ID BENB_ACIAD Reviewed; 169 AA. AC P07770; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 16-JUN-2009, entry version 61. DE RecName: Full=Benzoate 1,2-dioxygenase subunit beta; DE EC=1.14.12.10; GN Name=benB; OrderedLocusNames=ACIAD1437; OS Acinetobacter sp. (strain ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91358314; PubMed=1885518; RA Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., RA Harayama S.; RT "Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes RT for benzoate 1,2-dioxygenase reveal evolutionary relationships among RT multicomponent oxygenases."; RL J. Bacteriol. 173:5385-5395(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Degradation of benzoate to 2-hydro-1,2-dihydroxybenzoate CC (DHB). The beta subunit may be responsible for the substrate CC specificity of the enzyme. CC -!- CATALYTIC ACTIVITY: Benzoate + NADH + O(2) = (1R,6S)-1,6- CC dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+). CC -!- PATHWAY: Aromatic compound metabolism; benzoic acid degradation CC via hydroxylation; catechol from benzoic acid: step 1/2. CC -!- SUBUNIT: This dioxygenase system consists of three proteins: the CC two subunits of the hydroxylase (benA and benB), and an electron CC transfer component (benC). CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating CC dioxygenase beta subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF009224; AAC46437.1; -; Genomic_DNA. DR EMBL; CR543861; CAG68301.1; -; Genomic_DNA. DR PIR; S23478; S23478. DR RefSeq; YP_046123.1; -. DR GeneID; 2880891; -. DR GenomeReviews; CR543861_GR; ACIAD1437. DR KEGG; aci:ACIAD1437; -. DR NMPDR; fig|62977.3.peg.795; -. DR HOGENOM; P07770; -. DR OMA; P07770; TLSFRYK. DR BioCyc; ASP62977:ACIAD1437-MON; -. DR GO; GO:0018623; F:benzoate 1,2-dioxygenase activity; IEA:EC. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017641; Benzo_1-2-diOase_ssu. DR InterPro; IPR000391; Rng_hydr_dOase-bsu. DR Pfam; PF00866; Ring_hydroxyl_B; 1. DR TIGRFAMs; TIGR03232; benzo_1_2_benB; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; NAD; KW Oxidoreductase. FT CHAIN 1 169 Benzoate 1,2-dioxygenase subunit beta. FT /FTId=PRO_0000085065. SQ SEQUENCE 169 AA; 20073 MW; 4B0CD8F8AA001325 CRC64; MNATALLDTI SIEQISQFLY SEARFLDDEQ WDDWLECYAP QASFWMPAWD DNDQLTENPQ TEISLIYYPD RQGLEDRVFR IKTERSSATM PDTRTAHNIS NIEVESRDGL QITVRFNWNT LSFRYKNSYS YFGMSRYVID FSGEQPKILS KYVMLKNDYI NQVIDIYHI //