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InterPro: IPR004167 E3 binding

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3599 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
Matches in BioMart

Accession

IPR004167 E3_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:4.10.320.10	E3_bd	3025
Pfam	PF02817	E3_binding	3596
SuperFamily	SSF47005	E3_bd	3473
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:0005515 protein binding
GO:0008415 acyltransferase activity

InterPro annotation

Entry Details in BioMart

Abstract

A small domain of the E2 subunit of 2-oxo-acid dehydrogenases that is responsible for the binding of the E3 subunit. Proteins containing this domain include the branched-chain alpha-keto acid dehydrogenase complex of bacteria, which catalyses the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide; and the E-3 binding protein of eukaryotic pyruvate dehydrogenase.

Structural links Help

PDB - click here

SCOP: a.9.1.1

CATH: 4.10.320.10

Database links Help

Enzyme: EC:2.3.1

PANDIT: PF02817

Blocks: IPB004167

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004167

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 Help

Additional Reading Open in usermanual
	Frank RA, Titman CM, Pratap JV, Luisi BF, Perham RN. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science 306 2004 872-6 [PubMed: 15514159] http://dx.doi.org/10.1126/science.1101030
	Sadqi M, Fushman D, Munoz V. Atom-by-atom analysis of global downhill protein folding. Nature 442 2006 317-21 [PubMed: 16799571] http://dx.doi.org/10.1038/nature04859
	Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J. Biol. Chem. 281 2006 648-55 [PubMed: 16263718] http://dx.doi.org/10.1074/jbc.M507850200
	Allen MD, Broadhurst RW, Solomon RG, Perham RN. Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy. FEBS J. 272 2005 259-68 [PubMed: 15634348] http://dx.doi.org/10.1111/j.1432-1033.2004.04405.x
	Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR. Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. J. Mol. Biol. 353 2005 427-46 [PubMed: 16168437] http://dx.doi.org/10.1016/j.jmb.2005.08.031
	Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Structure 4 1996 277-86 [PubMed: 8805537] http://dx.doi.org/10.1016/S0969-2126(96)00032-9

InterPro 23.1