ID   IOLG2_MYCVP             Reviewed;         342 AA.
AC   A1TC97;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Inositol 2-dehydrogenase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG2 {ECO:0000255|HAMAP-Rule:MF_01671}; OrderedLocusNames=Mvan_4020;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000511; ABM14797.1; -; Genomic_DNA.
DR   RefSeq; WP_011781177.1; NC_008726.1.
DR   AlphaFoldDB; A1TC97; -.
DR   SMR; A1TC97; -.
DR   STRING; 350058.Mvan_4020; -.
DR   PRIDE; A1TC97; -.
DR   EnsemblBacteria; ABM14797; ABM14797; Mvan_4020.
DR   KEGG; mva:Mvan_4020; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OMA; RKPVMCE; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000009159; 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..342
FT                   /note="Inositol 2-dehydrogenase 2"
FT                   /id="PRO_0000352578"
SQ   SEQUENCE   342 AA;  36999 MW;  8E95AFF8C535F794 CRC64;
     MSELRVAVLG VGVMGADHVA RITSRISGAR VSVVNDYVTE KAEQIASEVD GCRAVVDPLD
     AIADPEVDAV VLATPGSTHE KQLLACLDHR KPVMCEKPLT TDVFTSLEIA RREAELECPL
     IQVGFMRRFD DEYMRLKALL DGGELGQPLV MHCVHRNPGV PSYFDSSLIV KDSLVHEVDV
     TRYLFGEEIA SVQIVRPVSN PAAPEGVIDP QIAILRTVSG RHVDVELFVT TGVAYEVRTE
     VVGERGSAMI GLDVGLIRKS APGTWGGLIA PGFRERFGRA YDTEIQRWVD AVRAGTNIDG
     PTAWDGYAAA AVCAAGVESL ESGLPVPVHL AERPDRSTIR PR