ID   XYLL_PSEPU              Reviewed;         269 AA.
AC   P23102;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=xylL;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid TOL pWW0.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
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).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; M64747; AAA26050.1; -; Genomic_DNA.
DR   PIR; S23485; S23485.
DR   RefSeq; NP_542868.1; NC_003350.1.
DR   RefSeq; WP_011005911.1; NC_003350.1.
DR   AlphaFoldDB; P23102; -.
DR   SMR; P23102; -.
DR   BioCyc; MetaCyc:MON-2964; -.
DR   UniPathway; UPA00156; UER00255.
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; Plasmid.
FT   CHAIN           1..269
FT                   /note="1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate
FT                   dehydrogenase"
FT                   /id="PRO_0000054814"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   269 AA;  28883 MW;  23708B9757C6FC41 CRC64;
     MNKRFQGKVA VITGAAQGIG RRVAERMAAE GGRLLLVDRS ELIHELADEL VGVAEVLTLT
     ADLEQFAECQ RVMAAALERF GRLDILINNV GGTIWAKPFE HYQEREIEAE VRRSLFPTLW
     CCHAALAPMI EQGSGAIVNV SSVATRGIHR VPYGAAKGGV NALTACLAFE TAERGIRVNA
     TAPGGTEARH GGFRNSAEPS EQEKVWYQQI VDQSLDSSLM KRYGSIDEQV EAILFLASDA
     ASYITGITLP VAGGDLGCQS CSVMFSVSG