Reviewed, UniProtKB/Swiss-Prot P07769 (BENA_ACIAD)

Names and origin

Protein names

Recommended name:
    Benzoate 1,2-dioxygenase subunit alpha
    EC=1.14.12.10

Gene names

Name:	benA
Ordered Locus Names:	ACIAD1436

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. Binds 1 iron ion Probable.
Pathway	Aromatic compound metabolism; benzoic acid degradation via hydroxylation; catechol from benzoic acid: step 1/2.
Subunit structure	This dioxygenase system consists of three proteins: the two subunits of the hydroxylase component (benA and benB), and an electron transfer component (benC).
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	Complete proteome
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 benzoate 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
	Chain	1 – 461	461	Benzoate 1,2-dioxygenase subunit alpha		PRO_0000085043
Regions
	Domain	54 – 151	98	Rieske
Sites
	Metal binding	95	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	97	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	115	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	118	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	224	1	Iron By similarity
	Metal binding	229	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P07769-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: CFCC3247A3C4C379	FASTA	461	52,229
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases." Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., Harayama S. J. Bacteriol. 173:5385-5395(1991) [PubMed: 1885518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Elby D.M., Neidle E.L. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 84; 103-104; 171-172 AND 380-382.
[3]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." 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. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF009224 Genomic DNA. Translation: AAC46436.2. CR543861 Genomic DNA. Translation: CAG68300.1.
RefSeq	YP_046122.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2880890.
GenomeReviews	Gene locus ACIAD1436 in contig CR543861_GR.
KEGG	aci:ACIAD1436.
NMPDR	fig|62977.3.peg.794.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P07769.
OMA	P07769. SVDKTEV.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD1436-MON.
Family and domain databases
InterPro	IPR017639. Benzo_1-2-diOase_lsu. 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.
TIGRFAMs	TIGR03229. benzo_1_2_benA. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BENA_ACIAD

Accession

Primary (citable) accession number: P07769

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	June 6, 2002
Last modified:	June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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