ID IOLG_SALPB Reviewed; 336 AA.
AC A9N564;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=SPAB_05572;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX70841.1; -; Genomic_DNA.
DR RefSeq; WP_000172704.1; NC_010102.1.
DR AlphaFoldDB; A9N564; -.
DR SMR; A9N564; -.
DR KEGG; spq:SPAB_05572; -.
DR PATRIC; fig|1016998.12.peg.5223; -.
DR HOGENOM; CLU_023194_0_1_6; -.
DR BioCyc; SENT1016998:SPAB_RS22745-MONOMER; -.
DR Proteomes; UP000008556; 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 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..336
FT /note="Inositol 2-dehydrogenase"
FT /id="PRO_0000352594"
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
//
