ID   IOLG_ALKHC              Reviewed;         348 AA.
AC   Q9KAH1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BH2316;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06035.1; -; Genomic_DNA.
DR   PIR; D83939; D83939.
DR   RefSeq; WP_010898472.1; NC_002570.2.
DR   AlphaFoldDB; Q9KAH1; -.
DR   SMR; Q9KAH1; -.
DR   STRING; 272558.10174936; -.
DR   EnsemblBacteria; BAB06035; BAB06035; BAB06035.
DR   KEGG; bha:BH2316; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_9; -.
DR   OMA; VNCKYGY; -.
DR   OrthoDB; 1465613at2; -.
DR   UniPathway; UPA00076; UER00143.
DR   Proteomes; UP000001258; 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..348
FT                   /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT                   dehydrogenase"
FT                   /id="PRO_0000352556"
SQ   SEQUENCE   348 AA;  38788 MW;  50EE88A0BEA9E5C8 CRC64;
     MTLRFGVIGT GAIGREHMKR IENKLSGGKI VAVTDMNQEA AKQVVTQMKL EADVYPDDRS
     LVAADNVDAV LVTSWGPAHE ANVLAAIEAG KYVFVEKPLA TTAEGCMKII KAEMNHGKRL
     VQVGFMRRYD KGYVQLKKAI DDHFIGEPLM VRCAHRNPEV GESYIDDMAI HDTLIHEIDV
     LHWLIDDEYE SVSVSFPKKT KHALPHLRDP RVVTLETKGG VLITAEVFVN CKYGYDIQCE
     VIREEGIASL PEVDSISFRK RATLGTNILM DWKQRFIEAY DVELQHFIDS IKQSGEPSGP
     NAWDGYVAAI TADAALKASN SGQKQFISLK EKPAFYSVKK ENAHEAML