ID   IOLG_PARDP              Reviewed;         336 AA.
AC   A1B2N1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Pden_1678;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
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}.
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DR   EMBL; CP000489; ABL69775.1; -; Genomic_DNA.
DR   RefSeq; WP_011747973.1; NC_008686.1.
DR   AlphaFoldDB; A1B2N1; -.
DR   SMR; A1B2N1; -.
DR   STRING; 318586.Pden_1678; -.
DR   PRIDE; A1B2N1; -.
DR   EnsemblBacteria; ABL69775; ABL69775; Pden_1678.
DR   KEGG; pde:Pden_1678; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_5; -.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000000361; Chromosome 1.
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_0000352579"
SQ   SEQUENCE   336 AA;  36484 MW;  1A680FC00718C622 CRC64;
     MTLKIGVIGT GAIGQDHTRR INQVLAGARV AALNDVNRAN AEACQRDHAP EARIFDDPHA
     LIRDAEVDAI LVCSWGQTHE EYVLAAIAAG KPCFCEKPLA TTAEGARRIV EAEEAAGKRL
     VQVGFMRRYD PGYVALKKAV AEVTGAPLMV HAAHRNPRVG ENYLTPMAIH DTLIHEIDVL
     RWLLDDDYVG ARVLFPRKSP RAHEKLRDPQ VVVLETARGV VIDVEVFVNC HYGYDIQCEI
     VGEDGIARLP EPMGIQTRSG AVLGQPILMD WKDRFIDSYD YELADFLKAA ARGTAAGPTA
     WDGYVAAVTA DACVAAQEAG GESVAIELPA RPALYA