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Database: UniProt
Entry: A0A0B0IF23_9BACI
LinkDB: A0A0B0IF23_9BACI
Original site: A0A0B0IF23_9BACI 
ID   A0A0B0IF23_9BACI        Unreviewed;       345 AA.
AC   A0A0B0IF23;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.18 {ECO:0000256|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.369 {ECO:0000256|HAMAP-Rule:MF_01671};
DE   AltName: Full=Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase/DCI 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
GN   Name=iolG {ECO:0000256|HAMAP-Rule:MF_01671};
GN   ORFNames=LQ50_14515 {ECO:0000313|EMBL:KHF39472.1};
OS   Halalkalibacter okhensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF39472.1, ECO:0000313|Proteomes:UP000030832};
RN   [1] {ECO:0000313|EMBL:KHF39472.1, ECO:0000313|Proteomes:UP000030832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA   Prakash J.S.;
RT   "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL   Submitted (SEP-2014) 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:0000256|HAMAP-
CC       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:0000256|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:0000256|HAMAP-Rule:MF_01671};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 1/7. {ECO:0000256|HAMAP-
CC       Rule:MF_01671}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01671}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHF39472.1}.
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DR   EMBL; JRJU01000018; KHF39472.1; -; Genomic_DNA.
DR   RefSeq; WP_034630286.1; NZ_JRJU01000018.1.
DR   AlphaFoldDB; A0A0B0IF23; -.
DR   STRING; 333138.LQ50_14515; -.
DR   eggNOG; COG0673; Bacteria.
DR   OrthoDB; 9815825at2; -.
DR   UniPathway; UPA00076; UER00143.
DR   Proteomes; UP000030832; Unassembled WGS sequence.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PANTHER; PTHR43593; -; 1.
DR   PANTHER; PTHR43593:SF1; INOSITOL 2-DEHYDROGENASE; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01671};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01671}; Reference proteome {ECO:0000313|Proteomes:UP000030832}.
FT   DOMAIN          3..125
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          137..323
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   345 AA;  38261 MW;  0DBA4F21542EDBD0 CRC64;
     MSLRFGVVGT GAIGREHIDR ITNKLSGGKV VAVTDVNQDS ALQTVEQYNL DAVIYPDDVA
     LIADNNVDVV VVTSWGPAHE ATVLAAVEAG KYVFCEKPLA TTADGCMRIV EAEMKQGKKL
     VQVGFMRRYD SGYVQLKEAI DQGEIGQPLM VRAVHRNPEV GENYVTEMAV VDTLIHEIDA
     LHWLVNDDYK SVQVVFPRKT KYAHDKVQDP QLFMIETNSG IVMNVEVFVN CKYGYDIQCE
     VIGEDGVAYL PEFPSVVTRK NGKLSSGILQ DWKYRFMDAY DVEIQDFIDS IGKKGEPQGP
     TSWDGYIAAV TADACVKAQK TGEKEAIRLQ EKPVFYSKDT VCETV
//
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