ID A0A0F6B1I0_SALT1 Unreviewed; 336 AA.
AC A0A0F6B1I0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adhP {ECO:0000313|EMBL:ACY88362.1};
GN OrderedLocusNames=STM14_1891 {ECO:0000313|EMBL:ACY88362.1};
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858 {ECO:0000313|EMBL:ACY88362.1, ECO:0000313|Proteomes:UP000002695};
RN [1] {ECO:0000313|EMBL:ACY88362.1, ECO:0000313|Proteomes:UP000002695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262 {ECO:0000313|Proteomes:UP000002695};
RX PubMed=19897643; DOI=10.1128/JB.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
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; CP001363; ACY88362.1; -; Genomic_DNA.
DR RefSeq; WP_000642447.1; NZ_CP043402.1.
DR AlphaFoldDB; A0A0F6B1I0; -.
DR SMR; A0A0F6B1I0; -.
DR KEGG; seo:STM14_1891; -.
DR PATRIC; fig|588858.6.peg.1804; -.
DR HOGENOM; CLU_026673_20_1_6; -.
DR BioCyc; SENT588858:STM14_RS08705-MONOMER; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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 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
//
