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InterPro: IPR017597 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y

Protein matchesHelp
UniProtKB
Matches:
586 proteins
AccessionHelp IPR017597 Pyrv_DH_E1_asu_subgrp-y
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001017 Dehydrogenase, E1 component
GO Term annotationHelp
Process GO:0006096 glycolysis
GO:0055114 oxidation reduction
Function GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
Component GO:0043231 intracellular membrane-bounded organelle
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH) [1]. This entry represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. The pyruvate dehydrogenase complex catalyses the overall conversion of pyruvate to acetyl-CoA and carbon dioxide. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Structural linksHelp
SCOP: c.36.1.11
CATH: 3.40.50.970
Database linksHelp
Enzyme: EC:1.2.4.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017597 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P08559 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

P16387 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

P35486 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

P52899 Probable pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

P52901 Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017597 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y
IPR001017 Dehydrogenase, E1 component
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Korotchkina LG, Ciszak EM, Patel MS.
Function of several critical amino acids in human pyruvate dehydrogenase revealed by its structure.
Arch. Biochem. Biophys. 429 171-9 2004 [PubMed: 15313220]
http://dx.doi.org/10.1016/j.abb.2004.06.027

Additional ReadingHelp
Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS.
Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase.
J. Biol. Chem. 278 2003 21240-6 [PubMed: 12651851]
http://dx.doi.org/10.1074/jbc.M300339200
Seifert F, Ciszak E, Korotchkina L, Golbik R, Spinka M, Dominiak P, Sidhu S, Brauer J, Patel MS, Tittmann K.
Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex.
Biochemistry 46 2007 6277-87 [PubMed: 17474719]
http://dx.doi.org/10.1021/bi700083z
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InterPro 23.1