IOLG_LACPL
ID IOLG_LACPL Reviewed; 350 AA.
AC Q88S38; F9ULG0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=lp_3606;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC80567.1; -; Genomic_DNA.
DR RefSeq; WP_011102248.1; NC_004567.2.
DR RefSeq; YP_004891081.1; NC_004567.2.
DR AlphaFoldDB; Q88S38; -.
DR SMR; Q88S38; -.
DR STRING; 220668.lp_3606; -.
DR EnsemblBacteria; CCC80567; CCC80567; lp_3606.
DR KEGG; lpl:lp_3606; -.
DR PATRIC; fig|220668.9.peg.3010; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_1_9; -.
DR OMA; VNCKYGY; -.
DR PhylomeDB; Q88S38; -.
DR BioCyc; LPLA220668:G1GW0-3054-MON; -.
DR UniPathway; UPA00076; UER00143.
DR Proteomes; UP000000432; 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..350
FT /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT dehydrogenase"
FT /id="PRO_0000352573"
SQ SEQUENCE 350 AA; 39180 MW; B17862B12C4514DD CRC64;
MAEAHVTKVG IVGIGFIGSD HLHRLTKTVA NVDVTAVCDI VPGKAQKALD QQGLTATTYE
DYHDLVNDPN VEVVVCTANN EAHYEIVMAA LKAGKFTFCE KPLALDAKQC MDIIDSEKKL
GRRMLQVGFM RHYAPEYVQM KKMIDDGVIG KPLMMDQRHY NQTQPEEYDS SRSIIETAIH
EIDIDHWLVN DDYANIRVFS PKQTRHVQNA KIQDPQIVMI ETKSGINIIN EVFVRCQYGY
DIKCDVIGEE GVLELPTVPQ VATRLNAQYS TAILTDWKAR FESAYDIEFR DFINHVSQNE
SPVGPSAWDG YIAAVTADAA LKSLAEDGAK QDLDFPSTPA FYTESEKVSE