ID   IOLG_CERS4              Reviewed;         334 AA.
AC   Q3IX44;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
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=RHOS4_33220;
GN   ORFNames=RSP_3283;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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; CP000144; ABA80890.2; -; Genomic_DNA.
DR   RefSeq; WP_017140345.1; NZ_CP030272.1.
DR   RefSeq; YP_354791.2; NC_007494.2.
DR   AlphaFoldDB; Q3IX44; -.
DR   SMR; Q3IX44; -.
DR   STRING; 272943.RSP_3283; -.
DR   EnsemblBacteria; ABA80890; ABA80890; RSP_3283.
DR   KEGG; rsp:RSP_3283; -.
DR   PATRIC; fig|272943.9.peg.3709; -.
DR   eggNOG; COG0673; Bacteria.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000002703; Chromosome 2.
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..334
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352586"
SQ   SEQUENCE   334 AA;  36118 MW;  D7D8F11181FB1432 CRC64;
     MTLRIGIIGT GAIGTDHARR INRVLSGAEV TAVTDVNRDS AEACVAGVAP GAQILGSAEE
     VIAASDAVLV CSWGTAHETQ VLAAIAAGKP CFCEKPLATE AYGARRIVEA EEAMGRRLVQ
     VGFMRRYDRG YVALKETVRT RLGPPLMIHA AHRNPSVPGR YRTPMAIHDT LIHEIDVLRW
     LLDDEYVSAQ VIFPRATRHT HAGLRDPQIV LLETAKGVRI DVEIFVNCRY GYDIQCEVVG
     EEGTARLPEP TAIPTRLGAV FGQPILMDWK DRFIDSYDVE LQDFLKAAAQ GTAAGPSAWD
     GYAAAITADV CVQAQERPGA ILPVTLPARP ALYA