSAVRQLISN AVQNDPVSGN FRCRRDIFTD AALFDYEMKY IFEQNWVFLA 70 80 90 100 110 120 HESQVANPDD YLVSNIGRQP VIITRNKAGD VSAVINACSH RGAELCRRKQ GNRSTFTCQF 130 140 150 160 170 180 HGWTFSNTGK LLKVKDGQDD NYPEGFNVDG SHDLTRIPSF ANYRGFLFGS MNPDACPIEE 190 200 210 220 230 240 HLGGSKAILD QVIDQTPGEL EVLRGSSSYI YDGNWKLQIE NGADGYHVGS VHWNYVATIG 250 260 270 280 290 300 RRDRTSDTIR TVDVTTWSKK NIGGTYTFEH GHMLLWTRLP NPEVRPVFAR REELKARVGE 310 320 330 340 350 360 EVADAIVNQT RNLCIYPNLY VMDQISTQIR VVRPISVDKT EVTIYCFAPR DESEEVRNAR 370 380 390 400 410 420 IRQYEDFFNV SGMGTPDDLE EFRACQSGYR GSAREWNDLS RGAPHWISGP DDNARRLGLA 430 440 450 460 PLMSGARMED EGLFVQQHTY WAETMLRGIE AEPKVFNVQP VEVAQ

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 2-21, CHARACTERIZATION. Strain: 2CBS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79076 Genomic DNA. Translation: CAA55681.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.12.13. 74079.
Family and domain databases
InterPro	IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHER	PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBDA_BURCE

Accession

Primary (citable) accession number: Q51601

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 52 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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