NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

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).
SUBUNIT: Heterodimer of an alpha and a beta chain.

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

BA000033; BAB94841.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645793.1; -.

3D structure databases

SMR

P60090; 8-370.

ModBase

P60090.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0976-MON; -.

Ontologies

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.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

ProtoNet

P60090.

Genome annotation databases

GeneID

1003088; -.

GenomeReviews

BA000033_GR; MW0976.

KEGG

sam:MW0976; -.

Phylogenomic databases

HOGENOM

P60090; -.

Genome annotation databases

CMR

P60090; MW0976.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 370`	`370`		`Pyruvate dehydrogenase E1 component subunit alpha.`	`PRO_0000162210`

Sequence information

Length: 370 AA [This is the length of the unprocessed precursor]

Molecular weight: 41383 Da [This is the MW of the unprocessed precursor]

CRC64: 66BD3BF8A0C9565F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPKLQAQFD AVKVLNDTQS KFEMVQILDE NGNVVNEDLV PDLTDEQLVE LMERMVWTRI 

        70         80         90        100        110        120 
LDQRSISLNR QGRLGFYAPT AGQEASQLAS QYALEKEDYI LPGYRDVPQI IWHGLPLTEA 

       130        140        150        160        170        180 
FLFSRGHFKG NQFPEGVNAL SPQIIIGAQY IQAAGVAFAL KKRGKNAVAI TYTGDGGSSQ 

       190        200        210        220        230        240 
GDFYEGINFA AAYKAPAIFV IQNNNYAIST PRSKQTAAET LAQKAIAVGI PGIQVDGMDA 

       250        260        270        280        290        300 
LAVYQATKEA RDRAVAGEGP TLIETMTYRY GPHTMAGDDP TRYRTSDEDA EWEKKDPLVR 

       310        320        330        340        350        360 
FRKFLENKGL WNEDKENEVI ERAKADIKAA IKEADNTEKQ TVTSLMEIMY EDMPQNLAEQ 

       370 
YEIYKEKESK

P60090 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