ID IOLG_KINRD Reviewed; 329 AA.
AC A6WFC5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 24-JAN-2024, entry version 86.
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=Krad_4051;
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS05514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000750; ABS05514.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012086198.1; NC_009664.2.
DR AlphaFoldDB; A6WFC5; -.
DR SMR; A6WFC5; -.
DR STRING; 266940.Krad_4051; -.
DR KEGG; kra:Krad_4051; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_1_11; -.
DR Proteomes; UP000001116; 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 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; Oxidoreductase; Reference proteome.
FT CHAIN 1..329
FT /note="Inositol 2-dehydrogenase"
FT /id="PRO_0000352570"
SQ SEQUENCE 329 AA; 34862 MW; 2628A4CBDD705353 CRC64;
MRVAVLGVGM MGQDHARRLA TLTKGAQLVA VSDVDAARTD AVAAELGVRA VHDPAAAIAD
PEVDAVVIAT PGFTHEGLVL EAIAAGKPTL CEKPLTTSPE TARAVVEAER ALGRPLVQVG
FMRRFDAEYE QLRALVASRE LGRPLFLHCV HRNATTPPNF NSEMLILDSV VHEVDIARFL
LGEEITAITV LTPGRTAHAP EGLQDPQFVL METASGTLVD VEIFVNTTFG YEVRTELVAE
RGSAMTGLGV GLVQHSAAGW GGRIAADFKQ RFGAAYDTEF QRWVDAVRSG AGVDGPGVWD
GYAAAAVCAA GVQSLRTGRR VEVDLGARS
//
