NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=10D;
DOI=10.1093/dnares/10.2.67; PubMed=12755171 [NCBI, ExPASy, EBI, Israel, Japan]
Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K., Shin-i T., Kohara Y., Kuroiwa T.;
"Complete sequence and analysis of the plastid genome of the unicellular red alga Cyanidioschyzon merolae.";
DNA Res. 10:67-77(2003).

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

AB002583; BAC76222.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_849060.1; -.

3D structure databases

HSSP

Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]

ModBase

Q85FX1.

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

Q85FX1.

Genome annotation databases

GeneID

844910; -.

Other

ProtoNet

Q85FX1.

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_0000280106`
`BINDING`	`61 61`		`Thiamine pyrophosphate (By similarity).`

Sequence information

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

Molecular weight: 35983 Da [This is the MW of the unprocessed precursor]

CRC64: FA96561EDDF71DF3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLHKLFMYEA LREAIDEEMA RDKRVFVLGE DVGHYGGSYK VTKQLHTKYG DLRVLDTPIA 

        70         80         90        100        110        120 
ENSFTGMAIG AAMTGLKPVV EGMNLSFLLL AFNQISNNAG MLHYTSGGNW SIPLVIRGPG 

       130        140        150        160        170        180 
GIGKQLSAEH SQRIEAYFQA VPGLKIVACS TPYNAKGLLK AAIRDNNPVL FLEHVLLYNL 

       190        200        210        220        230        240 
KQEIPKQEYV LPLDKAQVVR EGSDVTIITY SRMLHHVMQA VKQLVAQGMN PEVIDLISLK 

       250        260        270        280        290        300 
PIDLETLVTS VSKTHKAIIV EECMQTGGIA AEVMAQIYSH AFDELDAPIR RLSSKDVPTP 

       310        320 
YNGYLEQACL VQPTQIVEAV KTLMST

Q85FX1 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