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InterPro: IPR017596 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit subgroup x

Protein matchesHelp
UniProtKB
Matches:
479 proteins
AccessionHelp IPR017596 Pyrv_DH_E1_asu_subgrp-x
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
GO:0030976 thiamin pyrophosphate binding
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. PDH is a heterodimer of an alpha and a beta subunit. 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). The Bacillus subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.

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
IPR017596 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P21873 Pyruvate dehydrogenase E1 component subunit alpha

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017596 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit subgroup x
IPR001017 Dehydrogenase, E1 component
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
1. Hawkins CF, Borges A, Perham RN.
Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
Eur. J. Biochem. 191 337-46 1990 [PubMed: 2200674]
http://dx.doi.org/10.1111/j.1432-1033.1990.tb19128.x

Additional ReadingHelp
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
Lessard IA, Perham RN.
Expression in Escherichia coli of genes encoding the E1 alpha and E1 beta subunits of the pyruvate dehydrogenase complex of Bacillus stearothermophilus and assembly of a functional E1 component (alpha 2 beta 2) in vitro.
J. Biol. Chem. 269 1994 10378-83 [PubMed: 8144620]
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InterPro 23.1