ID   A0A0N1QT20_SALSV        Unreviewed;       336 AA.
AC   A0A0N1QT20;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=SeSA_A1683 {ECO:0000313|EMBL:ACF89133.1};
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843 {ECO:0000313|EMBL:ACF89133.1, ECO:0000313|Proteomes:UP000001865};
RN   [1] {ECO:0000313|EMBL:ACF89133.1, ECO:0000313|Proteomes:UP000001865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633 {ECO:0000313|EMBL:ACF89133.1,
RC   ECO:0000313|Proteomes:UP000001865};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP001127; ACF89133.1; -; Genomic_DNA.
DR   RefSeq; WP_000642447.1; NC_011094.1.
DR   AlphaFoldDB; A0A0N1QT20; -.
DR   SMR; A0A0N1QT20; -.
DR   KEGG; sew:SeSA_A1683; -.
DR   HOGENOM; CLU_026673_20_1_6; -.
DR   Proteomes; UP000001865; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08297; CAD3; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACF89133.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          7..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  35541 MW;  39E7F48AB54EDB66 CRC64;
     MKAAVVTQDH QVDVTEKTLR PLRHGEALLK MECCGVCHTD LHVKNGDFGD KTGVILGHEG
     IGVVAEVGPG VTSLKPGDRA SVAWFYEGCG HCEYCNTGNE TLCRNVKNAG YTVDGGMAEE
     CIVVADYAVK VPEGLDSAAA SSITCAGVTT YKAVKISHIK PGQWIAIYGL GGLGNLALQY
     AKNVFNAKVI AIDVNDGQLK LAEEMGADLT INSRTEDAAK IVQEKTGGAH AAVVTAVAKA
     AFNSAVDAVR AGGRVVAVGL PPEAMNLDIP RLVLDGIQVV GSLVGTRQDL TEAFQFAAEG
     KVVPKVALRP LEDINVIFKE MEQGQIRGRM VIDFRR
//