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Database: UniProt
Entry: Q2YSX0
LinkDB: Q2YSX0
Original site: Q2YSX0 
ID   ADH_STAAB               Reviewed;         336 AA.
AC   Q2YSX0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-DEC-2018, entry version 89.
DE   RecName: Full=Alcohol dehydrogenase;
DE            Short=ADH;
DE            EC=1.1.1.1;
GN   Name=adh; OrderedLocusNames=SAB0557;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80245.1; -; Genomic_DNA.
DR   RefSeq; WP_001200748.1; NC_007622.1.
DR   ProteinModelPortal; Q2YSX0; -.
DR   SMR; Q2YSX0; -.
DR   EnsemblBacteria; CAI80245; CAI80245; SAB0557.
DR   KEGG; sab:SAB0557; -.
DR   HOGENOM; HOG000294685; -.
DR   KO; K13953; -.
DR   OMA; GLKMTDT; -.
DR   BioCyc; SAUR273036:G1G1D-631-MONOMER; -.
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   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    336       Alcohol dehydrogenase.
FT                                /FTId=PRO_0000273034.
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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