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   03-AUG-2022, entry version 135.
DE   RecName: Full=Benzoate 1,2-dioxygenase subunit beta;
DE            EC=1.14.12.10;
GN   Name=benB; OrderedLocusNames=ACIAD1437;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1885518; DOI=10.1128/jb.173.17.5385-5395.1991;
RA   Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., Harayama S.;
RT   "Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for
RT   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].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   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:
CC       Reaction=benzoate + H(+) + NADH + O2 = (1R,6S)-1,6-dihydroxycyclohexa-
CC         2,4-diene-1-carboxylate + NAD(+); Xref=Rhea:RHEA:12633,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16150,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60129;
CC         EC=1.14.12.10;
CC   -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC       hydroxylation; catechol from benzoate: step 1/2.
CC   -!- SUBUNIT: This dioxygenase system consists of three proteins: the two
CC       subunits of the hydroxylase (BenA and BenB), and an electron transfer
CC       component (BenC).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000305}.
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DR   EMBL; AF009224; AAC46437.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68301.1; -; Genomic_DNA.
DR   PIR; S23478; S23478.
DR   RefSeq; WP_004925491.1; NC_005966.1.
DR   AlphaFoldDB; P07770; -.
DR   SMR; P07770; -.
DR   STRING; 62977.ACIAD1437; -.
DR   EnsemblBacteria; CAG68301; CAG68301; ACIAD1437.
DR   GeneID; 45233850; -.
DR   KEGG; aci:ACIAD1437; -.
DR   eggNOG; COG5517; Bacteria.
DR   HOGENOM; CLU_102527_0_1_6; -.
DR   OMA; GICRARC; -.
DR   OrthoDB; 1736098at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06640-MON; -.
DR   UniPathway; UPA00156; UER00254.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0018623; F:benzoate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR   InterPro; IPR017641; Benzo_1-2-diOase_ssu.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   PANTHER; PTHR41534; PTHR41534; 1.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
DR   TIGRFAMs; TIGR03232; benzo_1_2_benB; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..169
FT                   /note="Benzoate 1,2-dioxygenase subunit beta"
FT                   /id="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