NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/molbev/msk018; PubMed=16611644 [NCBI, ExPASy, EBI, Israel, Japan]
Turmel M., Otis C., Lemieux C.;
"The chloroplast genome sequence of Chara vulgaris sheds new light into the closest green algal relatives of land plants.";
Mol. Biol. Evol. 23:1324-1338(2006).

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

DQ229107; ABA61922.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_635737.1; -.

3D structure databases

ModBase

Q1ACL0.

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

4100209; -.

Other

ProtoNet

Q1ACL0.

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_0000280102`
`BINDING`	`60 60`		`Thiamine pyrophosphate (By similarity).`

Sequence information

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

Molecular weight: 36005 Da [This is the MW of the unprocessed precursor]

CRC64: DF4773E0A838D07A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEKLLYEAL NEGIHEEIER DPKVFVIGED IGHYGGSYKV TKGLFEKYGN LRILDTPIAE 

        70         80         90        100        110        120 
NSFTGIAIGA AMTGLRPIIE GMNMGFLLLA FNQIANNAGM LHYTSGGNFT TPLVVRGPGG 

       130        140        150        160        170        180 
VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNAKGLIKS AIRSQNPIIF FEHVLLYNIK 

       190        200        210        220        230        240 
ENIPQKEYLV PLEKAELVRS GNQITILTYS RMRYHVLQAA KTLIEKGYDP EIIDIISLKP 

       250        260        270        280        290        300 
LDMGTISTSL RKTHKVLIVE ECMKTGGIGT TLKSAILESL FDFLDTPIMS LSSQDVPTPY 

       310        320 
NGFLEDLTVI QPSQIVEAAE KIILYS

Q1ACL0 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