ID   BENA_ACIAD              Reviewed;         461 AA.
AC   P07769;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Benzoate 1,2-dioxygenase subunit alpha;
DE            EC=1.14.12.10;
GN   Name=benA; OrderedLocusNames=ACIAD1436;
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   SEQUENCE REVISION TO 84; 103-104; 171-172 AND 380-382.
RA   Elby D.M., Neidle E.L.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- CATALYTIC ACTIVITY: Benzoate + NADH + O(2) = (1R,6S)-1,6-
CC       dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster (Probable).
CC   -!- COFACTOR: Binds 1 iron ion (Probable).
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 component (benA and benB), and an
CC       electron transfer component (benC).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase alpha subunit family.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; AF009224; AAC46436.2; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68300.1; -; Genomic_DNA.
DR   RefSeq; YP_046122.1; -.
DR   GeneID; 2880890; -.
DR   GenomeReviews; CR543861_GR; ACIAD1436.
DR   KEGG; aci:ACIAD1436; -.
DR   NMPDR; fig|62977.3.peg.794; -.
DR   HOGENOM; P07769; -.
DR   OMA; P07769; SVDKTEV.
DR   BioCyc; ASP62977:ACIAD1436-MON; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018623; F:benzoate 1,2-dioxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
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; IPR017639; Benzo_1-2-diOase_lsu.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   PANTHER; PTHR21266:SF2; Rng_hydr_dOase-A; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   TIGRFAMs; TIGR03229; benzo_1_2_benA; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    461       Benzoate 1,2-dioxygenase subunit alpha.
FT                                /FTId=PRO_0000085043.
FT   DOMAIN       54    151       Rieske.
FT   METAL        95     95       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        97     97       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       115    115       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       118    118       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       224    224       Iron (By similarity).
FT   METAL       229    229       Iron (By similarity).
SQ   SEQUENCE   461 AA;  52229 MW;  CFCC3247A3C4C379 CRC64;
     MPRIPVINTS HLDRIDELLV DNTETGEFKL HRSVFTDQAL FDLEMKYIFE GNWVYLAHES
     QIPNNNDYYT TYIGRQPILI ARNRNGELNA MINACSHRGA QLCRHKRGNK TTYTCPFHGW
     TFNNSGKLLK VKDPSDAGYS DCFNQDGSHD LKKVARFESY KGFLFGSLNP DVPSLQEFLG
     ETTKIIDMIV GQSDQGLEVL RGVSTYTYEG NWKLTAENGA DGYHVSAVHW NYAATTQHRK
     EKQAGDTIRA MSAGSWGKHG GGSYGFEHGH MLLWTQWGNP EDRPNFPKAA EYTEKFGAAM
     SKWMIERSRN LCLYPNVYLM DQFGSQIRVL RPISVNKTEV TIYCIAPVGE APEARARRIR
     QYEDFFNASG MATPDDLEEF RACQAGYAGI ELEWNDMCRG SKHWIYGPDD AANEIGLKPA
     ISGIKTEDEG LYLAQHQYWL KSMKQAIAAE KEFASRQGEN A
//