ID   IOLG_BACLD              Reviewed;         344 AA.
AC   Q65D06; Q62NI2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.18 {ECO:0000255|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.369 {ECO:0000255|HAMAP-Rule:MF_01671};
DE   AltName: Full=Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase/DCI 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG {ECO:0000255|HAMAP-Rule:MF_01671};
GN   OrderedLocusNames=BLi04245, BL00240;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) and D-chiro-
CC       inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-
CC       chiro-inositol (1KDCI), respectively. {ECO:0000255|HAMAP-
CC       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   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-chiro-inositol + NAD(+) = H(+) + NADH + scyllo-inosine;
CC         Xref=Rhea:RHEA:25832, ChEBI:CHEBI:15378, ChEBI:CHEBI:27372,
CC         ChEBI:CHEBI:50920, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.369; Evidence={ECO:0000255|HAMAP-Rule:MF_01671};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 1/7. {ECO:0000255|HAMAP-
CC       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; CP000002; AAU25679.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU43058.1; -; Genomic_DNA.
DR   RefSeq; WP_003177810.1; NC_006322.1.
DR   AlphaFoldDB; Q65D06; -.
DR   SMR; Q65D06; -.
DR   STRING; 279010.BL00240; -.
DR   EnsemblBacteria; AAU25679; AAU25679; BL00240.
DR   KEGG; bld:BLi04245; -.
DR   KEGG; bli:BL00240; -.
DR   PATRIC; fig|279010.13.peg.4329; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_9; -.
DR   OMA; VNCKYGY; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BLIC279010:BLI_RS20875-MON; -.
DR   UniPathway; UPA00076; UER00143.
DR   Proteomes; UP000000606; 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..344
FT                   /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT                   dehydrogenase"
FT                   /id="PRO_0000352557"
SQ   SEQUENCE   344 AA;  38134 MW;  E38043FCDC23589C CRC64;
     MKLRIGVIGT GAIGKEHINR ITNKLAGGEI VAVTDVNQEA AQQVVTDYSL NAKVYPDDDS
     LIAAENVDAV LVTSWGPAHE SSVLKAIKAN KFVFCEKPLA TTAEGCMRIV NEEVKAGKRL
     VQVGFMRRYD SGYVQLKEAI DNRVIGEPLM IHCAHRNPVV GDNYTTDMAV VDTLVHEIDA
     LHWLINDDYE SVQVIYPKKS KNALPHLRDP QIVIIETKGG VVINAEIYVN CKYGYDIQCE
     IVGEDGIVKL PEPSSISLRK DGKFSTDILM DWQRRFVDAY DVEIQDFIDS IQQKGEVSGP
     TAWDGYIAAV TTDACVKAQE SGQKEPVALQ EKPEFYQTFT TVKK