ID   IOLG3_SACEN             Reviewed;         338 AA.
AC   A4FIQ1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Inositol 2-dehydrogenase 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG3 {ECO:0000255|HAMAP-Rule:MF_01671}; OrderedLocusNames=SACE_4657;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM03926.1; -; Genomic_DNA.
DR   RefSeq; WP_009943452.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FIQ1; -.
DR   SMR; A4FIQ1; -.
DR   STRING; 405948.SACE_4657; -.
DR   EnsemblBacteria; CAM03926; CAM03926; SACE_4657.
DR   KEGG; sen:SACE_4657; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OMA; FRDHPCP; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000006728; 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..338
FT                   /note="Inositol 2-dehydrogenase 3"
FT                   /id="PRO_0000352592"
SQ   SEQUENCE   338 AA;  36130 MW;  905B0B425EF22E3C CRC64;
     MTVRVGVIGT GMIGQDHIRR LTRVVTGAEI VAVTDIDADR AASVAGGVGA RTMPSGADVI
     GSADVDAVLV TSWGPTHAEH VLAAIEAGKA VFCEKPLATE VEDCLRIVEA ESARGKRLVQ
     VGFMRRYDAG YREMKELVDA GGIGTPLMAH CVHRNPTVPE TYHSAMAAQD TAVHEIDTLR
     WLLDDEIVSA QVIRPRRTSK RFEHLQDPQI MLFETESGAR IDVEVFVNCQ YGYDIQCEVV
     GESGTVRLPD PARTGLPSAG SVRAAITQDW KQRFADAFDA ELQSWVDSVA HGAAGGPSAW
     DGYAATAICG ATVEALHSGQ VVPVALKDRP GLYGGNNQ