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Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi231Magnesium1
Metal bindingi261Magnesium1
Metal bindingi263Magnesium; via carbonyl oxygen1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • magnesium ion binding Source: CAFA
  • protein homodimerization activity Source: CAFA
  • pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  • pyruvate dehydrogenase activity Source: EcoliWiki
  • thiamine pyrophosphate binding Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandMagnesium, Metal-binding, Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:E1P-MONOMER
MetaCyc:E1P-MONOMER
BRENDAi1.2.4.1 2026
SABIO-RKiP0AFG8

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
Short name:
PDH E1 component
Gene namesi
Name:aceE
Ordered Locus Names:b0114, JW0110
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10024 aceE

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB01987 Thiamin Diphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001622432 – 887Pyruvate dehydrogenase E1 componentAdd BLAST886

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei716N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0AFG8
PaxDbiP0AFG8
PRIDEiP0AFG8

2D gel databases

SWISS-2DPAGEiP0AFG8

PTM databases

CarbonylDBiP0AFG8
iPTMnetiP0AFG8

Interactioni

Subunit structurei

Homodimer. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4261303, 14 interactors
849234, 1 interactor
DIPiDIP-9039N
IntActiP0AFG8, 104 interactors
STRINGi316385.ECDH10B_0094

Structurei

Secondary structure

1887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00427
ProteinModelPortaliP0AFG8
SMRiP0AFG8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG8

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105DAQ Bacteria
COG2609 LUCA
HOGENOMiHOG000115215
InParanoidiP0AFG8
KOiK00163
OMAiREPWFPG
PhylomeDBiP0AFG8

Family and domain databases

CDDicd02017 TPP_E1_EcPDC_like, 1 hit
Gene3Di3.40.50.920, 1 hit
InterProiView protein in InterPro
IPR004660 2-oxoA_DH_E1
IPR035807 PDC_E1_N
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005474 Transketolase_N
PANTHERiPTHR43825:SF3 PTHR43825:SF3, 1 hit
PfamiView protein in Pfam
PF00456 Transketolase_N, 1 hit
PIRSFiPIRSF000156 Pyruvate_dh_E1, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
TIGRFAMsiTIGR00759 aceE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFG8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN
60 70 80 90 100
VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK
110 120 130 140 150
DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA
160 170 180 190 200
RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI
210 220 230 240 250
GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK
260 270 280 290 300
LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
310 320 330 340 350
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA
360 370 380 390 400
DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA
410 420 430 440 450
AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT
460 470 480 490 500
YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV
510 520 530 540 550
RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD
560 570 580 590 600
REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
610 620 630 640 650
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS
660 670 680 690 700
LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP
710 720 730 740 750
AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY
760 770 780 790 800
GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA
810 820 830 840 850
STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV
860 870 880
VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA
Length:887
Mass (Da):99,668
Last modified:January 23, 2007 - v2
Checksum:i7FB3811DE11BDD02
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti146P → R in CAA24740 (PubMed:6343085).Curated1
Sequence conflicti276Missing in CAA24740 (PubMed:6343085).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01498 Genomic DNA Translation: CAA24740.1
U00096 Genomic DNA Translation: AAC73225.1
AP009048 Genomic DNA Translation: BAB96684.2
S67363 Genomic DNA Translation: AAB29357.1
PIRiB64734 DEECPV
RefSeqiNP_414656.1, NC_000913.3
WP_000003820.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73225; AAC73225; b0114
BAB96684; BAB96684; BAB96684
GeneIDi944834
KEGGiecj:JW0110
eco:b0114
PATRICifig|1411691.4.peg.2168

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01498 Genomic DNA Translation: CAA24740.1
U00096 Genomic DNA Translation: AAC73225.1
AP009048 Genomic DNA Translation: BAB96684.2
S67363 Genomic DNA Translation: AAB29357.1
PIRiB64734 DEECPV
RefSeqiNP_414656.1, NC_000913.3
WP_000003820.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L8AX-ray1.85A/B2-887[»]
1RP7X-ray2.09A/B2-887[»]
2G25X-ray2.10A/B2-887[»]
2G28X-ray1.85A/B2-887[»]
2G67X-ray2.32A/B2-887[»]
2IEAX-ray1.85A/B2-887[»]
2QTAX-ray1.85A/B2-887[»]
2QTCX-ray1.77A/B2-887[»]
DisProtiDP00427
ProteinModelPortaliP0AFG8
SMRiP0AFG8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261303, 14 interactors
849234, 1 interactor
DIPiDIP-9039N
IntActiP0AFG8, 104 interactors
STRINGi316385.ECDH10B_0094

Chemistry databases

DrugBankiDB01987 Thiamin Diphosphate

PTM databases

CarbonylDBiP0AFG8
iPTMnetiP0AFG8

2D gel databases

SWISS-2DPAGEiP0AFG8

Proteomic databases

EPDiP0AFG8
PaxDbiP0AFG8
PRIDEiP0AFG8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73225; AAC73225; b0114
BAB96684; BAB96684; BAB96684
GeneIDi944834
KEGGiecj:JW0110
eco:b0114
PATRICifig|1411691.4.peg.2168

Organism-specific databases

EchoBASEiEB0023
EcoGeneiEG10024 aceE

Phylogenomic databases

eggNOGiENOG4105DAQ Bacteria
COG2609 LUCA
HOGENOMiHOG000115215
InParanoidiP0AFG8
KOiK00163
OMAiREPWFPG
PhylomeDBiP0AFG8

Enzyme and pathway databases

BioCyciEcoCyc:E1P-MONOMER
MetaCyc:E1P-MONOMER
BRENDAi1.2.4.1 2026
SABIO-RKiP0AFG8

Miscellaneous databases

EvolutionaryTraceiP0AFG8
PROiPR:P0AFG8

Family and domain databases

CDDicd02017 TPP_E1_EcPDC_like, 1 hit
Gene3Di3.40.50.920, 1 hit
InterProiView protein in InterPro
IPR004660 2-oxoA_DH_E1
IPR035807 PDC_E1_N
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005474 Transketolase_N
PANTHERiPTHR43825:SF3 PTHR43825:SF3, 1 hit
PfamiView protein in Pfam
PF00456 Transketolase_N, 1 hit
PIRSFiPIRSF000156 Pyruvate_dh_E1, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
TIGRFAMsiTIGR00759 aceE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiODP1_ECOLI
AccessioniPrimary (citable) accession number: P0AFG8
Secondary accession number(s): P06958, P78049, Q53382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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