[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1569021 [NCBI, ExPASy, EBI, Israel, Japan] Erickson B.D., Mondello F.J.; "Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400."; J. Bacteriol. 174:2903-2912(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1073/pnas.0606924103; PubMed=17030797 [NCBI, ExPASy, EBI, Israel, Japan] Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.; "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility."; Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
[3]	PROTEIN SEQUENCE OF 2-12, AND CHARACTERIZATION. PubMed=7592331 [NCBI, ExPASy, EBI, Israel, Japan] Haddock J.D., Gibson D.T.; "Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400."; J. Bacteriol. 177:5834-5839(1995).
[4]	ERRATUM. Haddock J.D., Gibson D.T.; J. Bacteriol. 178:258-258(1996).

Comments

FUNCTION: The beta subunit may be responsible for the substrate specificity of the enzyme.
CATALYTIC ACTIVITY: Biphenyl + NADH + O₂ = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD⁺.
PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 1/4 .
SUBUNIT: Heterohexamer consisting of three BphA subunits and three BphE subunits. A ferredoxin (BphF) and a ferredoxin reductase (BphG) must be present to obtain activity.
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M86348; AAB63426.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000272; ABE37058.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_556408.1; -.

3D structure databases

ModBase

P37334.

Enzyme and pathway databases

BioCyc

BXEN266265:BXE_C1196-MON; -.

Ontologies

GO:0018687;	Molecular function: biphenyl 2,3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0016702;	Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000391; Rng_hydr_dOase-B.
Graphical view of domain structure.

Pfam

PF00866; Ring_hydroxyl_B; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

4010708; -.

GenomeReviews

CP000272_GR; Bxeno_C1130.

KEGG

bxe:Bxe_C1196; -.

Phylogenomic databases

HOGENOM

P37334; -.

Genome annotation databases

CMR

P37334; Bxeno_C1130.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 188`	`187`	`Biphenyl dioxygenase subunit beta.`	`PRO_0000085068`

Sequence information

Length: 188 AA [This is the length of the unprocessed precursor]

Molecular weight: 22085 Da [This is the MW of the unprocessed precursor]

CRC64: 36DBE14E22FEA67B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNPSPHFFK TFEWPSKAAG LELQNEIEQF YYREAQLLDH RAYEAWFALL DKDIHYFMPL 

        70         80         90        100        110        120 
RTNRMIREGE LEYSGDQDLA HFDETHETMY GRIRKVTSDV GWAENPPSRT RHLVSNVIVK 

       130        140        150        160        170        180 
ETATPDTFEV NSAFILYRNR LERQVDIFAG ERRDVLRRAD NNLGFSIAKR TILLDASTLL 


SNNLSMFF

P37334 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools