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Reviewed, UniProtKB/Swiss-Prot A9H5B7 (IOLG_GLUDA)

Last modified January 19, 2010. Version 21. 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: GDI0366, Gdia_2417
OrganismGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]
Taxonomic identifier272568 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

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_0000352569

Experimental info

Sequence conflict2701N → K in ACI52167. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A9H5B7-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: B9104F42F458C6AC

FASTA33737,032
        10         20         30         40         50         60 
MTLGIGVIGT GAIGQDHIRR VSRALSGGRI VALNDINADN ARRAAQEWAP DAVICDTARD 

        70         80         90        100        110        120 
LVARPDVQAV MVTSWGGTHA EYVLDAIAAG KPVFCEKPLA TNAADCLRIM EAEMARGRRL 

       130        140        150        160        170        180 
VQVGFNRRYD SGYLDLKAIL DNGTIGDVLM VHAMHRNQRV GPNYKTEMAI TDTLVHELDV 

       190        200        210        220        230        240 
HRWLLDGEYV SAQVIFPRRT SKALPHMRDP QIALLETKRG IRIDVEIFVN CQYGYDIQCA 

       250        260        270        280        290        300 
VVGELGQANL PDPPAVPVKT GETLSRHIMN DWKYRFIDAY DAEIQDFIDR ASTGSPAGPD 

       310        320        330 
SWAGYAASVA ADACVRAQES GRIEPIEMIA KPAFYSR 

« Hide

References

[1]"Gluconacetobacter diazotrophicus Pal5 complete genome."
Bertalan M., Baldani I.J., Ferreira P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete sequence of chromosome of Gluconacetobacter diazotrophicus PAl 5."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Triplett E.W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM889285 Genomic DNA. Translation: CAP54309.1.
CP001189 Genomic DNA. Translation: ACI52167.1.
RefSeqYP_001600653.1.
YP_002276782.1.

3D structure databases

SMRA9H5B7. Positions 2-327.
ModBaseSearch...

Genome annotation databases

GeneID5789781.
6975847.
GenomeReviewsGene locus GDI0366 in contig AM889285_GR.
Gene locus Gdia_2417 in contig CP001189_GR.
KEGGgdj:Gdia_2417.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG612336.
OMADWKDRFI.

Family and domain databases

HAMAPMF_01671. IolG.
[Tree]
InterProIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLG_GLUDA
AccessionPrimary (citable) accession number: A9H5B7
Secondary accession number(s): B5ZFL5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: February 5, 2008
Last modified: January 19, 2010
This is version 21 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