ID   IOLG_BACVZ              Reviewed;         344 AA.
AC   A7ZAH5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=RBAM_036720;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS76001.1; -; Genomic_DNA.
DR   RefSeq; WP_012118842.1; NC_009725.2.
DR   AlphaFoldDB; A7ZAH5; -.
DR   SMR; A7ZAH5; -.
DR   STRING; 326423.RBAM_036720; -.
DR   EnsemblBacteria; ABS76001; ABS76001; RBAM_036720.
DR   KEGG; bay:RBAM_036720; -.
DR   HOGENOM; CLU_023194_0_1_9; -.
DR   OMA; VNCKYGY; -.
DR   UniPathway; UPA00076; UER00143.
DR   Proteomes; UP000001120; 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.
FT   CHAIN           1..344
FT                   /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT                   dehydrogenase"
FT                   /id="PRO_0000352554"
SQ   SEQUENCE   344 AA;  38131 MW;  7C48F4C22FBED5DA CRC64;
     MNLRIGVIGT GAIGKEHINR ITNKLSGAEI TAVTDVNQEA AQQTVQDFNL NASVYPDDDS
     LLAAENVDAV LVTSWGPAHE SSVLKAIQHG KHVFCEKPLA TTAEGCMRIV EEEMKTGKRL
     VQVGFMRRYD SGYVQLKEAI DNRVVGEPLM IHCAHRNPTV ASNYSTEMAV VDTLVHEIDV
     LHWLVNDDYE SVQVIYPKKS KNALPHLKDP QMVIIETKGG IVINAEIYVN CKYGYDIQCE
     IVGEDGIIKL PEPSSISLRK EGKFSTDILM DWQRRFVAAY DVEIQDFIDS IRNKGEVSGP
     TAWDGYIAAV TTDACVKAQE SGQKEPVALQ EKPAFYQSFT TVNK