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InterPro: IPR004660 2-oxo-acid dehydrogenase E1 component homodimeric type

Protein matches Help

UniProtKB

Matches:

736 proteins

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

Accession

IPR004660 2-oxoA_DH_E1

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000156	Pyruvate_dh_E1	726
TIGRFAMs	TIGR00759	aceE	723
Signatures in BioMart

InterPro Relationships Help

Children

IPR017600 Alpha-ketoglutarate dehydrogenase

Contains

IPR015941 Transketolase-like, C-terminal

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Most members of this family are pyruvate dehydrogenase complex, E1 component. It includes a counterexample from Pseudomonas putida, MdeB, that is active as an E1 component of an alpha-ketoglutarate dehydrogenase complex rather than a pyruvate dehydrogenase complex. The second pyruvate dehydrogenase complex E1 protein from Ralstonia eutropha (Alcaligenes eutrophus), PdhE, complements an aceE mutant of Escherichia coli but is not part of a pyruvate dehydrogenase complex operon, is more similar to the Pseudomonas putida MdeB than to E. coli AceE, and may have also have a different primary specificity.

Structural links Help

PDB - click here

SCOP: c.36.1.10 , c.36.1.6 , c.48.1.1

CATH: 3.40.50.920

Database links Help

Enzyme: EC:1.2.4.1

CluSTr: ALLvsALL:14654:40.4

COMe: PRX001034

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004660

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0AFG8 Pyruvate dehydrogenase E1 component

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005474	Transketolase, N-terminal
IPR004660	2-oxo-acid dehydrogenase E1 component homodimeric type
IPR009014	Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain II
IPR015941	Transketolase-like, C-terminal
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Inoue H, Inagaki K, Eriguchi SI, Tamura T, Esaki N, Soda K, Tanaka H. Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida. J. Bacteriol. 179 1997 3956-62 [PubMed: 9190812] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=9190812
	Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry 41 2002 5213-21 [PubMed: 11955070] http://dx.doi.org/10.1021/bi0118557
	Kale S, Arjunan P, Furey W, Jordan F. A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J. Biol. Chem. 282 2007 28106-16 [PubMed: 17635929] http://dx.doi.org/10.1074/jbc.M704326200
	Chandrasekhar K, Arjunan P, Sax M, Nemeria N, Jordan F, Furey W. Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution. Acta Crystallogr. D Biol. Crystallogr. 62 2006 1382-6 [PubMed: 17057342] http://dx.doi.org/10.1107/S0907444906034408
	Arjunan P, Chandrasekhar K, Sax M, Brunskill A, Nemeria N, Jordan F, Furey W. Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Biochemistry 43 2004 2405-11 [PubMed: 14992577] http://dx.doi.org/10.1021/bi030200y
	Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. J. Biol. Chem. 281 2006 15296-303 [PubMed: 16531404] http://dx.doi.org/10.1074/jbc.M600656200

InterPro 23.1