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: Tetramer of 2 alpha and 2 beta subunits (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).

Copyright

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Cross-references

Sequence databases

EMBL

CR857655; CAH89928.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q5RE79; 30-359.

ModBase

Q5RE79.

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

Q5RE79.

Phylogenomic databases

HOVERGEN

Q5RE79; -.

Other

ProtoNet

Q5RE79.

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`	`31 359`	`329`	`Pyruvate dehydrogenase E1 component subunit beta, mitochondrial.`	`PRO_0000271409`
`BINDING`	`89 89`		`Thiamine pyrophosphate (By similarity).`
`MOD_RES`	`67 67`		`Phosphotyrosine (By similarity).`

Sequence information

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

Molecular weight: 39333 Da [This is the MW of the unprocessed precursor]

CRC64: 8575D7E8740D431B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVSGLVRR PLREVSRLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 

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

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

       190        200        210        220        230        240 
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI

Q5RE79 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