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InterPro: IPR018955 Branched-chain alpha-ketoacid dehydrogenase kinase/Pyruvate dehydrogenase kinase, mitochondrial

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380 proteins

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Accession

IPR018955 BCDHK/PDK_mit

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF10436	BCDHK_Adom3	380
Signatures in BioMart

InterPro annotation

Entry Details in BioMart

Abstract

Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. Regulating the activity of the branched-chain alpha-ketoacid dehydrogenase (BCDH) complex is the primary means by which these processes are coordinated. BCDH kinase regulates BCDH by phosphorylation, thereby inactivating it when synthesis is required.

Pyruvate dehydrogenase kinase inhibits the pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism. It is also involved in telomere maintenance.

This entry is associated with IPR003594 which is found towards the C terminus.

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SCOP: a.29.5.1 , d.122.1.4

CATH: 1.20.140.20 , 3.30.565.10

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Enzyme: EC:2.7.11

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Example proteins Help

O55028 [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial

P40530 [Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial

P91622 [Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial

Q02332 Probable [pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial

Q15118 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005467	Signal transduction histidine kinase, core
IPR003594	ATPase-like, ATP-binding domain
IPR018955	Branched-chain alpha-ketoacid dehydrogenase kinase/Pyruvate dehydrogenase kinase, mitochondrial
IPR004358	Signal transduction histidine kinase-related protein, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Popov KM, Zhao Y, Shimomura Y, Kuntz MJ, Harris RA. Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. J. Biol. Chem. 267 1992 13127-30 [PubMed: 1377677]
	Devedjiev Y, Steussy CN, Vassylyev DG. Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications. J. Mol. Biol. 370 2007 407-16 [PubMed: 17532006] http://dx.doi.org/10.1016/j.jmb.2007.04.083
	Knoechel TR, Tucker AD, Robinson CM, Phillips C, Taylor W, Bungay PJ, Kasten SA, Roche TE, Brown DG. Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands. Biochemistry 45 2006 402-15 [PubMed: 16401071] http://dx.doi.org/10.1021/bi051402s
	Kato M, Li J, Chuang JL, Chuang DT. Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol. Structure 15 2007 992-1004 [PubMed: 17683942] http://dx.doi.org/10.1016/j.str.2007.07.001
	Green T, Grigorian A, Klyuyeva A, Tuganova A, Luo M, Popov KM. Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2. J. Biol. Chem. 283 2008 15789-98 [PubMed: 18387944] http://dx.doi.org/10.1074/jbc.M800311200
	Kato M, Chuang JL, Tso SC, Wynn RM, Chuang DT. Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 24 2005 1763-74 [PubMed: 15861126] http://dx.doi.org/10.1038/sj.emboj.7600663

InterPro 23.1