ID   A7ZMP4_ECO24            Unreviewed;       347 AA.
AC   A7ZMP4;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   08-OCT-2025, entry version 90.
DE   SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:ABV17131.1};
DE            EC=1.1.1.14 {ECO:0000313|EMBL:ABV17131.1};
GN   Name=gutB {ECO:0000313|EMBL:ABV17131.1};
GN   OrderedLocusNames=EcE24377A_1998 {ECO:0000313|EMBL:ABV17131.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17131.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV17131.1; -; Genomic_DNA.
DR   RefSeq; WP_000798115.1; NC_009801.1.
DR   AlphaFoldDB; A7ZMP4; -.
DR   KEGG; ecw:EcE24377A_1998; -.
DR   HOGENOM; CLU_026673_11_5_6; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0003939; F:L-iditol 2-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05285; sorbitol_DH; 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; IPR020843; ER.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR045306; SDH-like.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABV17131.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          9..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  37773 MW;  E49219FA1CE1E963 CRC64;
     MKNSKAILQV PGTMKIISAE IPVPKEDEVL IKVEYVGICG SDVHGFESGP FIPPKDPNQE
     IGLGHECAGT VVAVGSRVRK FKPGDRVNIE PGVPCGHCRY CLEGKYNICP DVDFMATQPN
     YRGALTHYLC HPESFTYKLP DNMDTMEGAL VEPAAVGMHA AMLADVKPGK KIIILGAGCI
     GLMTLQACKC LGATEIAVVD VLEKRLIMAE QLGATVVING TKEDTIARCQ QFTEDMGADI
     VFETAGSAVT VKQAPYLVMR GGKIMIVGTV PGDSAINFLK INREVTIQTV FRYANRYPVT
     IEAISSGRFD VKSMVTHIYD YRDVQQAFEE SVNNKRDIIK GVIKISD
//