[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0166-6851(92)90198-S; PubMed=1565136 [NCBI, ExPASy, EBI, Israel, Japan] Johnson K.R., Komuniecki R., Sun Y., Wheelock M.J.; "Characterization of cDNA clones for the alpha subunit of pyruvate dehydrogenase from Ascaris suum."; Mol. Biochem. Parasitol. 51:37-48(1992).
[2]	PROTEIN SEQUENCE OF 285-298, AND PHOSPHORYLATION AT SER-289 AND SER-296. PubMed=3198613 [NCBI, ExPASy, EBI, Israel, Japan] Thissen J., Komuniecki R.; "Phosphorylation and inactivation of the pyruvate dehydrogenase from the anaerobic parasitic nematode, Ascaris suum. Stoichiometry and amino acid sequence around the phosphorylation sites."; J. Biol. Chem. 263:19092-19097(1988).

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

M76555; AAA29376.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31963; A31963.
A45608; A45608.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

ModBase

P26267.

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 25`	`25`	`Mitochondrion.`
`CHAIN`	`26 396`	`371`	`Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial.`	`PRO_0000020437`
`MOD_RES`	`289 289`		`Phosphoserine.`
`MOD_RES`	`296 296`		`Phosphoserine.`

Sequence information

Length: 396 AA [This is the length of the unprocessed precursor]

Molecular weight: 43771 Da [This is the MW of the unprocessed precursor]

CRC64: 60A810BB5B48B836 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIFVFANIFK VPTVSPSVMA ISVRLASTEA TFQTKPFKLH KLDSGPDINV HVTKEDAVHY 

        70         80         90        100        110        120 
YTQMLTIRRM ESAAGNLYKE KKVRGFCHLY SGQEACAVGT KAAMDAGDAA VTAYRCHGWT 

       130        140        150        160        170        180 
YLSGSSVAKV LCELTGRITG NVYGKGGSMH MYGENFYGGN GIVGAQQPLG TGIAFAMKYR 

       190        200        210        220        230        240 
KEKNVCITMF GDGATNQGQL FESMNMAKLW DLPVLYVCEN NGYGMGTAAA RSSASTDYYT 

       250        260        270        280        290        300 
RGDYVPGIWV DGMDVLAVRQ AVRWAKEWCN AGKGPLMIEM ATYRYSGHSM SDPGTSYRTR 

       310        320        330        340        350        360 
EEVQEVRKTR DPITGFKDKI VTAGLVTEDE IKEIDKQVRK EIDAAVKQAH TDKESPVELM 

       370        380        390 
LTDIYYNTPA QYVRCTTDEV LQKYLTSEEA VKALAK

P26267 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