NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1735725 [NCBI, ExPASy, EBI, Israel, Japan]
Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.";
J. Bacteriol. 174:1388-1396(1992).

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).
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.

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

M81753; AAA21907.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42653; A42653.

3D structure databases

HSSP

P12694; 1DTW. [HSSP ENTRY / PDB]

ModBase

P35485.

Ontologies

GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
IPR017596; Pyrv_DH_E1_asu_subgrp-x.
Graphical view of domain structure.

Pfam

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

Other

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

Keywords

Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 345`	`>345`	`Pyruvate dehydrogenase E1 component subunit alpha.`	`PRO_0000162197`
`NON_TER`	`1 1`

Sequence information

Length: 345 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 38962 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 797F9F67DE0C2995 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DQNGKVVNEK MEPKLPKETL LKMYKTAVLG RNADIKALQY QRQGRMLTYA PNMGQEAAQI 

        70         80         90        100        110        120 
GMAAAMEPQD WNSPMYRELN TLLYRGDKLE NVFLYWYGNE RGSIKPEGVK ILPTNIIIGS 

       130        140        150        160        170        180 
QSNIAAGLAM ASKIRKTNEV TAFTIGDGGT AHGEFYEGLN FAASFKAPVV AVIQNNQWAI 

       190        200        210        220        230        240 
STPVRKASNS ETLAQKGVAF GIPYIQVDGN DMLAMYVASK EAMDRARKGD GPTLIEAFTY 

       250        260        270        280        290        300 
RMGPHTTSDD PCSIYRTKEE ENEWAKKDQI ARFKTYLINK GYWSEEEDKK LEEEVLAEIN 

       310        320        330        340 
DTFKKVESYG ANVELIEIFE HTYAEMTPQL KEQYEEHKKY LEGVK

P35485 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