Reviewed, UniProtKB/Swiss-Prot P11180 (ODP2_BOVIN)

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)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
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	Forms a 24-polypeptide structural core with octahedral symmetry.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Lipoyl Repeat
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis 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 lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW
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)
	P11180-1 [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: 3117054] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases
IPI	IPI00704214.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P11180.
Enzyme and pathway databases
BRENDA	2.3.1.12. 251.
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:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)