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Entry: IOLG_SALTY
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ID   IOLG_SALTY              Reviewed;         336 AA.
AC   Q8ZK57;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 110.
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=STM4425;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL23245.1; -; Genomic_DNA.
DR   RefSeq; NP_463286.1; NC_003197.2.
DR   RefSeq; WP_000172704.1; NC_003197.2.
DR   PDB; 3EC7; X-ray; 2.15 A; A/B/C/D/E/F/G/H=1-336.
DR   PDBsum; 3EC7; -.
DR   AlphaFoldDB; Q8ZK57; -.
DR   SMR; Q8ZK57; -.
DR   STRING; 99287.STM4425; -.
DR   PaxDb; 99287-STM4425; -.
DR   DNASU; 1255951; -.
DR   GeneID; 1255951; -.
DR   PATRIC; fig|99287.12.peg.4653; -.
DR   HOGENOM; CLU_023194_0_1_6; -.
DR   OMA; VNCKYGY; -.
DR   PhylomeDB; Q8ZK57; -.
DR   BioCyc; SENT99287:STM4425-MONOMER; -.
DR   EvolutionaryTrace; Q8ZK57; -.
DR   Proteomes; UP000001014; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   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   1: Evidence at protein level;
KW   3D-structure; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Inositol 2-dehydrogenase"
FT                   /id="PRO_0000352595"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           12..23
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          28..34
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           40..48
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           79..88
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           103..116
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          121..124
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           131..142
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          147..156
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           174..185
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          189..195
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          209..216
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          221..227
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          235..248
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          256..259
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           276..292
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           301..320
FT                   /evidence="ECO:0007829|PDB:3EC7"
FT   HELIX           333..335
FT                   /evidence="ECO:0007829|PDB:3EC7"
SQ   SEQUENCE   336 AA;  37267 MW;  5E66D7BC40158197 CRC64;
     MTLKAGIVGI GMIGSDHLRR LANTVSGVEV VAVCDIVAGR AQAALDKYAI EAKDYNDYHD
     LINDKDVEVV IITASNEAHA DVAVAALNAN KYVFCEKPLA VTAADCQRVI EAEQKNGKRM
     VQIGFMRRYD KGYVQLKNII DSGEIGQPLM VHGRHYNAST VPEYKTPQAI YETLIHEIDV
     MHWLLNEDYK TVKVYFPRQS SLVTTLRDPQ LVVMETTSGI NIVVEVFVNC QYGYDIHCDV
     TGEKGMAELP TVASAAVRKA AKYSTDILVD WKQRFIDAYD IEFQDFFDRL NAGLPPAGPT
     SWDGYLAAVT ADACVKSQET GNTEIVELPS KPDFYK
//
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