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Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex



Bos taurus (Bovine)
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli


The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.


(R)-lipoateBy similarityNote: Binds 2 lipoyl cofactors covalently.By similarity

GO - Molecular functioni

GO - Biological processi


Molecular functionAcyltransferase, Transferase
Biological processCarbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Gene namesi
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000162297‹1 – ›10Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex›10

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6-lipoyllysine1 Publication1

Post-translational modificationi

Delipoylated at Lys-5 by SIRT4, delipoylation decreases the PHD complex activity.By similarity


Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (By similarity). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (PubMed:20361979). Interacts with PDK2 and PDK3 (By similarity). Interacts with SIRT4 (By similarity). Interacts with PDHB (By similarity).By similarity1 Publication

Protein-protein interaction databases


Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat


Sequence statusi: Fragment.

Mass (Da):1,066
Last modified:July 1, 1989 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei101

Sequence databases


Entry informationi

Entry nameiODP2_BOVIN
AccessioniPrimary (citable) accession number: P11180
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 27, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program


Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome