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Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandPyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciRPRO272947:G1GT0-264-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha (EC:1.2.4.1)
Gene namesi
Name:pdhA
Ordered Locus Names:RP261
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
Proteomesi
  • UP000002480 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622041 – 326Pyruvate dehydrogenase E1 component subunit alphaAdd BLAST326

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

STRINGi272947.RP261

Structurei

3D structure databases

ProteinModelPortaliQ9ZDR4
SMRiQ9ZDR4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4107R0V Bacteria
COG1071 LUCA
HOGENOMiHOG000281336
KOiK00161
OMAiYRSHGFT

Family and domain databases

InterProiView protein in InterPro
IPR001017 DH_E1
IPR017597 Pyrv_DH_E1_asu_subgrp-y
IPR029061 THDP-binding
PfamiView protein in Pfam
PF00676 E1_dh, 1 hit
SUPFAMiSSF52518 SSF52518, 1 hit
TIGRFAMsiTIGR03182 PDH_E1_alph_y, 1 hit

Sequencei

Sequence statusi: Complete.

Q9ZDR4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDIKPEKYKP IKEEYIKSFK DMLLLRRFEE KCGQLYGMGK IGGFCHLYIG
60 70 80 90 100
QEAVISAVAM IKKKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS
110 120 130 140 150
KGKGGSMHLF DIPNKFYGGH GIVGAQVPIG TGLAFAEKYN GTNNICFTFL
160 170 180 190 200
GDGAVNQGQV YEAFNMASLW GLPIVYIIEN NEYSMGTSVA RSTFMCDLYK
210 220 230 240 250
KGESFGIRGF QLDGMDFEEM YNGTKQVAEY VRENSFPVIL EVKTYRYRGH
260 270 280 290 300
SMSDPAKYRS KEEVEKYKER DTLVRIREII LDNKYATEAD LKAIEQSVRE
310 320
IIKVAVEFSE NSPLPAEDEL YTEIYV
Length:326
Mass (Da):36,824
Last modified:May 1, 1999 - v1
Checksum:iBC9A6F66044B213A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235271 Genomic DNA Translation: CAA14723.1
PIRiA71681
RefSeqiNP_220646.1, NC_000963.1
WP_004596096.1, NC_000963.1

Genome annotation databases

EnsemblBacteriaiCAA14723; CAA14723; CAA14723
GeneIDi883166
KEGGirpr:RP261
PATRICifig|272947.5.peg.268

Similar proteinsi

Entry informationi

Entry nameiODPA_RICPR
AccessioniPrimary (citable) accession number: Q9ZDR4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: March 28, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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