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UniProtKB/Swiss-Prot entry P26935


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IOLG_BACSU
Primary accession number P26935
Secondary accession number Q6B6R7
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
Synonyms EC 1.1.1.18
EC 1.1.1.n6
Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
MI 2-dehydrogenase/DCI 3-dehydrogenase
Gene name
Name: iolG
Synonyms: idh
OrderedLocusNames: BSU39700
ORFNames: E83G
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=168 / 60015;
DOI=10.1016/0378-1119(91)90496-X; PubMed=1761221 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita Y., Shindo K., Miwa Y., Yoshida K.;
"Bacillus subtilis inositol dehydrogenase-encoding gene (idh): sequence and expression in Escherichia coli.";
Gene 108:121-125(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / BGSC1A1;
PubMed=7952181 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
"Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon.";
Microbiology 140:2289-2298(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Daniellou R., Phenix C.P., Tam P.H., Laliberte M.C., Palmer D.R.J.;
"Probing the active site of Bacillus subtilis myo-inositol dehydrogenase.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=168 / 60015;
PubMed=112095 [NCBI, ExPASy, EBI, Israel, Japan]
Ramaley R., Fujita Y., Freese E.;
"Purification and properties of Bacillus subtilis inositol dehydrogenase.";
J. Biol. Chem. 254:7684-7690(1979).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=168 / 60015;
DOI=10.1128/AEM.72.2.1310-1315.2006; PubMed=16461681 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida K., Yamaguchi M., Morinaga T., Ikeuchi M., Kinehara M., Ashida H.;
"Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome.";
Appl. Environ. Microbiol. 72:1310-1315(2006).
Comments
  • FUNCTION: Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively. Can also use D-glucose and D-xylose, and shows a trace of activity with D-ribose and D-fructose.
  • CATALYTIC ACTIVITY: Myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH.
  • CATALYTIC ACTIVITY: D-chiro-inositol + NAD+ = 2,3,5/4,6-pentahydroxycyclohexanone + NADH.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=0.036 mM for NADH (in the presence of 5 mM 2-inosose at 25 degrees Celsius and pH 7);
    KM=0.23 mM for NAD (in the presence of 40 mM myo-inositol at 25 degrees Celsius and pH 9);
    KM=1.61 mM for 2-inosose (in the presence of 0.1 mM NADH at 25 degrees Celsius and pH 7);
    KM=18.2 mM for myo-inositol (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9);
    KM=55.6 mM for alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9);
    KM=167 mM for D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9);
    KM=190 mM for D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9);
    Vmax=42 µmol/min/mg enzyme for 2-inosose reduction reaction (at 25 degrees Celsius and pH 7);
    Vmax=21 µmol/min/mg enzyme for myo-inositol oxidation reaction (at 25 degrees Celsius and pH 9);
    Vmax=13.5 µmol/min/mg enzyme with for alpha-D-glucose oxidation reaction (at 25 degrees Celsius and pH 9);
    Vmax=7.3 µmol/min/mg enzyme for D-glucose oxidation reaction (at 25 degrees Celsius and pH 9);
    Vmax=6.7 µmol/min/mg enzyme for D-xylose oxidation reaction (at 25 degrees Celsius and pH 9);
    pH dependence:   Optimum pH is 9.5 for inositol 2-dehydrogenase activity;
  • PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 1/7.
  • SUBUNIT: Homotetramer.
  • INDUCTION: By inositol. Subjected to catabolite repression.
  • SIMILARITY: Belongs to the gfo/idh/mocA family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M76431; AAA22543.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D14399; BAA03296.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY676876; AAT78431.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99124; CAB16006.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JH0511; JH0511.
RefSeq NP_391849.1; -.
3D structure databases
ModBase P26935.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3966-MON; -.
Organism-specific databases
SubtiList BG10669; iolG. [Micado]
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050112; Molecular function: inositol 2-dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019310; Biological process: inositol catabolic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01671; -; 1.
PBIL [Tree]
InterPro IPR000683; GFO/IDH/MocA_N.
IPR016040; NAD(P)-bd.
IPR004104; OxRdtase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01408; GFO_IDH_MocA; 1.
PF02894; GFO_IDH_MocA_C; 1.
Pfam graphical view of domain structure.
ProtoNet P26935.
Genome annotation databases
GeneID 937615; -.
GenomeReviews AL009126_GR; BSU39700.
KEGG bsu:BSU39700; -.
NMPDR fig|224308.1.peg.3975; -.
Phylogenomic databases
HOGENOM P26935; -.
Genome annotation databases
CMR P26935; BSU39700.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   344  344     Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase. PRO_0000091774
CONFLICT   145   145        N -> I (in Ref. 3; AAT78431). 
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 38352 Da [This is the MW of the unprocessed precursor] CRC64: 2FCE908D4E2C332F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLRIGVIGT GAIGKEHINR ITNKLSGAEI VAVTDVNQEA AQKVVEQYQL NATVYPNDDS 

        70         80         90        100        110        120 
LLADENVDAV LVTSWGPAHE SSVLKAIKAQ KYVFCEKPLA TTAEGCMRIV EEEIKVGKRL 

       130        140        150        160        170        180 
VQVGFMRRYD SGYVQLKEAL DNHVNGEPLM IHCAHRNPTV GDNYTTDMAV VDTLVHEIDV 

       190        200        210        220        230        240 
LHWLVNDDYE SVQVIYPKKS KNALPHLKDP QIVVIETKGG IVINAEIYVN CKYGYDIQCE 

       250        260        270        280        290        300 
IVGEDGIIKL PEPSSISLRK EGRFSTDILM DWQRRFVAAY DVEIQDFIDS IQKKGEVSGP 

       310        320        330        340 
TAWDGYIAAV TTDACVKAQE SGQKEKVELK EKPEFYQSFT TVQN 

P26935 in FASTA format

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