NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/j.gene.2007.04.013; PubMed=17574350 [NCBI, ExPASy, EBI, Israel, Japan]
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome.";
Gene 399:1-10(2007).

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) (By similarity).
CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
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 (By similarity).

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

AB222138; BAF62383.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001104283.1; -.

3D structure databases

ModBase

A5A6L0.

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).
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.

Genome annotation databases

Ensembl

ENSPTRG00000021717; Pan troglodytes. [Contig view]

GeneID

465525; -.

Other

ProtoNet

A5A6L0.

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 29`	`29`	`Mitochondrion (By similarity).`
`CHAIN`	`30 390`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial.`	`PRO_0000297491`
`MOD_RES`	`232 232`		`Phosphoserine (By similarity).`
`MOD_RES`	`289 289`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`293 293`		`Phosphoserine (By similarity).`
`MOD_RES`	`295 295`		`Phosphoserine (By similarity).`
`MOD_RES`	`300 300`		`Phosphoserine (By similarity).`
`MOD_RES`	`301 301`		`Phosphotyrosine (By similarity).`

Sequence information

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

Molecular weight: 43238 Da [This is the MW of the unprocessed precursor]

CRC64: 4F95746CBB792E78 [This is a checksum on the sequence]

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

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

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

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

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS 

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

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

A5A6L0 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