Pyruvate dehydrogenase E1 component - Escherichia coli (strain K12)

Contribute

Reviewed, UniProtKB/Swiss-Prot P0AFG8 (ODP1_ECOLI)

Last modified November 25, 2008. Version 41. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component
EC=1.2.4.1

Gene names

Name:	aceE
Ordered Locus Names:	b0114, JW0110

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
Cofactor	Magnesium. Thiamine pyrophosphate.
Subunit structure	Homodimer.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Magnesium Metal-binding Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB mitochondrion Inferred from direct assay. Source: UniProtKB
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fryA	P77439	1	EBI-542683,EBI-545399
ftsK	P46889	1	EBI-542683,EBI-550795
groL	P0A6F5	1	EBI-542683,EBI-543750
hycI	P0AEV9	1	EBI-542683,EBI-552628
nth	P0AB83	1	EBI-542683,EBI-555213
poxA	P0A8N7	1	EBI-542683,EBI-562598
purB	P0AB89	1	EBI-542683,EBI-556534
ribF	P0AG40	1	EBI-542683,EBI-542969
tag	P05100	1	EBI-542683,EBI-558722
ubiC	P26602	1	EBI-542683,EBI-559360
ybhF	P0A9U1	1	EBI-542683,EBI-547696
yciU	P0A8L7	1	EBI-542683,EBI-544511
ycjY	P76049	1	EBI-542683,EBI-544654
ynfB	P76170	1	EBI-542683,EBI-544774

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

886

Pyruvate dehydrogenase E1 component

PRO_0000162243

Sites

Metal binding

1

Magnesium

Metal binding

1

Magnesium

Metal binding

1

Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue

1

N6-acetyllysine

Experimental info

Sequence conflict

1

P → R Ref.1 Ref.2

Sequence conflict

1

Missing Ref.1 Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

887

Helix Strand Turn