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P10801 (ODP1_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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.
Protein existencePredicted

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. 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 + CO2.

Cofactor

Thiamine pyrophosphate.

Subunit structure

Homodimer.

Ontologies

Keywords
   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12455 Genomic DNA. Translation: CAA30986.1.
PIRS12208.

3D structure databases

ProteinModelPortalP10801.
SMRP10801. Positions 1-42.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
[Graphical view]
SUPFAMSSF52922. SSF52922. 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: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program