NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1885518 [NCBI, ExPASy, EBI, Israel, Japan]
Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., Harayama S.;
"Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases.";
J. Bacteriol. 173:5385-5395(1991).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(2004).

Comments

FUNCTION: Degradation of benzoate to 2-hydro-1,2-dihydroxybenzoate (DHB). The beta subunit may be responsible for the substrate specificity of the enzyme.
CATALYTIC ACTIVITY: Benzoate + NADH + O₂ = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD⁺.
PATHWAY: Aromatic compound metabolism; benzoic acid degradation via hydroxylation; catechol from benzoic acid: step 1/2 .
SUBUNIT: This dioxygenase system consists of three proteins: the two subunits of the hydroxylase (benA and benB), and an electron transfer component (benC).
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

AF009224; AAC46437.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR543861; CAG68301.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23478; S23478.

RefSeq

YP_046123.1; -.

3D structure databases

ModBase

P07770.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1437-MON; -.

Ontologies

GO:0018623;	Molecular function: benzoate 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: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

IPR017641; Benzo_1-2-diOase_ssu.
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

2880891; -.

GenomeReviews

CR543861_GR; ACIAD1437.

KEGG

aci:ACIAD1437; -.

NMPDR

fig|62977.3.peg.795; -.

Phylogenomic databases

HOGENOM

P07770; -.

Genome annotation databases

CMR

P07770; ACIAD1437.

Other

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 169`	`169`		`Benzoate 1,2-dioxygenase subunit beta.`	`PRO_0000085065`

Sequence information

Length: 169 AA [This is the length of the unprocessed precursor]

Molecular weight: 20073 Da [This is the MW of the unprocessed precursor]

CRC64: 4B0CD8F8AA001325 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNATALLDTI SIEQISQFLY SEARFLDDEQ WDDWLECYAP QASFWMPAWD DNDQLTENPQ 

        70         80         90        100        110        120 
TEISLIYYPD RQGLEDRVFR IKTERSSATM PDTRTAHNIS NIEVESRDGL QITVRFNWNT 

       130        140        150        160 
LSFRYKNSYS YFGMSRYVID FSGEQPKILS KYVMLKNDYI NQVIDIYHI

P07770 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