[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Avonport; Reith M.E., Munholland J.; "Complete nucleotide sequence of the Porphyra purpurea chloroplast genome."; Plant Mol. Biol. Rep. 13:333-335(1995).

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.
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

U38804; AAC08153.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S73188; S73188.

RefSeq

NP_053877.1; -.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

ModBase

P51267.

Family and domain databases

InterPro

IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

BLOCKS

P51267.

Genome annotation databases

GeneID

809896; -.

Other

ProtoNet

P51267.

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`	`1 344`	`344`		`Pyruvate dehydrogenase E1 component subunit alpha.`	`PRO_0000162215`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 38507 Da [This is the MW of the unprocessed precursor]

CRC64: 799BD9AFA06FF455 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYPKKVELP LTNCNQINLT KHKLLVLYED MLLGRNFEDM CAQMYYKGKM FGFVHLYNGQ 

        70         80         90        100        110        120 
EAVSTGVIKL LDSKDYVCST YRDHVHALSK GVPSQNVMAE LFGKETGCSR GRGGSMHIFS 

       130        140        150        160        170        180 
APHNFLGGFA FIAEGIPVAT GAAFQSIYRQ QVLKEPGELR VTACFFGDGT TNNGQFFECL 

       190        200        210        220        230        240 
NMAVLWKLPI IFVVENNQWA IGMAHHRSSS IPEIHKKAEA FGLPGIEVDG MDVLAVRQVA 

       250        260        270        280        290        300 
EKAVERARQG QGPTLIEALT YRFRGHSLAD PDELRSRQEK EAWVARDPIK KLKKHILDNQ 

       310        320        330        340 
IASSDELNDI QSSVKIDLEQ SVEFAMSSPE PNISELKRYL FADN

P51267 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