[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4781(91)90076-X; PubMed=2025639 [NCBI, ExPASy, EBI, Israel, Japan] Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T.; "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase."; Biochim. Biophys. Acta 1089:1-7(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Liver; PubMed=8158120 [NCBI, ExPASy, EBI, Israel, Japan] Cullingford T.E., Clark J.B., Phillips I.R.; "The pyruvate dehydrogenase complex: cloning of the rat somatic E1 alpha subunit and its coordinate expression with the mRNAs for the E1 beta, E2, and E3 catalytic subunits in developing rat brain."; J. Neurochem. 62:1682-1690(1994).
[3]	PROTEIN SEQUENCE OF 133-141; 216-226; 245-253; 289-302 AND 324-343, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus; Lubec G., Diao W., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295; SER-300 AND TYR-301, AND MASS SPECTROMETRY. TISSUE=Kidney; DOI=10.1073/pnas.0600895103; PubMed=16641100 [NCBI, ExPASy, EBI, Israel, Japan] Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).

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.
TISSUE SPECIFICITY: In all tissues, but in very low amount in testis.

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

Z12158; CAA78146.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15891; DERTPA.
S21553; DERTP1.

UniGene

Rn.3655

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

P26284; 29-390.

PTM databases

P26284; -.

Organism-specific databases

RGD

3286; Pdha1.

Gene expression databases

ArrayExpress

P26284; -.

GermOnline

ENSRNOG00000025383; Rattus norvegicus.

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

P26284.

Genome annotation databases

Ensembl

ENSRNOG00000025383; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P26284; -.

Other

ProtoNet

P26284.

UniRef

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 29`	`29`	`Mitochondrion (By similarity).`
`CHAIN`	`30 390`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial.`	`PRO_0000020445`
`MOD_RES`	`232 232`		`Phosphoserine (By similarity).`
`MOD_RES`	`289 289`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`293 293`		`Phosphoserine.`
`MOD_RES`	`295 295`		`Phosphoserine.`
`MOD_RES`	`300 300`		`Phosphoserine.`
`MOD_RES`	`301 301`		`Phosphotyrosine.`
`CONFLICT`	`10 10`		`R -> H (in Ref. 2; CAA78146).`
`CONFLICT`	`126 126`		`N -> T (in Ref. 2; CAA78146).`
`CONFLICT`	`129 130`		`HA -> LP (in Ref. 2; CAA78146).`
`CONFLICT`	`134 134`		`I -> V (in Ref. 1).`

Sequence information

Length: 390 AA [This is the length of the unprocessed precursor]

Molecular weight: 43227 Da [This is the MW of the unprocessed precursor]

CRC64: 254B5A801E750DC0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKMLAAVSR VLAGAAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFNRGHA VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

P26284 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