[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 [LARGE SCALE MRNA]. TISSUE=Kidney; 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).
[3]	PROTEIN SEQUENCE OF 31-38. TISSUE=Heart; Dunn M.J.; Submitted (MAR-1996) to UniProtKB.
[4]	PROTEIN SEQUENCE OF 286-324, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Diao W.; Submitted (APR-2007) to UniProtKB.

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.
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

BC079137; AAH79137.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S15892; S15892.

NP_001007621.1; -.

3D structure databases

HSSP

P11177; 1NI4. [HSSP ENTRY / PDB]

SMR

P49432; 30-359.

ModBase

P49432.

Protein-protein interaction databases

IntAct

P49432; -.

2D gel databases

HSC-2DPAGE

P49432; -.

Organism-specific databases

RGD

1359146; Pdhb.

Gene expression databases

ArrayExpress

P49432; -.

GermOnline

ENSRNOG00000007895; Rattus norvegicus.

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).
QuickGo view.

Family and domain databases

InterPro

IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.920; Transketo_C_like; 1.

Pfam

PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.

BLOCKS

P49432.

Genome annotation databases

Ensembl

ENSRNOG00000007895; Rattus norvegicus. [Contig view]

GeneID

289950; -.

KEGG

rno:289950; -.

NMPDR

fig|10116.3.peg.11094; -.

Phylogenomic databases

HOVERGEN

P49432; -.

Other

ProtoNet

P49432.

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 30`	`30`	`Mitochondrion.`
`CHAIN`	`31 359`	`329`	`Pyruvate dehydrogenase E1 component subunit beta, mitochondrial.`	`PRO_0000020459`
`BINDING`	`89 89`		`Thiamine pyrophosphate (By similarity).`
`MOD_RES`	`67 67`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`3 3`		`A -> G (in Ref. 1).`
`CONFLICT`	`11 15`		`PLRQA -> LCGRL (in Ref. 1).`
`CONFLICT`	`22 22`		`R -> L (in Ref. 1).`
`CONFLICT`	`25 25`		`R -> C (in Ref. 1).`
`CONFLICT`	`238 238`		`T -> N (in Ref. 1).`
`CONFLICT`	`241 242`		`AH -> CY (in Ref. 1).`
`CONFLICT`	`259 259`		`E -> G (in Ref. 1).`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 38982 Da [This is the MW of the unprocessed precursor]

CRC64: 1B942D0A68C86D51 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV 

        70         80         90        100        110        120 
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 

       130        140        150        160        170        180 
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDDNPVVML ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI

P49432 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