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

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Cross-references

Sequence databases

EMBL

U51918; AAA97411.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T06531; T06531.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

ModBase

P52902.

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.

Other

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 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 397`		`Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial.`	`PRO_0000020454`

Sequence information

Length: 397 AA [This is the length of the unprocessed precursor]

Molecular weight: 43530 Da [This is the MW of the unprocessed precursor]

CRC64: 3C0257CB0032E50B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSRLSSSS SSSNGSNLFN PFSAAFTLNR PISSDTTATL TIETSLPFTA HNCDPPSRSV 

        70         80         90        100        110        120 
TTSPSELLSF FRTMALMRRM EIAADSLYKA NLIRGFCHLY DGQEAVAVGM EAGTTKKDCI 

       130        140        150        160        170        180 
ITAYRDHCTF LGRGGTLLRV YAELMGRRDG CSKGKGGSMH FYKKDSGFYG GHGIVGAQVP 

       190        200        210        220        230        240 
LGCGLAFGQK YLKDESVTFA LYGDGAANQG QLFEALNISA LWDLPAILVC ENNHYGMGTA 

       250        260        270        280        290        300 
TWRSAKSPAY FKRGDYVPGL KVDGMDALAV KQACKFAKEH ALKNGPIILE MDTYRYHGHS 

       310        320        330        340        350        360 
MSDPGSTYRT RDEISGVRQE RDPIERVRKL LLSHDIATEK ELKDTEKEVR KEVDEAIAKA 

       370        380        390 
KDSPMPDPSD LFSNVYVKGY GVEAFGVDRK EVRVTLP

P52902 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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