ID   IOLG_CERS1              Reviewed;         334 AA.
AC   A3PRX7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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};
GN   OrderedLocusNames=Rsph17029_4015;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000578; ABN79093.1; -; Genomic_DNA.
DR   RefSeq; WP_011842816.1; NC_009050.1.
DR   AlphaFoldDB; A3PRX7; -.
DR   SMR; A3PRX7; -.
DR   EnsemblBacteria; ABN79093; ABN79093; Rsph17029_4015.
DR   GeneID; 57472657; -.
DR   KEGG; rsh:Rsph17029_4015; -.
DR   HOGENOM; CLU_023194_0_1_5; -.
DR   OMA; VNCKYGY; -.
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..334
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352587"
SQ   SEQUENCE   334 AA;  36104 MW;  17BDE2CEDC26BA02 CRC64;
     MTLRIGIIGT GAIGTDHARR INRVLSGAEV TAVTDVNRDN AEACVAGVAP GAQILGSAEE
     VIAASDAVLV CSWGAAHEAQ VLAAIAAGKP CFCEKPLATE AYGARRIVEA EGAMGRRLVQ
     VGFMRRYDRG YIALKETVRT RLGPPLMIHA AHRNPTVPGR YRTPMAIHDT LIHEIDVLRW
     LLDDEYVSAQ VIFPRATRHT HAGLRDPQIV LLETAKGVRI DVEIFVNCRY GYDIQCEVVG
     EEGTARLPEP MAIPTRLGAM FGQPILMDWK DRFIDSYDVE LQDFLKAAAQ GTAAGPSAWD
     GYAAAITADV CVQAQERPGA ILPVTLPARP ALYA