ID B7MUR2_ECO81 Unreviewed; 336 AA.
AC B7MUR2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
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:CAR07828.2};
GN OrderedLocusNames=ECED1_1631 {ECO:0000313|EMBL:CAR07828.2};
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR07828.2, ECO:0000313|Proteomes:UP000000748};
RN [1] {ECO:0000313|Proteomes:UP000000748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR07828.2; -; Genomic_DNA.
DR RefSeq; WP_000642412.1; NC_011745.1.
DR AlphaFoldDB; B7MUR2; -.
DR KEGG; ecq:ECED1_1631; -.
DR HOGENOM; CLU_026673_20_1_6; -.
DR OMA; GLKMTDT; -.
DR Proteomes; UP000000748; 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:CAR07828.2}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 8..332
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 336 AA; 35368 MW; D27DBC265C6A0A30 CRC64;
MKAAVVTKDH HVDVTDKTLR SLKHGEALLK MECCGVCHTD LHVKNGDFGD KTGVILGHEG
IGVVAEVGPG VTSLKPGDRA SVAWFYEGCG HCEYCNSGNE TLCRSVKNAG YSVDGGMAEE
CIVVADYAVK VPDGLDSAAA SSITCAGVTT YKAVKLSKIR PGQWIAIYGL GGLGNLALQY
AKNVFNAKVI AIDVNDEQLK LATEMGADLA INSRTEDAAR IVQEKAGGAH AAVVTAVAKA
AFNSAVDAVR AGGRVVAVGL PPESMSLDIP RLVLDGIEVV GSLVGTRQDL TEAFQFAAEG
KVVPKVALRP LADINTIFTE MEEGKIRGRM VIDFRR
//