ID F5NUJ6_SHIFL Unreviewed; 347 AA.
AC F5NUJ6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Sorbitol dehydrogenase {ECO:0000313|EMBL:EGK38018.1};
DE EC=1.1.1.14 {ECO:0000313|EMBL:EGK38018.1};
GN Name=gutB {ECO:0000313|EMBL:EGK38018.1};
GN ORFNames=SFK227_1796 {ECO:0000313|EMBL:EGK38018.1};
OS Shigella flexneri K-227.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766147 {ECO:0000313|EMBL:EGK38018.1, ECO:0000313|Proteomes:UP000004520};
RN [1] {ECO:0000313|EMBL:EGK38018.1, ECO:0000313|Proteomes:UP000004520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K-227 {ECO:0000313|EMBL:EGK38018.1,
RC ECO:0000313|Proteomes:UP000004520};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGK38018.1}.
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DR EMBL; AFGY01000021; EGK38018.1; -; Genomic_DNA.
DR AlphaFoldDB; F5NUJ6; -.
DR PATRIC; fig|766147.3.peg.1768; -.
DR Proteomes; UP000004520; Unassembled WGS sequence.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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:EGK38018.1};
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; 37708 MW; DA2D7BA3B7DAFD30 CRC64;
MKNSKAILQV PGTMEIISAE IPDPKEDEVL IKVEYVGICG SDVHGFESGP FIPPKDPNQE
IGLGHECAGT VVAVGSRVRK FKPGDRVNIE SGVPCGHCRY CLEGKYNICP DVDFMATQPN
YRGALTHYLC HPESFTYKLP DNMDTMEGAL VEPAAVGMHA AMLADVKPGK KIIILGAGCI
GLMTLQACKC LGATEIAVVD VLEKRLAMAE QLGATVVING AKEDTIARCQ QFTEDMGADI
VFETAGSAVT VKQAPYLVMR GGKIMIVGTV PGDSAINFLK INREVTIQTV FRYANRYPVT
IEAISSGRFD VKSMVTHIYD YRDVQQAFEE SVNNKRDLIK GVIKISD
//
