NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Madrid E;
DOI=10.1038/24094; PubMed=9823893 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.;
"The genome sequence of Rickettsia prowazekii and the origin of mitochondria.";
Nature 396:133-140(1998).

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.

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

AJ235271; CAA14724.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B71681; B71681.

RefSeq

NP_220647.1; -.

3D structure databases

HSSP

Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]

ModBase

Q9ZDR3.

Enzyme and pathway databases

BioCyc

RPRO272947:RP262-MON; -.

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

Q9ZDR3.

Genome annotation databases

GeneID

883167; -.

GenomeReviews

AJ235269_GR; RP262.

KEGG

rpr:RP262; -.

Phylogenomic databases

HOGENOM

Q9ZDR3; -.

Genome annotation databases

CMR

Q9ZDR3; RP262.

Other

ProtoNet

Q9ZDR3.

UniRef

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

Keywords

Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 326`	`326`	`Pyruvate dehydrogenase E1 component subunit beta.`	`PRO_0000162227`
`BINDING`	`59 59`		`Thiamine pyrophosphate (By similarity).`

Sequence information

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

Molecular weight: 35917 Da [This is the MW of the unprocessed precursor]

CRC64: 12A50A7ABBB28A46 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQITVREALR DAMQEEMLRD EKVFVIGEEV AEYQGAYKVT QGLLEQFGSK RVIDTPITEY 

        70         80         90        100        110        120 
GFAGLAVGAA FAGLRPIVEF MTFNFAMQAF DHIVNSAAKT HYMSGGQVKC PIVFRGPNGA 

       130        140        150        160        170        180 
ASRVAAQHSQ NYTACYSHIP GLKVVAPYSA EDHKGLMLTA IRDDNPVIFL ENEILYGHSF 

       190        200        210        220        230        240 
DVPDIIEPIP FSKAKILKEG SNVTIVTFSI QVKLALDVVN ILQNDNIDCE LIDLRTIKPL 

       250        260        270        280        290        300 
DTDSIIESVK KTNRLVIVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDVPLPYA 

       310        320 
VNLEKLAMPS ANDLIEAVKK VCYYSI

Q9ZDR3 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