[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Desiree; TISSUE=Leaf; DOI=10.1104/pp.108.4.1623; PubMed=7659754 [NCBI, ExPASy, EBI, Israel, Japan] Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J.; "Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis."; Plant Physiol. 108:1623-1629(1995).
[2]	PROTEIN SEQUENCE OF 27-42. STRAIN=cv. Romano; TISSUE=Tuber; PubMed=9729464 [NCBI, ExPASy, EBI, Israel, Japan] Millar A.H., Knorpp C., Leaver C.J., Hill S.A.; "Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato."; Biochem. J. 334:571-576(1998).

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 (By similarity).
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

Z26949; CAA81558.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T07372; T07372.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

ModBase

P52903.

Protein-protein interaction databases

IntAct

P52903; -.

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).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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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.

Other

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

Keywords

Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 26`	`26`	`Mitochondrion.`
`CHAIN`	`27 391`	`365`	`Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial.`	`PRO_0000020455`

Sequence information

Length: 391 AA [This is the length of the unprocessed precursor]

Molecular weight: 43228 Da [This is the MW of the unprocessed precursor]

CRC64: F9110B374B022F0D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP SRSVETSPKE 

        70         80         90        100        110        120 
LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV AVGMEAAITK KDCIITAYRD 

       130        140        150        160        170        180 
HCIFLGRGGT LVEAFAELMG RRDGCSRGKG GSMHFYKKES GFYGGHGIVG AQVPLGIGLA 

       190        200        210        220        230        240 
FAQKYKKEDY VTFAMYGDGA ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK 

       250        260        270        280        290        300 
SPAYYKRGDY VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS 

       310        320        330        340        350        360 
TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA IAKAKESPMP 

       370        380        390 
DPSELFTNVY VKGFGVEAYG ADRKELRATL P

P52903 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