ID   IOLG_DELAS              Reviewed;         337 AA.
AC   A9BZG3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-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}; OrderedLocusNames=Daci_2925;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-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; CP000884; ABX35563.1; -; Genomic_DNA.
DR   RefSeq; WP_012204773.1; NC_010002.1.
DR   AlphaFoldDB; A9BZG3; -.
DR   SMR; A9BZG3; -.
DR   STRING; 398578.Daci_2925; -.
DR   PRIDE; A9BZG3; -.
DR   EnsemblBacteria; ABX35563; ABX35563; Daci_2925.
DR   KEGG; dac:Daci_2925; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_4; -.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000000784; 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..337
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352568"
SQ   SEQUENCE   337 AA;  36323 MW;  0DDFF42E638AE308 CRC64;
     MTLQIGVIGC GAIGQDHVRR MYQTLSGARV VAVTDIDAQQ VREVMARHGP DIEAFDSGPA
     LIAAPQVQAV LVTSWGPTHE ELVLAAIAQG KPVFCEKPLA VTAAGCLRIV QAEMAHGQRL
     VQVGFMRPYD AGYRALRQVI ASGQIGAPLM VHCAHRNPCV ADGYTTGMAI TDTLIHELDV
     LRWLLDDEYA SAQVVYPKRT RHALPHLADP QIVLLETVGG IRIDVEVFVN CRYGYDIQCE
     VVGETGIARM PDPAAVPLKS AAMYSIPILT DWKQRFMAAY DVELQAFIDG VRGQRLTGPS
     AWDAHAAAVA ADACVLAQSS GAVERMAAAP RPAFYQS