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Reviewed, UniProtKB/Swiss-Prot Q8NTY7 (IOLG_CORGL)

Last modified February 9, 2010. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Inositol 2-dehydrogenase
    EC=1.1.1.18
Alternative name(s):
    Myo-inositol 2-dehydrogenase
      Short name=MI 2-dehydrogenase
Gene names
Name: iolG
Ordered Locus Names: Cgl0164, cg0204
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose) By similarity. HAMAP MF_01671

Catalytic activity

Myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH. HAMAP MF_01671

Subunit structure

Homotetramer By similarity. HAMAP MF_01671

Sequence similarities

Belongs to the gfo/idh/mocA family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processinositol catabolic process

Inferred from electronic annotation. Source: HAMAP

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

inositol 2-dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Inositol 2-dehydrogenase HAMAP MF_01671
PRO_0000352566

Sequences

Sequence LengthMass (Da)Tools
Q8NTY7-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F5EF6EAFA65924A3

FASTA33736,431
        10         20         30         40         50         60 
MSKSLRVGVV GAGAMGADHI DRINNRTSGA HISAIIEPDA ARAAAAAEDA PGAQAFTRIE 

        70         80         90        100        110        120 
DAIAADAVDA VLIAVPGQFH EPVLVPALEA GLPILCEKPL TPDSESSLRI VELEQKLDKP 

       130        140        150        160        170        180 
HIQVGFMRRF DPEYNNLRKL VESGEAGELL MLRGLHRNPS VGESYTQSML ITDSVVHEFD 

       190        200        210        220        230        240 
VIPWLAGSRV VSVEVKYPKT SSLAHSGLKE PILVIMELEN GVLVDVEMNV NIQFGYQVAT 

       250        260        270        280        290        300 
EAVFEKGLAR IGQPSGMQRW RDGEFLINEH TDFTTRFATA YDRQIQSWVD AVHEGTLVAG 

       310        320        330 
PNAWDGYLVA LSCEAGVKAL DGGVIPVDAA PRPDFYA 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB97557.1.
BX927148 Genomic DNA. Translation: CAF18731.1.
RefSeqNP_599416.1.
YP_224460.1.

3D structure databases

SMRQ8NTY7. Positions 6-328.
ModBaseSearch...

Genome annotation databases

GeneID1021235.
3342797.
GenomeReviewsGene locus Cgl0164 in contig BA000036_GR.
KEGGcgb:cg0204.
cgl:NCgl0161.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG612336.
OMAFGYQVAT.

Enzyme and pathway databases

BioCycCGLU196627:CG0204-MONOMER.

Family and domain databases

HAMAPMF_01671. IolG.
[Tree]
InterProIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLG_CORGL
AccessionPrimary (citable) accession number: Q8NTY7
Secondary accession number(s): Q6M8J3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 1, 2002
Last modified: February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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