NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1007/s00239-004-2638-3; PubMed=15638458 [NCBI, ExPASy, EBI, Israel, Japan]
Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
"Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids.";
J. Mol. Evol. 59:464-477(2004).

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

AY673996; AAT79704.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_063629.1; -.

3D structure databases

ModBase

Q6B8T1.

Ontologies

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

Q6B8T1.

Genome annotation databases

GeneID

2943994; -.

Other

ProtoNet

Q6B8T1.

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`	`1 323`	`323`	`Pyruvate dehydrogenase E1 component subunit beta.`	`PRO_0000280108`
`BINDING`	`60 60`		`Thiamine pyrophosphate (By similarity).`

Sequence information

Length: 323 AA [This is the length of the unprocessed precursor]

Molecular weight: 35742 Da [This is the MW of the unprocessed precursor]

CRC64: EF7821FA426BFEED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTEVLMFDAL REATDEEMQN DSSVFILGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE 

        70         80         90        100        110        120 
NSFMGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFQ IPIVIRGPGG 

       130        140        150        160        170        180 
VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVIF FEHVLLYNLK 

       190        200        210        220        230        240 
DELPNDEYFL PLDKAELVRD GLDVTILTYS RMRHHVMQAV VDLVNDGYNP EVIDLISLKP 

       250        260        270        280        290        300 
LDITSIAQSL MKTHKLIIVE ECMKTGGIGA EIIAQINDNY FDFLDAPIVR LSSQDIPTPY 

       310        320 
NGKLEKATVI YPQQIIEAVK SIV

Q6B8T1 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