ID   IOLG_SALA4              Reviewed;         336 AA.
AC   B5F3F4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.18 {ECO:0000255|HAMAP-Rule:MF_01671};
DE   AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG {ECO:0000255|HAMAP-Rule:MF_01671}; OrderedLocusNames=SeAg_B4707;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC       inositol (2KMI or 2-inosose). {ECO:0000255|HAMAP-Rule:MF_01671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose;
CC         Xref=Rhea:RHEA:16949, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:17811, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01671};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01671}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01671}.
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DR   EMBL; CP001138; ACH52077.1; -; Genomic_DNA.
DR   RefSeq; WP_000172704.1; NC_011149.1.
DR   AlphaFoldDB; B5F3F4; -.
DR   SMR; B5F3F4; -.
DR   EnsemblBacteria; ACH52077; ACH52077; SeAg_B4707.
DR   KEGG; sea:SeAg_B4707; -.
DR   HOGENOM; CLU_023194_0_1_6; -.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01671; IolG; 1.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR023794; MI/DCI_dehydrogenase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..336
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_1000187321"
SQ   SEQUENCE   336 AA;  37267 MW;  5E66D7BC40158197 CRC64;
     MTLKAGIVGI GMIGSDHLRR LANTVSGVEV VAVCDIVAGR AQAALDKYAI EAKDYNDYHD
     LINDKDVEVV IITASNEAHA DVAVAALNAN KYVFCEKPLA VTAADCQRVI EAEQKNGKRM
     VQIGFMRRYD KGYVQLKNII DSGEIGQPLM VHGRHYNAST VPEYKTPQAI YETLIHEIDV
     MHWLLNEDYK TVKVYFPRQS SLVTTLRDPQ LVVMETTSGI NIVVEVFVNC QYGYDIHCDV
     TGEKGMAELP TVASAAVRKA AKYSTDILVD WKQRFIDAYD IEFQDFFDRL NAGLPPAGPT
     SWDGYLAAVT ADACVKSQET GNTEIVELPS KPDFYK