Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase

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Reviewed, UniProtKB/Swiss-Prot P26935 (IOLG_BACSU)

Last modified June 16, 2009. Version 70. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
    EC=1.1.1.18
    EC=1.1.1.n6
Alternative name(s):
    Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
      Short name=MI 2-dehydrogenase/DCI 3-dehydrogenase

Gene names

Name:	iolG
Synonyms:	idh
Ordered Locus Names:	BSU39700
ORF Names:	E83G

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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. Ref.5 Ref.6
Catalytic activity	Myo-inositol + NAD⁺ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH. Ref.6 D-chiro-inositol + NAD⁺ = 2,3,5/4,6-pentahydroxycyclohexanone + NADH. Ref.6
Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 1/7. HAMAP MF_01671
Subunit structure	Homotetramer. Ref.5
Induction	By inositol. Subjected to catabolite repression. Ref.1
Sequence similarities	Belongs to the gfo/idh/mocA family.
biophysicochemical properties	Kinetic parameters: K_M=0.036 mM for NADH (in the presence of 5 mM 2-inosose at 25 degrees Celsius and pH 7) HAMAP MF_01671 K_M=0.23 mM for NAD (in the presence of 40 mM myo-inositol at 25 degrees Celsius and pH 9) K_M=1.61 mM for 2-inosose (in the presence of 0.1 mM NADH at 25 degrees Celsius and pH 7) K_M=18.2 mM for myo-inositol (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9) K_M=55.6 mM for alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9) K_M=167 mM for D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9) K_M=190 mM for D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9) V_max=42 µmol/min/mg enzyme for 2-inosose reduction reaction (at 25 degrees Celsius and pH 7) V_max=21 µmol/min/mg enzyme for myo-inositol oxidation reaction (at 25 degrees Celsius and pH 9) V_max=13.5 µmol/min/mg enzyme with for alpha-D-glucose oxidation reaction (at 25 degrees Celsius and pH 9) V_max=7.3 µmol/min/mg enzyme for D-glucose oxidation reaction (at 25 degrees Celsius and pH 9) V_max=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.

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Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	inositol catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro inositol 2-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 344

344

Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase HAMAP MF_01671

PRO_0000091774

Experimental info

Sequence conflict

145

N → I in AAT78431. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P26935-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2FCE908D4E2C332F
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FASTA

344

38,352

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis inositol dehydrogenase-encoding gene (idh): sequence and expression in Escherichia coli." Fujita Y., Shindo K., Miwa Y., Yoshida K. Gene 108:121-125(1991) [PubMed: 1761221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: 168 / 60015.
[2]	"Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon." Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y. Microbiology 140:2289-2298(1994) [PubMed: 7952181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[3]	"Probing the active site of Bacillus subtilis myo-inositol dehydrogenase." Daniellou R., Phenix C.P., Tam P.H., Laliberte M.C., Palmer D.R.J. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[5]	"Purification and properties of Bacillus subtilis inositol dehydrogenase." Ramaley R., Fujita Y., Freese E. J. Biol. Chem. 254:7684-7690(1979) [PubMed: 112095] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: 168 / 60015.
[6]	"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." Yoshida K., Yamaguchi M., Morinaga T., Ikeuchi M., Kinehara M., Ashida H. Appl. Environ. Microbiol. 72:1310-1315(2006) [PubMed: 16461681] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: 168 / 60015.

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Cross-references

Sequence databases
	M76431 Genomic DNA. Translation: AAA22543.1. D14399 Genomic DNA. Translation: BAA03296.1. AY676876 Genomic DNA. Translation: AAT78431.1. Z99124 Genomic DNA. Translation: CAB16006.1.
PIR	JH0511.
RefSeq	NP_391849.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	937615.
GenomeReviews	Gene locus BSU39700 in contig AL009126_GR.
KEGG	bsu:BSU39700.
NMPDR	fig\|224308.1.peg.3975.
Organism-specific databases
SubtiList	BG10669. iolG. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P26935.
OMA	P26935. DWKDRFI.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3966-MON.
BRENDA	1.1.1.18. 150.
Family and domain databases
HAMAP	MF_01671. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR000683. Oxidoreductase_N. IPR004104. OxRdtase_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01408. GFO_IDH_MocA. 1 hit. PF02894. GFO_IDH_MocA_C. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

IOLG_BACSU

Accession

Primary (citable) accession number: P26935
Secondary accession number(s): Q6B6R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents