[1]	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]	SEQUENCE REVISION TO 84; 103-104; 171-172 AND 380-382. Elby D.M., Neidle E.L.; Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]	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).
CATALYTIC ACTIVITY: Benzoate + NADH + O₂ = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD⁺.
COFACTOR: Binds 1 2Fe-2S cluster (Probable).
COFACTOR: Binds 1 iron ion (Probable).
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 component (benA and benB), and an electron transfer component (benC).
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.
SIMILARITY: Contains 1 Rieske domain.

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; AAC46436.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR543861; CAG68300.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_046122.1; -.

3D structure databases

ModBase

P07769.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1436-MON; -.

Ontologies

GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018623;	Molecular function: benzoate 1,2-dioxygenase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
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 InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR017639; Benzo_1-2-diOase_lsu.
IPR005806; Rieske_reg.
IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879; Ring_hydroxy_dOase_asu_C.
IPR001663; Rng_hydr_dOase-A.
Graphical view of domain structure.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

PANTHER

PTHR21266:SF2; Rng_hydr_dOase-A; 1.

Pfam

PF00355; Rieske; 1.
PF00848; Ring_hydroxyl_A; 1.
Pfam graphical view of domain structure.

PRINTS

PR00090; RNGDIOXGNASE.

PROSITE

PS51296; RIESKE; 1.
PS00570; RING_HYDROXYL_ALPHA; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

2880890; -.

GenomeReviews

CR543861_GR; ACIAD1436.

KEGG

aci:ACIAD1436; -.

NMPDR

fig|62977.3.peg.794; -.

Phylogenomic databases

HOGENOM

P07769; -.

Genome annotation databases

CMR

P07769; ACIAD1436.

Other

ProtoNet

P07769.

UniRef

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

Keywords

2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 461`	`461`	`Benzoate 1,2-dioxygenase subunit alpha.`	`PRO_0000085043`
`DOMAIN`	`54 151`	`98`	`Rieske.`
`METAL`	`95 95`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`97 97`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`115 115`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`118 118`		`Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity).`
`METAL`	`224 224`		`Iron (By similarity).`
`METAL`	`229 229`		`Iron (By similarity).`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 52229 Da [This is the MW of the unprocessed precursor]

CRC64: CFCC3247A3C4C379 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPRIPVINTS HLDRIDELLV DNTETGEFKL HRSVFTDQAL FDLEMKYIFE GNWVYLAHES 

        70         80         90        100        110        120 
QIPNNNDYYT TYIGRQPILI ARNRNGELNA MINACSHRGA QLCRHKRGNK TTYTCPFHGW 

       130        140        150        160        170        180 
TFNNSGKLLK VKDPSDAGYS DCFNQDGSHD LKKVARFESY KGFLFGSLNP DVPSLQEFLG 

       190        200        210        220        230        240 
ETTKIIDMIV GQSDQGLEVL RGVSTYTYEG NWKLTAENGA DGYHVSAVHW NYAATTQHRK 

       250        260        270        280        290        300 
EKQAGDTIRA MSAGSWGKHG GGSYGFEHGH MLLWTQWGNP EDRPNFPKAA EYTEKFGAAM 

       310        320        330        340        350        360 
SKWMIERSRN LCLYPNVYLM DQFGSQIRVL RPISVNKTEV TIYCIAPVGE APEARARRIR 

       370        380        390        400        410        420 
QYEDFFNASG MATPDDLEEF RACQAGYAGI ELEWNDMCRG SKHWIYGPDD AANEIGLKPA 

       430        440        450        460 
ISGIKTEDEG LYLAQHQYWL KSMKQAIAAE KEFASRQGEN A

P07769 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