ID   BEND_ACIAD              Reviewed;         261 AA.
AC   P07772; Q6FCA8;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase;
DE            EC=1.3.1.25;
DE   AltName: Full=Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase;
DE   AltName: Full=Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase;
DE   AltName: Full=2-hydro-1,2-dihydroxybenzoate dehydrogenase;
DE            Short=DHB dehydrogenase;
GN   Name=benD; OrderedLocusNames=ACIAD1439;
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=92155191; PubMed=1740120;
RX   DOI=10.1111/j.1432-1033.1992.tb16612.x;
RA   Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M.,
RA   Harayama S.;
RT   "Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and
RT   the Acinetobacter calcoaceticus chromosomal benD gene are members of
RT   the short-chain alcohol dehydrogenase superfamily.";
RL   Eur. J. Biochem. 204:113-120(1992).
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 2-hydro-1,2-dihydroxy benzoate (DHB) to
CC       catechol.
CC   -!- CATALYTIC ACTIVITY: (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-
CC       carboxylate + NAD(+) = catechol + CO(2) + NADH.
CC   -!- PATHWAY: Aromatic compound metabolism; benzoic acid degradation
CC       via hydroxylation; catechol from benzoic acid: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AF009224; AAC46439.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68303.1; -; Genomic_DNA.
DR   PIR; S23480; S23480.
DR   RefSeq; YP_046125.1; -.
DR   HSSP; P97852; 1GZ6.
DR   GeneID; 2880309; -.
DR   GenomeReviews; CR543861_GR; ACIAD1439.
DR   KEGG; aci:ACIAD1439; -.
DR   NMPDR; fig|62977.3.peg.797; -.
DR   HOGENOM; P07772; -.
DR   OMA; P07772; MQQVVDQ.
DR   BioCyc; ASP62977:ACIAD1439-MON; -.
DR   GO; GO:0047116; F:1,6-dihydroxycyclohexa-2,4-diene-1-carboxyl...; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Complete proteome; NAD;
KW   Oxidoreductase.
FT   CHAIN         1    261       1,6-dihydroxycyclohexa-2,4-diene-1-
FT                                carboxylate dehydrogenase.
FT                                /FTId=PRO_0000054529.
FT   NP_BIND      13     37       NAD (By similarity).
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
FT   BINDING     145    145       Substrate (By similarity).
FT   CONFLICT    159    159       S -> C (in Ref. 1; AAC46439).
SQ   SEQUENCE   261 AA;  27982 MW;  E29D0FAC6E9AE55E CRC64;
     MNSTQRFEHK VVIVTGAAQG IGRGVALRIA QEGGCLILAD RSDLIQAVLA EIKALGALAI
     AVETDLETYA GAELVVSHAI AEYGRIDVLI NNVGGAIWMK PFQEFSEEEI IQEVHRSLFP
     ALWCCRAVLP EMLKHQQGTI VNVSSIATRG IHRIPYSASK GGVNALTASL AFEHAQHGIR
     VNAVATGGTK APPRKIPRNA QPLSKSEQVW MQQVVDQTID RSFLGRYGSI DEQVNAITFL
     ASDESSYITG SVLPVGGGDQ G
//