ID   IOLG1_SACEN             Reviewed;         337 AA.
AC   A4FDY3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Inositol 2-dehydrogenase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01671};
GN   Name=iolG1 {ECO:0000255|HAMAP-Rule:MF_01671};
GN   OrderedLocusNames=SACE_2980;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; 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 /
RC   NRRL 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(+) = scyllo-inosose + NADH + H(+);
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=CAM02258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM420293; CAM02258.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029621968.1; NC_009142.1.
DR   AlphaFoldDB; A4FDY3; -.
DR   SMR; A4FDY3; -.
DR   STRING; 405948.SACE_2980; -.
DR   GeneID; 306459701; -.
DR   KEGG; sen:SACE_2980; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OrthoDB; 9815825at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0050112; F:inositol 2-dehydrogenase (NAD+) 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; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01671; IolG; 1.
DR   InterPro; IPR050424; Gfo-Idh-MocA_inositol_DH.
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..337
FT                   /note="Inositol 2-dehydrogenase 1"
FT                   /id="PRO_0000352590"
SQ   SEQUENCE   337 AA;  35446 MW;  0C12AEBE8A6A7B95 CRC64;
     MTVRVGVVGT GVMGADHVRT LTGGVAGARV VAVSDADQGR GRAVAAEAGD EVVFHADPVD
     LIGDAGVDAV VVASPDHTHE ALATACVEAG KPVLCEKPLA ATAADCLRIV AHEVAKGRRL
     VQAGYMRRFD PSYVDMKRAL DAGSIGDPVL VHCVHRNARA LHFFTPEMPF TSAAVHEFDV
     VRWLLSSEIV RVTVHRTRSS SRAAARLADP RLLVLETAAG VTVDVEVFVN AQYGYDVRCE
     LVGELGTVSL ALPSTTVVRA GGAEGVAVHA DFRTRFAEAY RLQLQAWVDA AARGEACGPS
     AWDGYAATAV AEACLRAQED GTPVEVELAD KPALYGT
//