NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
PubMed=2670929 [NCBI, ExPASy, EBI, Israel, Japan]
Zylstra G.J., Gibson D.T.;
"Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli.";
J. Biol. Chem. 264:14940-14946(1989).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
"Complete sequence of Pseudomonas putida F1.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes both the oxidation of benzene and toluene. The beta subunit may be responsible for the substrate specificity of the enzyme.
CATALYTIC ACTIVITY: Benzene + NADH + O₂ = cis-cyclohexa-3,5-diene-1,2-diol + NAD⁺.
CATALYTIC ACTIVITY: Toluene + NADH + O₂ = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD⁺.
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Aromatic compound metabolism; benzene degradation; catechol from benzene: step 1/2 .
PATHWAY: Xenobiotic degradation; toluene degradation .
PATHWAY: Xenobiotic degradation; xylene degradation .
SUBUNIT: This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bnzA and bnzB), a ferredoxin (bnzC) and a ferredoxin reductase (bnzD).
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

J04996; AAA26006.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000712; ABQ79011.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B29830; B29830.

RefSeq

YP_001268195.1; -.

3D structure databases

ModBase

A5W4F1.

Ontologies

GO:0018619;	Molecular function: benzene 1,2-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:0018624;	Molecular function: toluene dioxygenase activity (inferred from electronic annotation from EC).
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

5195398; -.

GenomeReviews

CP000712_GR; Pput_2880.

KEGG

ppf:Pput_2880; -.

CMR

A5W4F1; Pput_2880.

Other

ProtoNet

A5W4F1.

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`
`CHAIN`	`1 187`	`187`		`Benzene 1,2-dioxygenase subunit beta.`	`PRO_0000314466`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 22013 Da [This is the MW of the unprocessed precursor]

CRC64: 39A5D2BECB6116B5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIDSANRADV FLRKPAPVAP ELQHEVEQFY YWEAKLLNDR RFEEWFALLA EDIHYFMPIR 

        70         80         90        100        110        120 
TTRIMRDSRL EYSGSREYAH FDDDATMMKG RLRKITSDVS WSENPASRTR HLVSNVMIVG 

       130        140        150        160        170        180 
AEAEGEYEIS SAFIVYRNRL ERQLDIFAGE RRDTLRRNTS EAGFEIVNRT ILIDQSTILA 


NNLSFFF

A5W4F1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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