NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1016/S0888-7543(05)80366-0; PubMed=8307573 [NCBI, ExPASy, EBI, Israel, Japan]
Fitzgerald J., Wilcox S.A., Graves J.A., Dahl H.H.M.;
"A eutherian X-linked gene, PDHA1, is autosomal in marsupials: a model for the evolution of a second, testis-specific variant in eutherian mammals.";
Genomics 18:636-642(1993).

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 (By similarity).
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

L20774; AAA31589.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

SMR

P52900; 2-363.

ModBase

P52900.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
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

P52900.

Phylogenomic databases

HOVERGEN

P52900; -.

Other

ProtoNet

P52900.

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 2`	`>2`	`Mitochondrion (By similarity).`
`CHAIN`	`3 363`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial.`	`PRO_0000020446`
`MOD_RES`	`205 205`		`Phosphoserine (By similarity).`
`MOD_RES`	`262 262`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`266 266`		`Phosphoserine (By similarity).`
`MOD_RES`	`268 268`		`Phosphoserine (By similarity).`
`MOD_RES`	`273 273`		`Phosphoserine (By similarity).`
`MOD_RES`	`274 274`		`Phosphotyrosine (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 363 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 40735 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 4884E0A17D7A15A8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
RNFANDATFD IKKCDVHRLE EGPPTTAVLT REEGLKYYKI MQTVRRMELK ADQLYKQKII 

        70         80         90        100        110        120 
RGFCHLYDGQ EACCMGLEAG INPTDHVITA YRAHGFTYTR GLPVREILAE LTGRRGGCAK 

       130        140        150        160        170        180 
GKGGSMHMYA KNFYGGNGIV GAQVPLGVGI ALACKYNEKD EICLTLYGDG AANQGQIFEA 

       190        200        210        220        230        240 
YNMAALWKLP CIFICENNRY GMGTSVERAA ASTDYYKRGD FIPGIMVDGM DVLCVREATK 

       250        260        270        280        290        300 
FAAAYCRSGK GPMLMELQTY RYHGHSMSDP GVSYRTREEI QEVRSKSDPI MLLKDRMVNN 

       310        320        330        340        350        360 
NLASIEELKE IDVEVRKEIE DAAQFATADP EPPLEELGYH IYSRDPPFEV RGANQWIKYK 


SVS

P52900 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