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Database: UniProt
Entry: Q5HI63
LinkDB: Q5HI63
Original site: Q5HI63 
ID   ADH_STAAC               Reviewed;         336 AA.
AC   Q5HI63;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 100.
DE   RecName: Full=Alcohol dehydrogenase;
DE            Short=ADH;
DE            EC=1.1.1.1;
GN   Name=adh; OrderedLocusNames=SACOL0660;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
DR   EMBL; CP000046; AAW36350.1; -; Genomic_DNA.
DR   RefSeq; WP_001200748.1; NC_002951.2.
DR   ProteinModelPortal; Q5HI63; -.
DR   SMR; Q5HI63; -.
DR   STRING; 93062.SACOL0660; -.
DR   EnsemblBacteria; AAW36350; AAW36350; SACOL0660.
DR   KEGG; sac:SACOL0660; -.
DR   eggNOG; ENOG4105DQ4; Bacteria.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294685; -.
DR   KO; K13953; -.
DR   OMA; GLKMTDT; -.
DR   BioCyc; SAUR93062:G1G4B-709-MONOMER; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    336       Alcohol dehydrogenase.
FT                                /FTId=PRO_0000273035.
FT   METAL        37     37       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        58     58       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        89     89       Zinc 2. {ECO:0000250}.
FT   METAL        92     92       Zinc 2. {ECO:0000250}.
FT   METAL        95     95       Zinc 2. {ECO:0000250}.
FT   METAL       103    103       Zinc 2. {ECO:0000250}.
FT   METAL       145    145       Zinc 1; catalytic. {ECO:0000250}.
SQ   SEQUENCE   336 AA;  36048 MW;  DB68A432F9E72EF9 CRC64;
     MRAAVVTKDH KVSIEDKKLR ALKPGEALVQ TEYCGVCHTD LHVKNADFGD VTGVTLGHEG
     IGKVIEVAED VESLKIGDRV SIAWMFESCG RCEYCTTGRE TLCRSVKNAG YTVDGAMAEQ
     VIVTADYAVK VPEKLDPAAA SSITCAGVTT YKAVKVSNVK PGQWLGVFGI GGLGNLALQY
     AKNVMGAKIV AFDINDDKLA FAKELGADAI INSKDVDPVA EVMKLTDNKG LDATVVTSVA
     KTPFNQAVDV VKAGARVVAV GLPVDKMNLD IPRLVLDGIE VVGSLVGTRQ DLREAFEFAA
     ENKVTPKVQL RKLEEINDIF EEMENGTITG RMVIKF
//
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