NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=M1311;
DOI=10.1073/pnas.162203299; PubMed=12161560 [NCBI, ExPASy, EBI, Israel, Japan]
Turmel M., Otis C., Lemieux C.;
"The chloroplast and mitochondrial genome sequences of the charophyte Chaetosphaeridium globosum: insights into the timing of the events that restructured organelle DNAs within the green algal lineage that led to land plants.";
Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(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 (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.

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

AF494278; AAM96525.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_683783.1; -.

3D structure databases

HSSP

Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]

ModBase

Q8MA03.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
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

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

GeneID

860807; -.

Other

ProtoNet

Q8MA03.

UniRef

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

Keywords

Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 326`	`326`	`Pyruvate dehydrogenase E1 component subunit beta.`	`PRO_0000280101`
`BINDING`	`60 60`		`Thiamine pyrophosphate (By similarity).`

Sequence information

Length: 326 AA [This is the length of the unprocessed precursor]

Molecular weight: 35969 Da [This is the MW of the unprocessed precursor]

CRC64: 9E99DFC6EBABDB3C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEVLLFEAL RDALDEEMQR DPSVLVMGED VGHYGGSYKV TKGFHEKYGD LRLLDTPIAE 

        70         80         90        100        110        120 
NSFTGMAIGA AMTGLRPIVE GMNMGFLLLA FNQIANNAGM LHYTSGGNFK IPIVIRGPGG 

       130        140        150        160        170        180 
VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNGKGLLKS AIRNDNPVIF FEHVLLYNLN 

       190        200        210        220        230        240 
ENLIEQEYLL CLEKAEVVRP GNDITILTYS RMRHHVLQAA KVLVNKGYDP EIIDILSLKP 

       250        260        270        280        290        300 
LDMGTISLSV RKTHKVLIVE ECMRTGGIGA SLRAAILEDL FDYLDAPIQC LSSQDVPTPY 

       310        320 
SGPLEELTVI QPNQIIQAVE EMCKIE

Q8MA03 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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