ID   CHNA_ACISS              Reviewed;         251 AA.
AC   Q9F7E0;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cyclohexanol dehydrogenase {ECO:0000303|PubMed:10940013};
DE            EC=1.1.1.245 {ECO:0000305|PubMed:10940013};
GN   Name=chnA {ECO:0000303|PubMed:10940013};
OS   Acinetobacter sp. (strain SE19).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=135835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=SE19;
RX   PubMed=10940013; DOI=10.1128/jb.182.17.4744-4751.2000;
RA   Cheng Q., Thomas S.M., Kostichka K., Valentine J.R., Nagarajan V.;
RT   "Genetic analysis of a gene cluster for cyclohexanol oxidation in
RT   Acinetobacter sp. strain SE19 by in vitro transposition.";
RL   J. Bacteriol. 182:4744-4751(2000).
CC   -!- FUNCTION: Catalyzes the oxidation of cyclohexanol to cyclohexanone.
CC       Required for the conversion of cyclohexanol to adipic acid.
CC       {ECO:0000269|PubMed:10940013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclohexanol + NAD(+) = cyclohexanone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10044, ChEBI:CHEBI:15378, ChEBI:CHEBI:17854,
CC         ChEBI:CHEBI:18099, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.245; Evidence={ECO:0000305|PubMed:10940013};
CC   -!- DISRUPTION PHENOTYPE: Mutant accumulates cyclohexanol.
CC       {ECO:0000269|PubMed:10940013}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AF282240; AAG10026.1; -; Genomic_DNA.
DR   SMR; Q9F7E0; -.
DR   BioCyc; MetaCyc:MON-3121; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..251
FT                   /note="Cyclohexanol dehydrogenase"
FT                   /id="PRO_0000453522"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         21..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
SQ   SEQUENCE   251 AA;  26159 MW;  B5BAA48055997D5D CRC64;
     MEKIMSNKFN NKVALITGAG SGIGKSTALL LAQQGVSVVV SDINLEAAQK VVDEIVALGG
     KAAANKANTA EPEDMKAAVE FAVSTFGALH LAFNNAGILG EVNSTEELSI EGWRRVIDVN
     LNAVFYSMHY EVPAILAAGG GAIVNTASIA GLIGIQNISG YVAAKHGVTG LTKAAALEYA
     DKGIRINSVH PGYIKTPLIA EFEEAEMVKL HPIGRLGQPE EVAQVVAFLL SDDASFVTGS
     QYVVDGAYTS K