BEND_ACIAD
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 03-AUG-2022, entry version 149.
DE RecName: Full=1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase;
DE EC=1.3.1.25;
DE AltName: Full=2-hydro-1,2-dihydroxybenzoate dehydrogenase;
DE Short=DHB dehydrogenase;
DE AltName: Full=Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase;
DE AltName: Full=Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase;
GN Name=benD; OrderedLocusNames=ACIAD1439;
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=1740120; DOI=10.1111/j.1432-1033.1992.tb16612.x;
RA Neidle E.L., Hartnett C., Ornston L.N., Bairoch A., Rekik M., Harayama S.;
RT "Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the
RT Acinetobacter calcoaceticus chromosomal benD gene are members of the short-
RT chain alcohol dehydrogenase superfamily.";
RL Eur. J. Biochem. 204:113-120(1992).
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 2-hydro-1,2-dihydroxy benzoate (DHB) to
CC catechol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate +
CC NAD(+) = catechol + CO2 + NADH; Xref=Rhea:RHEA:11560,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18135, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:60129; EC=1.3.1.25;
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation; catechol from benzoate: step 2/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF009224; AAC46439.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68303.1; -; Genomic_DNA.
DR PIR; S23480; S23480.
DR RefSeq; WP_004925479.1; NC_005966.1.
DR AlphaFoldDB; P07772; -.
DR SMR; P07772; -.
DR STRING; 62977.ACIAD1439; -.
DR EnsemblBacteria; CAG68303; CAG68303; ACIAD1439.
DR GeneID; 45233852; -.
DR KEGG; aci:ACIAD1439; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_2_6; -.
DR OMA; VWDTTMA; -.
DR OrthoDB; 1356861at2; -.
DR BioCyc; ASP62977:ACIAD_RS06650-MON; -.
DR UniPathway; UPA00156; UER00255.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0047116; F:1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..261
FT /note="1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate
FT dehydrogenase"
FT /id="PRO_0000054529"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 159
FT /note="S -> C (in Ref. 1; AAC46439)"
FT /evidence="ECO:0000305"
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
