IOLG_ALKCK
ID IOLG_ALKCK Reviewed; 346 AA.
AC Q5WKY6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-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=ABC0427;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD62969.1; -; Genomic_DNA.
DR RefSeq; WP_011245288.1; NC_006582.1.
DR AlphaFoldDB; Q5WKY6; -.
DR SMR; Q5WKY6; -.
DR STRING; 66692.ABC0427; -.
DR EnsemblBacteria; BAD62969; BAD62969; ABC0427.
DR KEGG; bcl:ABC0427; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_1_9; -.
DR OMA; VNCKYGY; -.
DR OrthoDB; 1465613at2; -.
DR UniPathway; UPA00076; UER00143.
DR Proteomes; UP000001168; 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..346
FT /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT dehydrogenase"
FT /id="PRO_0000352555"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 38171 MW; 3BBDA0E986095B37 CRC64;
MTVRVGVIGT GAIGQDHIRR LECKLSGAKV TAVTDVNQDL ARKVANTYAK QATVYANDRE
LIAARDVDAV LVASWGPAHE ASVLAALEAG KRVFCEKPLA TTADGCMRIV EAEMAHGKRL
VQVGFMRRFD SGYLQLKQAL EQELVGEPLM VRCIHRNVES AESYTTDMAI TDTLIHEIDV
LHWLLNDEYQ HVRVLYPKKT KHALPHLQDP QLVLLETKKG VIIQAEIFVN CKYGYDIQCE
IAGEEGVISL PDVPAVRLCS NGRKGTEVLQ DWKKRFEAAY DVELQAFIDD GLKDEPASGP
SAWDGYVAAV TADACVKAQE SGREESIELP KKPAFYQHSA ATPEQV
