ID   IOLG_BURL3              Reviewed;         337 AA.
AC   Q39H98;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Bcep18194_A4572;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000151; ABB08168.1; -; Genomic_DNA.
DR   RefSeq; WP_011351738.1; NC_007510.1.
DR   AlphaFoldDB; Q39H98; -.
DR   SMR; Q39H98; -.
DR   EnsemblBacteria; ABB08168; ABB08168; Bcep18194_A4572.
DR   GeneID; 45094467; -.
DR   KEGG; bur:Bcep18194_A4572; -.
DR   PATRIC; fig|482957.22.peg.1476; -.
DR   HOGENOM; CLU_023194_0_1_4; -.
DR   OMA; VNCKYGY; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000002705; 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_0000352564"
SQ   SEQUENCE   337 AA;  36631 MW;  4EB1035E0247A917 CRC64;
     MTLQIGVIGC GAIGQDHIRR LTRTLSGARV VAVNDIDPQQ ARDAVTKYGL DAEIYGDGHE
     VVAAADVQAV LVTSWGPTHE AFVLDAIAHG KPVFCEKPLA VTAEGCMRIV EAEVAHGKRL
     VQVGFMRPYD EGYRALKRVI DSGEIGAPLM LHCAHRNQSV GERYTTDMAI TDTLIHELDV
     LRWLLGEDYV STQVVYPKKT RHASSHLADP QIVLLETASG VRIDVEIFVN CQYGYDIQCE
     VVGEQGIAKL PDPPAVGLKH GARQSVEIMT DWKERFIASY DVELQAFIDG VRAHALTGPS
     AWDGYAAAVA ADACVRAQKS GAVEPIAMAE RPAFYRG