[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 31-54. DOI=10.1016/0006-291X(88)90714-0; PubMed=2829898 [NCBI, ExPASy, EBI, Israel, Japan] Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.; "Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex."; Biochem. Biophys. Res. Commun. 150:904-908(1988).

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.
SEQUENCE CAUTION:
- Sequence=AAX46758.1; Type=Frameshift; Positions=201;

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

BT021911; AAX46758.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC150020; AAI50021.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B27712; B27712.

NP_001030512.2; -.

3D structure databases

HSSP

P11177; 1NI4. [HSSP ENTRY / PDB]

SMR

P11966; 30-359.

ModBase

P11966.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
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

P11966.

Genome annotation databases

Ensembl

ENSBTAG00000021724; Bos taurus. [Contig view]

GeneID

613610; -.

KEGG

bta:613610; -.

Phylogenomic databases

HOVERGEN

P11966; -.

Other

ProtoNet

P11966.

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_0000162216`
`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: 39126 Da [This is the MW of the unprocessed precursor]

CRC64: 584B86D36A233EFC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVVAVLVRK PLEQVSGLLR RRFHRTAPAA LQVTVREAIN QGMDEELERD EKVFLLGEEV 

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

       130        140        150        160        170        180 
DQVINSAAKT YYMSGGLQSV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWSS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF ELPSEAQSKD FLIPIGKAKI ERQGTHVTIV 

       250        260        270        280        290        300 
AHSRPVGHCL EAATVLSKEG IECEVINLRT IRPMDIETIE GSVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSVPQVKDII FAIKKTLNI

P11966 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