ID I2DLU9_9BURK Unreviewed; 337 AA.
AC I2DLU9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=MYA_1261 {ECO:0000313|EMBL:AFJ85625.1};
OS Burkholderia sp. KJ006.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ85625.1, ECO:0000313|Proteomes:UP000010108};
RN [1] {ECO:0000313|EMBL:AFJ85625.1, ECO:0000313|Proteomes:UP000010108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ85625.1,
RC ECO:0000313|Proteomes:UP000010108};
RX PubMed=22843575; DOI=10.1128/JB.00821-12;
RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT Strain KJ006.";
RL J. Bacteriol. 194:4432-4433(2012).
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; CP003514; AFJ85625.1; -; Genomic_DNA.
DR RefSeq; WP_011884463.1; NC_017920.1.
DR AlphaFoldDB; I2DLU9; -.
DR SMR; I2DLU9; -.
DR KEGG; buk:MYA_1261; -.
DR PATRIC; fig|416344.3.peg.1284; -.
DR HOGENOM; CLU_023194_0_1_4; -.
DR Proteomes; UP000010108; Chromosome 1.
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..125
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 137..321
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 337 AA; 36533 MW; 97580B8727770171 CRC64;
MTLQIGVIGC GAIGQDHIRR LTRTLSGARV VAVNDIDPQQ ARDAVTKYGL DAEIYGDGHD
VVAAADVQAL LVTSWGPTHE AFVLDAIAHG KPVFCEKPLA VTADGCMRIV EAEVAHGKRL
VQVGFMRPYD EGYRALKRVI DSGEIGAPLM LHCAHRNQSV GERYTTDMAI TDTLIHELDV
LRWLLGEDYA SAQVVYPKKT RHASAHLADP QIVLLETVSG VRIDVEIFVN CQYGYDIQCE
VVGENGIAKL PDPPAVGLKH AARQSVEIMT DWKERFIASY DVELQAFIDG VRAGALTGPS
AWDGYAAAVA ADACVRAQRS AAVEPIAMAE RPAFYRG
//
