ID A0A0T9XKK2_SALET Unreviewed; 336 AA.
AC A0A0T9XKK2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE EC=1.1.1.18 {ECO:0000256|HAMAP-Rule:MF_01671};
DE AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE Short=MI 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
GN Name=iolG {ECO:0000256|HAMAP-Rule:MF_01671,
GN ECO:0000313|EMBL:SUE49084.1};
GN Synonyms=iolG1 {ECO:0000313|EMBL:EDG4995712.1};
GN ORFNames=B7N00_16975 {ECO:0000313|EMBL:EDG5018639.1}, B7N01_14900
GN {ECO:0000313|EMBL:EDG4995712.1}, B7N35_16190
GN {ECO:0000313|EMBL:EDG5127564.1}, B7N72_17690
GN {ECO:0000313|EMBL:EDG5371929.1}, B7N78_17905
GN {ECO:0000313|EMBL:EDG5281639.1}, B7N80_12720
GN {ECO:0000313|EMBL:EDG5289241.1}, B7N84_18435
GN {ECO:0000313|EMBL:EDG5268313.1}, DRU31_16315
GN {ECO:0000313|EMBL:EBS2453856.1}, E0916_17290
GN {ECO:0000313|EMBL:ECF1447701.1}, EJV93_18195
GN {ECO:0000313|EMBL:ECA2723117.1}, ERS008198_03201
GN {ECO:0000313|EMBL:CNU62944.1}, ERS008202_03377
GN {ECO:0000313|EMBL:CNU71656.1}, ERS008207_02114
GN {ECO:0000313|EMBL:CNU20360.1}, EWC73_14190
GN {ECO:0000313|EMBL:ECE8537340.1}, G0B02_18465
GN {ECO:0000313|EMBL:HAC6381061.1}, G0D18_21360
GN {ECO:0000313|EMBL:HAC6683150.1}, G2206_13320
GN {ECO:0000313|EMBL:HAE0435738.1}, NCTC5754_04072
GN {ECO:0000313|EMBL:SUE49084.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE49084.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000041314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU71656.1,
RC ECO:0000313|Proteomes:UP000039541}, A1104
RC {ECO:0000313|EMBL:CNU62944.1, ECO:0000313|Proteomes:UP000041314}, and
RC D4891 {ECO:0000313|EMBL:CNU20360.1,
RC ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6381061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381061.1}, M123
RC {ECO:0000313|EMBL:HAC6683150.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435738.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE49084.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE49084.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2453856.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4995712.1}, 138330
RC {ECO:0000313|EMBL:EDG5289241.1}, 143652
RC {ECO:0000313|EMBL:EDG5371929.1}, 273631
RC {ECO:0000313|EMBL:EDG5018639.1}, 330535
RC {ECO:0000313|EMBL:EDG5268313.1}, 333944
RC {ECO:0000313|EMBL:EDG5281639.1}, 337042
RC {ECO:0000313|EMBL:EDG5127564.1}, 387147
RC {ECO:0000313|EMBL:EBS2453856.1}, 470200
RC {ECO:0000313|EMBL:ECE8537340.1}, 598023
RC {ECO:0000313|EMBL:ECA2723117.1}, and 692616
RC {ECO:0000313|EMBL:ECF1447701.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAC6381061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6381061.1}, M123
RC {ECO:0000313|EMBL:HAC6683150.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435738.1};
RG NCBI Pathogen Detection Project;
RL Submitted (AUG-2018) 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:0000256|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:0000256|HAMAP-Rule:MF_01671};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01671}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000256|HAMAP-
CC Rule:MF_01671}.
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DR EMBL; CQPD01000018; CNU20360.1; -; Genomic_DNA.
DR EMBL; CQPA01000029; CNU62944.1; -; Genomic_DNA.
DR EMBL; CQPC01000051; CNU71656.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000013; EBS2453856.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000011; ECA2723117.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000012; ECE8537340.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000012; ECF1447701.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000015; EDG4995712.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000012; EDG5018639.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000014; EDG5127564.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000012; EDG5268313.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000014; EDG5281639.1; -; Genomic_DNA.
DR EMBL; AAMEML010000012; EDG5289241.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000023; EDG5371929.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000014; HAC6381061.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000024; HAC6683150.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000013; HAE0435738.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE49084.1; -; Genomic_DNA.
DR RefSeq; WP_000172704.1; NZ_WFIN01000007.1.
DR AlphaFoldDB; A0A0T9XKK2; -.
DR SMR; A0A0T9XKK2; -.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000041314; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01671};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01671}.
FT DOMAIN 4..124
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 137..322
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
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
//
