ID   IOLG_BURCM              Reviewed;         337 AA.
AC   Q0BG57;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
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=Bamb_1308;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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; CP000440; ABI86866.1; -; Genomic_DNA.
DR   RefSeq; WP_011656629.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BG57; -.
DR   SMR; Q0BG57; -.
DR   STRING; 339670.Bamb_1308; -.
DR   EnsemblBacteria; ABI86866; ABI86866; Bamb_1308.
DR   GeneID; 44691985; -.
DR   KEGG; bam:Bamb_1308; -.
DR   PATRIC; fig|339670.21.peg.240; -.
DR   eggNOG; COG0673; Bacteria.
DR   OMA; VNCKYGY; -.
DR   Proteomes; UP000000662; 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.
FT   CHAIN           1..337
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352558"
SQ   SEQUENCE   337 AA;  36600 MW;  433489B8F8262409 CRC64;
     MTLQIGVIGC GAIGQDHIRR LTRTLSGARV VAVNDIDPQQ ARDAVTKYGL DAEIYGDGHE
     VVAAADVQAV LVTSWGPTHE AFVLDAIAHG KPVFCEKPLA VTAQGCMRIV EAEVAHGRRL
     VQVGFMRPYD EGYRALKHVI DSGEIGAPLM LHCAHRNQSV GERYTTDMAI TDTLIHELDV
     LRWLLGEDYT SAQVVYPKKT RHASAHLADP QIVLLETASG VRIDVEIFVN CQYGYDIQCE
     VVGENGIAKL PDPPAVGLKH AARRSVEIMT DWKERFIASY DVELQAFIDG VRQGALTGPS
     AWDGYAAAVA ADACVRAQQS GAVEPIAMAE RPAFYRG