[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Muscle; DOI=10.1093/nar/18.16.4925; PubMed=2395657 [NCBI, ExPASy, EBI, Israel, Japan] Sermon K., Demeirleir L., Elpers I., Lissens W., Liebaers I.; "Characterisation of a cDNA for porcine PDH-E1 alpha and comparison with the human cDNA."; Nucleic Acids Res. 18:4925-4925(1990).
[2]	PHOSPHORYLATION AT SER-231; SER-292 AND SER-299. PubMed=227365 [NCBI, ExPASy, EBI, Israel, Japan] Kerbey A.L., Radcliffe P.M., Randle P.J., Sugden P.H.; "Regulation of kinase reactions in pig heart pyruvate dehydrogenase complex."; Biochem. J. 181:427-433(1979).

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 + CO₂.
COFACTOR: Thiamine pyrophosphate.
ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
SUBCELLULAR LOCATION: Mitochondrion matrix.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X52990; CAA37180.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S20813; DEPGPA.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

SMR

P29804; 28-389.

ModBase

P29804.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

BLOCKS

P29804.

Phylogenomic databases

HOVERGEN

P29804; -.

Other

ProtoNet

P29804.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 28`	`>28`	`Mitochondrion (By similarity).`
`CHAIN`	`29 389`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial.`	`PRO_0000020443`
`MOD_RES`	`231 231`		`Phosphoserine.`
`MOD_RES`	`288 288`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`292 292`		`Phosphoserine.`
`MOD_RES`	`294 294`		`Phosphoserine (By similarity).`
`MOD_RES`	`299 299`		`Phosphoserine.`
`MOD_RES`	`300 300`		`Phosphotyrosine (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 389 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 43121 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E9C7DF85389A9A47 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GKMLAAVSRV LSGVAQKPAS RVLVASRTFA NDATFEIKKC DLHRLEEGPP VTTVLTREDG 

        70         80         90        100        110        120 
LKYYRMMQTV RRMELKADQL YKQKIIRGFC HLCDGQEACC VGLEAGINPT DHLITAYRAH 

       130        140        150        160        170        180 
GFTFTRGLSV REILAELTGR RGGCGKGKGG SMHMYAKNFY GGNGIVGAQV PLGAGIALAC 

       190        200        210        220        230        240 
KYNGKDEVCL TLYGDGAANQ GQIFEAYNMA ALWKLPCVFI CENNRYGMGT SVERAAASTD 

       250        260        270        280        290        300 
YYKRGDFIPG LRVDGMDILC VREATRFAAA YCRSGKGPIL MELQTYRYHG HSMSDPGVSY 

       310        320        330        340        350        360 
RTREEIQEVR SKSDPIMLLK DRMVNSNLAS VEELKEIDVE VRKEIEDAAQ FATADPEPPL 

       370        380 
EELGYHIYCN DPPFEVRGAN QWIKFKSIS

P29804 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools