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InterPro: IPR001078 2-oxoacid dehydrogenase acyltransferase, catalytic domain

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Matches:

4007 proteins

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Accession

IPR001078 2-oxoacid_DH_actylTfrase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00198	2-oxoacid_dh	4007
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006255 Dihydrolipoamide succinyltransferase
IPR006256 Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex
IPR006257 Dihydrolipoamide acetyltransferase, long form
IPR014276 2-oxoglutarate dehydrogenase, E2 component
IPR015761 Lipoamide Acyltransferase

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0008415 acyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in the lipoamide acyltransferase component of the branched-chain alpha-keto acid dehydrogenase complex EC:2.3.1, which catalyses the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide [1]. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The domain is also found in the dihydrolipoamide succinyltransferase component of the 2-oxoglutarate dehydrogenase complex EC:2.3.1.61. These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.

Structural links Help

PDB - click here

SCOP: c.43.1.1

CATH: 3.30.559.10

Database links Help

Enzyme: EC:2.3.1

PANDIT: PF00198

Blocks: IPB001078

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001078

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00330 Pyruvate dehydrogenase protein X component, mitochondrial

P12695 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

P53395 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Q0WQF7 Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial

Q19749 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006257	Dihydrolipoamide acetyltransferase, long form
IPR001078	2-oxoacid dehydrogenase acyltransferase, catalytic domain
IPR004167	E3 binding
IPR011053	Single hybrid motif
IPR003016	2-oxo acid dehydrogenase, lipoyl-binding site
IPR000089	Biotin/lipoyl attachment
IPR015761	Lipoamide Acyltransferase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Mattevi A, Obmolova G, Kalk KH, Westphal AH, de Kok A, Hol WG. Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 A resolution. J. Mol. Biol. 230 1183-99 1993 [PubMed: 8487300] http://dx.doi.org/10.1006/jmbi.1993.1235

Additional Reading Open in usermanual
	Mattevi A, Obmolova G, Kalk KH, Teplyakov A, Hol WG. Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p). Biochemistry 32 1993 3887-901 [PubMed: 8471601] http://dx.doi.org/10.1021/bi00066a007
	Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML. Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase. Protein Sci. 9 2000 37-48 [PubMed: 10739245] http://www.proteinscience.org/cgi/content/abstract/9/1/37
	Hendle J, Mattevi A, Westphal AH, Spee J, de Kok A, Teplyakov A, Hol WG. Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). Biochemistry 34 1995 4287-98 [PubMed: 7703242] http://dx.doi.org/10.1021/bi00013a018
	Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 1998 655-68 [PubMed: 9677295] http://dx.doi.org/10.1006/jmbi.1998.1924
	Izard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc. Natl. Acad. Sci. U.S.A. 96 1999 1240-5 [PubMed: 9990008] http://dx.doi.org/10.1073/pnas.96.4.1240

InterPro 23.1