ID   IOLG_PSEFS              Reviewed;         336 AA.
AC   C3K9I8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=PFLU_2580;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; AM181176; CAY48814.1; -; Genomic_DNA.
DR   RefSeq; WP_012723781.1; NC_012660.1.
DR   AlphaFoldDB; C3K9I8; -.
DR   SMR; C3K9I8; -.
DR   STRING; 216595.PFLU_2580; -.
DR   PRIDE; C3K9I8; -.
DR   EnsemblBacteria; CAY48814; CAY48814; PFLU_2580.
DR   KEGG; pfs:PFLU_2580; -.
DR   PATRIC; fig|216595.4.peg.2784; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_6; -.
DR   OMA; VNCKYGY; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000002332; 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; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_1000215885"
SQ   SEQUENCE   336 AA;  36605 MW;  173842A2072D598D CRC64;
     MSLKLGVIGT GAIGRDHIRR CSQTLLNSQV VAVTDINLEQ AAKVVADLKL DAEVYPDGHA
     LINSPQVEAV LVTSWGPSHE EFVLAAIAAG KPVFCEKPLA VTAEGCRRIV DAEVAYGKRL
     VQVGFMRPYD EGYRALKAVI DSGQIGEPLM LHCAHRNPTV GENYKTDMAI TDTLIHELDV
     LRWLLNDDYV SVQVVFPRKS SKALAHLRDP QIVLLETAKG TRIDVEVFVN CQYGYDIQCE
     VVGETGIAKL PEPSQVQLRS GAKLSNAILM DWKDRFIGAY DVELQAFIDS VRAGQVGGPS
     AWDGFAAAVA ADACIEAQGS EQIVKMSLPD RPRFYG