IOLG_SALTY
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 03-AUG-2022, entry version 103.
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; Proteobacteria; 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; Q8ZK57; -.
DR DNASU; 1255951; -.
DR EnsemblBacteria; AAL23245; AAL23245; STM4425.
DR GeneID; 1255951; -.
DR KEGG; stm:STM4425; -.
DR PATRIC; fig|99287.12.peg.4653; -.
DR HOGENOM; CLU_023194_0_1_6; -.
DR OMA; VNCKYGY; -.
DR PhylomeDB; Q8ZK57; -.
DR BioCyc; SENT99287:STM4425-MON; -.
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 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 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
