ID   B1LRF5_ECOSM            Unreviewed;       339 AA.
AC   B1LRF5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family {ECO:0000313|EMBL:ACB19224.1};
GN   OrderedLocusNames=EcSMS35_4750 {ECO:0000313|EMBL:ACB19224.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB19224.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB19224.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP000970; ACB19224.1; -; Genomic_DNA.
DR   RefSeq; WP_012311922.1; NC_010498.1.
DR   AlphaFoldDB; B1LRF5; -.
DR   KEGG; ecm:EcSMS35_4750; -.
DR   HOGENOM; CLU_026673_20_2_6; -.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
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   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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          13..335
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  36518 MW;  C8E927D3F15EF538 CRC64;
     MSMIKSYAAK EAGGELELYE YDPGELKPQD VEVQVDYCGI CHSDLSMIDN EWGFSQYPLV
     AGHEVIGRVV ALGSAAQDKG LQVGQRVGIG WTARSCGHCD ACISGNQINC EQGAVPTIMN
     RGGFAEKLRA DWQWVIPLPE NIDIESAGPL LCGGITVFKP LLMHHITATS RVGVIGIGGL
     GHIAIKLLHA MGCEVTAFSS NPAKEQEVLA MGADKVVNSR DPQALKTLAG QFDLIINTVN
     VSLDWQPYFE ALTYGGNFHT VGAVLTPLSV PAFTLIAGDR SVSGSATGTP YELRKLMRFA
     ARSKVAPTTE LFPMSKINDA IQHVRDGKAR YRVVLKADF
//