ID   IOLG_STRCO              Reviewed;         342 AA.
AC   Q9X7U5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=SCO7254;
GN   ORFNames=SC5H1.38;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939131; CAB42963.1; -; Genomic_DNA.
DR   PIR; T35354; T35354.
DR   RefSeq; NP_631310.1; NC_003888.3.
DR   RefSeq; WP_011031545.1; NZ_VNID01000019.1.
DR   AlphaFoldDB; Q9X7U5; -.
DR   SMR; Q9X7U5; -.
DR   STRING; 100226.SCO7254; -.
DR   GeneID; 1102692; -.
DR   KEGG; sco:SCO7254; -.
DR   PATRIC; fig|100226.15.peg.7356; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   InParanoid; Q9X7U5; -.
DR   OMA; VNCKYGY; -.
DR   PhylomeDB; Q9X7U5; -.
DR   Proteomes; UP000001973; 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..342
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352598"
SQ   SEQUENCE   342 AA;  36020 MW;  2196592F0116AEAC CRC64;
     MSELLGVAVL GAGHMGADHI RRVDQVVSGA RVAAVADPDA ERAKEAVGGI GGTGRITVHT
     DVEAALDAPG VEAVLIASPG EAHEEALLAA FARGLPVLCE KPMAPNSAGA LRVVEAEARL
     GRRLAQIGFM RRYDAEYRQL KSLLDGGRLG RPLMLHCVHR NVSSPPHFTS AMLINSSVSH
     EIDAARWLLG QELSAVTVLR PRPSAGAPEG LLDPQLVLFE TEGGAVVDVE VFVNCGFGYE
     VRCEAVCEAG SARIGAAHTM MVTAAGGARE EVPQDYLVRF ADAYDREVQS WVDATRRGLV
     TGPGTWDGYA AAAVAEAGVR ALDTGVRTPV DMAPRPSLHD RA