[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[2]	PROTEIN SEQUENCE OF 130-137; 237-246 AND 262-272, AND MASS SPECTROMETRY. Bienvenut W.V.; Submitted (SEP-2005) 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) (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).
INTERACTION:
O45924:-; NbExp=1; IntAct=EBI-326559, EBI-330432;
Q9NGT3:mdf-2; NbExp=1; IntAct=EBI-326559, EBI-328699;
Q09620:sdz-38; NbExp=1; IntAct=EBI-326559, EBI-332504;
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

AF038606; AAB92024.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T32598; T32598.

NP_500340.1; -.

3D structure databases

HSSP

P11177; 1NI4. [HSSP ENTRY / PDB]

ModBase

O44451.

Protein-protein interaction databases

DIP

DIP:24348N; -.

IntAct

O44451; 6.

Organism-specific databases

WormBase

WBGene00015413; C04C3.3.

WormPep

C04C3.3; CE27647. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

O44451; -.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
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).
GO:0040010;	Biological process: positive regulation of growth rate (inferred from mutant phenotype from WormBase).
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.

Genome annotation databases

Ensembl

C04C3.3; Caenorhabditis elegans. [Contig view]

GeneID

177108; -.

KEGG

cel:C04C3.3; -.

Other

895372; -.

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

Keywords

Complete proteome; Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 21`	`21`	`Mitochondrion (Potential).`
`CHAIN`	`22 352`	`331`	`Pyruvate dehydrogenase E1 component subunit beta, mitochondrial.`	`PRO_0000042638`
`BINDING`	`81 81`		`Thiamine pyrophosphate (By similarity).`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 38141 Da [This is the MW of the unprocessed precursor]

CRC64: 37F4A4A28C8ADECA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRKCGNLF VARLAGTSTR AASTMTVRDA LNQAMDEEIK RDDRVFLMGE EVAQYDGAYK 

        70         80         90        100        110        120 
ISKGLWKKHG DKRVVDTPIT EMGFAGIAVG AAFAGLRPIC EFMTFNFSMQ AIDQIINSAA 

       130        140        150        160        170        180 
KTYYMSAGRV PVPIVFRGPN GAAAGVAAQH SQDFSAWYAH CPGLKVVCPY SAEDAKGLLK 

       190        200        210        220        230        240 
AAIRDDNPVV FLENEILYGQ SFPVGDEVLS DDFVVPIGKA KIERAGDHVT IVSYSRGVEF 

       250        260        270        280        290        300 
SLEAAKQLEA IGVSAEVINL RSLRPFDFES IRQSVHKTHH LVSVETGWPF AGIGSEIAAQ 

       310        320        330        340        350 
VMESDVFDQL DAPLLRVTGV DVPMPYTQTL EAAALPTAEH VVKAVKKSLN IA

O44451 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