ID   IOLG2_SACEN             Reviewed;         339 AA.
AC   A4FID1;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Inositol 2-dehydrogenase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG2 {ECO:0000255|HAMAP-Rule:MF_01671}; OrderedLocusNames=SACE_4537;
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; CAM03806.1; -; Genomic_DNA.
DR   RefSeq; WP_009951448.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FID1; -.
DR   SMR; A4FID1; -.
DR   STRING; 405948.SACE_4537; -.
DR   PRIDE; A4FID1; -.
DR   EnsemblBacteria; CAM03806; CAM03806; SACE_4537.
DR   KEGG; sen:SACE_4537; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OMA; RKPVMCE; -.
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..339
FT                   /note="Inositol 2-dehydrogenase 2"
FT                   /id="PRO_0000352591"
SQ   SEQUENCE   339 AA;  35899 MW;  CE088D69EE28AB6F CRC64;
     MTMNIGVIGC GLMGADHIRT LTTAVSGARV AAVNDADEGR AAGAAAEAEG ARVHSDPFGL
     IDDAEVDAVV VASADETHEE FALACVRAGK PVLCEKPLAT TSEACLRVVE AEMRGGRPLV
     QVGFMRRFDP SYLEMKRVLD SGRIGRALML HSVHRNAGYP PALPDSALIT GTGVHDIDIA
     RWLLGQEIVT ATAHTPRRSG LARPDFQDTR FLVLETENGV LVDVEIFVNA GYGYDVRGEL
     VGELGSISLH PPATLTTRYE GLEGRPVARD FRPRFQDAYR NELQAWVTAG ASGEVRGATA
     WDGYASAAVA EACLHSVATG STAPVEIAPQ PALYAPLAA