ID   IOLG_MYCS2              Reviewed;         345 AA.
AC   A0R191; I7GCN3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 98.
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};
GN   OrderedLocusNames=MSMEG_4666, MSMEI_4547;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK74556.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41001.1; -; Genomic_DNA.
DR   RefSeq; WP_011729996.1; NZ_SIJM01000004.1.
DR   RefSeq; YP_888929.1; NC_008596.1.
DR   AlphaFoldDB; A0R191; -.
DR   SMR; A0R191; -.
DR   STRING; 246196.MSMEI_4547; -.
DR   EnsemblBacteria; ABK74556; ABK74556; MSMEG_4666.
DR   EnsemblBacteria; AFP41001; AFP41001; MSMEI_4547.
DR   GeneID; 66735983; -.
DR   KEGG; msg:MSMEI_4547; -.
DR   KEGG; msm:MSMEG_4666; -.
DR   PATRIC; fig|246196.19.peg.4559; -.
DR   eggNOG; COG0673; Bacteria.
DR   OMA; VNCKYGY; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..345
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352576"
SQ   SEQUENCE   345 AA;  36836 MW;  A2137030D06F738D CRC64;
     MSDLRVAVLG VGVMGADHVE RLSTRIAGVK VAVVNDFIET RAEEIAAGVP GCRVVSDPLE
     AIADPDVDAV VLATPGPTHD KQLLACLEQR KPVLCEKPLT TDVDSALDVV RREAELGVRL
     IQVGFMRRFD PEYAELKTLI DAGEFGQPLV LHCVHRNAAV PPSFDSTMIV KDSLVHEVDV
     TRFLFDEEIA SVHILRPTPN PGAPEGIQDP QIAIMKTPSG KHVDVELFVT TGVGYEVRTE
     LVAEKGTAMI GLDVGLIRKG VPGTWGGAIA PDFRVRFGTA YDIEFQRWVA AVRHGIATGS
     DDYTDGPTAW DGYAAAAVCA AGVESLAGGQ PVEVKMVERA SINGA