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Reviewed, UniProtKB/Swiss-Prot P10801 (ODP1_AZOVI)

Last modified November 4, 2008. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | 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

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length45 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existencePredicted.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).

Cofactor

Thiamine pyrophosphate.

Subunit structure

Homodimer.

Ontologies

Keywords

   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 45›45Pyruvate dehydrogenase E1 component
PRO_0000162239

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P10801-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: C2929BB637D1B032

FASTA454,957
        10         20         30         40 
EVDRYWVVLA ALEALADRGD IEAKVVAEAI AKFGIDPDKR NPLDC 

« Hide

References

[1]"The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis."
Hanemaaijer R., Janssen A., de Kok A., Veeger C.
Eur. J. Biochem. 174:593-599(1988) [PubMed: 3292237] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.

Cross-references

Sequence databases

X12455 Genomic DNA. Translation: CAA30986.1.
PIRS12208.

3D structure databases

HSSPHSSP built from PDB template 1L8A based on UniProtKB P06958.
ModBaseSearch...

Family and domain databases

InterProIPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODP1_AZOVI
AccessionPrimary (citable) accession number: P10801
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 4, 2008
This is version 43 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)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information