[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Testis; DOI=10.1016/0167-4781(93)90054-H; PubMed=7916643 [NCBI, ExPASy, EBI, Israel, Japan] Cullingford T.E., Clark J.B., Phillips I.R.; "Characterization of cDNAs encoding the rat testis-specific E1 alpha subunit of the pyruvate dehydrogenase complex: comparison of expression of the corresponding mRNA with that of the somatic E1 alpha subunit."; Biochim. Biophys. Acta 1216:149-153(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; DOI=10.1016/S0305-0491(98)10010-X; PubMed=9787790 [NCBI, ExPASy, EBI, Israel, Japan] Jeng J., Kallarakal A.T., Kim S.F., Popov K.M., Song B.J.; "Pyruvate dehydrogenase E1 alpha isoform in rat testis: cDNA cloning, characterization, and biochemical comparison of the recombinant testis and liver enzymes."; Comp. Biochem. Physiol. 120B:205-216(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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 (Probable).
TISSUE SPECIFICITY: 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

Z18878; CAA79318.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U44125; AAB68458.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC078757; AAH78757.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S31416; S31416.

NP_446446.1; -.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

SMR

Q06437; 31-391.

ModBase

Q06437.

Organism-specific databases

RGD

620095; Pdha2.

Gene expression databases

ArrayExpress

Q06437; -.

GermOnline

ENSRNOG00000016223; Rattus norvegicus.

Ontologies

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

Q06437.

Genome annotation databases

Ensembl

ENSRNOG00000016223; Rattus norvegicus. [Contig view]

GeneID

117098; -.

KEGG

rno:117098; -.

NMPDR

fig|10116.3.peg.17098; -.

Phylogenomic databases

HOVERGEN

Q06437; -.

Other

ProtoNet

Q06437.

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 30`	`30`	`Mitochondrion (By similarity).`
`CHAIN`	`31 391`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial.`	`PRO_0000020449`
`MOD_RES`	`294 294`		`Phosphoserine (By similarity).`
`MOD_RES`	`301 301`		`Phosphoserine (By similarity).`

Sequence information

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

Molecular weight: 43393 Da [This is the MW of the unprocessed precursor]

CRC64: 5BF049BEE483EF5D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKMLATVLS QVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYLLEQG PPTSTVLTRE 

        70         80         90        100        110        120 
EALKYYRNMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CNVGLEAGIN PTDHIITSYR 

       130        140        150        160        170        180 
AHGLCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYAKN FYGGNGIVGA QVPLGAGVAL 

       190        200        210        220        230        240 
ACKYLKNGQI CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNRYGM GTAIERSAAS 

       250        260        270        280        290        300 
TDYHKKGFVI PGLRVNGMDI LSVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI 

       310        320        330        340        350        360 
SYRTREEVQN VRSKSDPIML LRERMISNNL SSVEELKEID ADVKKEVEEA AQFATTDPEP 

       370        380        390 
PLEDLANYLY HQNPPFEVRG AHKWLKFKSV S

Q06437 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