ID   IOLG_RHOJR              Reviewed;         366 AA.
AC   Q0SH07;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=RHA1_ro01355;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG93179.1; -; Genomic_DNA.
DR   RefSeq; WP_009474062.1; NC_008268.1.
DR   AlphaFoldDB; Q0SH07; -.
DR   SMR; Q0SH07; -.
DR   STRING; 101510.RHA1_ro01355; -.
DR   EnsemblBacteria; ABG93179; ABG93179; RHA1_ro01355.
DR   KEGG; rha:RHA1_ro01355; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000008710; 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..366
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352588"
SQ   SEQUENCE   366 AA;  38830 MW;  0AF723DDFA589E2A CRC64;
     MSGSNDLRIA VLGVGMMGAD HVARITERIK GATVAVVNDY FIEKAEQIAA GIPGCRVIGD
     PLDAIADPDV DAVVLATPGP THEKQLLACL EHGKPVMCEK PLTTDVATSL EIVKREAELG
     KKLIQVGFMR RFDHEYEQLK TLIDDGTFGQ VLLAHCVHRN PAVPPSFDSS MIVKDSLVHE
     VDVTRFLFDE EITSVHILRP AANPGAPEGL QDPQIALFST ESGRHVDVEV FVTTGVAYEV
     RTEIVAEKGS AFIGLDVGLV RKFGTGAGNG RSGAGMSGGE ITPSFKERFG QAYDVEIQRW
     VNAARTGAET GNYIDGPGAW DGYAAAAVCA AGVQSLETGE RVAVDMVDRS SIPGAEPAER
     PIGPGA