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Reviewed, UniProtKB/Swiss-Prot P0AFG8 (ODP1_ECOLI)

Last modified November 25, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1
Gene names
Name: aceE
Ordered Locus Names: b0114, JW0110
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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

Magnesium.

Thiamine pyrophosphate.

Subunit structure

Homodimer.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 887886Pyruvate dehydrogenase E1 component
PRO_0000162243

Sites

Metal binding2311Magnesium
Metal binding2611Magnesium
Metal binding2631Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue7161N6-acetyllysine

Experimental info

Sequence conflict1461P → R Ref.1 Ref.2
Sequence conflict2761Missing Ref.1 Ref.2

Secondary structure

............................................................................................................................................ 887
Helix Strand Turn

Details...