ADH_STAA8
ID ADH_STAA8 Reviewed; 336 AA.
AC Q2G0G1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alcohol dehydrogenase;
DE Short=ADH;
DE EC=1.1.1.1;
GN Name=adh; OrderedLocusNames=SAOUHSC_00608;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; 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; 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}.
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DR EMBL; CP000253; ABD29746.1; -; Genomic_DNA.
DR RefSeq; WP_001200748.1; NZ_LS483365.1.
DR RefSeq; YP_499171.1; NC_007795.1.
DR AlphaFoldDB; Q2G0G1; -.
DR SMR; Q2G0G1; -.
DR STRING; 1280.SAXN108_0671; -.
DR EnsemblBacteria; ABD29746; ABD29746; SAOUHSC_00608.
DR GeneID; 3918927; -.
DR GeneID; 66838896; -.
DR KEGG; sao:SAOUHSC_00608; -.
DR PATRIC; fig|93061.5.peg.545; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_1_9; -.
DR OMA; GLKMTDT; -.
DR PRO; PR:Q2G0G1; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046187; P:acetaldehyde catabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_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; Reference proteome; Zinc.
FT CHAIN 1..336
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000273033"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="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