IOLG_YERE8
ID IOLG_YERE8 Reviewed; 337 AA.
AC A1JSK7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE EC=1.1.1.18 {ECO:0000255|HAMAP-Rule:MF_01671};
DE AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE Short=MI 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
GN Name=iolG {ECO:0000255|HAMAP-Rule:MF_01671}; OrderedLocusNames=YE4026;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC inositol (2KMI or 2-inosose). {ECO:0000255|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:0000255|HAMAP-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; AM286415; CAL14044.1; -; Genomic_DNA.
DR RefSeq; WP_011817367.1; NC_008800.1.
DR RefSeq; YP_001008169.1; NC_008800.1.
DR AlphaFoldDB; A1JSK7; -.
DR SMR; A1JSK7; -.
DR STRING; 393305.YE4026; -.
DR EnsemblBacteria; CAL14044; CAL14044; YE4026.
DR KEGG; yen:YE4026; -.
DR PATRIC; fig|393305.7.peg.4286; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_1_6; -.
DR OMA; VNCKYGY; -.
DR Proteomes; UP000000642; 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..337
FT /note="Inositol 2-dehydrogenase"
FT /id="PRO_0000352599"
SQ SEQUENCE 337 AA; 37150 MW; 10508CE417F0707F CRC64;
MSLNIGVIGT GAIGQDHIRR CSKVLQGSRI VAVTDINRES ATKVIRDLGI EANVYADGYE
VINAKEVEAV LVTSWGPSHE EFVLAAVAAG KYVFCEKPLA VTAEGCKRIV EAEAAQGKRL
VQVGFMRPYD QGYRALKDVI TSGKIGEPLM LHCAHRNPRV GDNYTTSMAI TDTLIHEIDV
LRWLLDDDYV SVQVVFPRKA KHAKTHLRDP QVVLFETAKG TRIDVEIFVN CQYGYDIQCE
VVGDSGIAKL PEPSSVLLRS EARLSNEILT DWKDRFIDAY DVELQAFIND VLAEKLTGPS
AWDGFAAAVT ADACIAAQES GQIVPIRLPQ RPDFYDK