P11180 (ODP2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
EC=2.3.1.12

Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2

Gene names

Name:

DLAT

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	10 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 2 lipoyl cofactors covalently By similarity.
Subunit structure	Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 By similarity.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›10	›10	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162297
Amino acid modifications
	Modified residue	5	1	N6-lipoyllysine
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	10	1

Sequences

	Sequence		Length	Mass (Da)
	P11180 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 889BECD1ADD33AB1	FASTA	10	1,066
	10 VETDKATVGF

References

[1]	"Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex." Bradford A.P., Howell S., Aitken A., James L.A., Yeaman S.J. Biochem. J. 245:919-922(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases
IPI	IPI00704214.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00189. LIPOYL. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_BOVIN

Accession

Primary (citable) accession number: P11180

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program