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Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • metal ion binding Source: UniProtKB-KW
  • pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  • pyruvate dehydrogenase activity Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding, Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:E1P-MONOMER.
ECOL316407:JW0110-MONOMER.
MetaCyc:E1P-MONOMER.
BRENDAi1.2.4.1. 2026.
SABIO-RKP0AFG8.

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

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

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-2DPAGEP0AFG8.

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

WithEntry#Exp.IntActNotes
itself2EBI-542683,EBI-542683
groLP0A6F52EBI-542683,EBI-543750
nthP0AB832EBI-542683,EBI-555213
ybhFP0A9U12EBI-542683,EBI-547696
yciUP0A8L72EBI-542683,EBI-544511

Protein-protein interaction databases

BioGridi4261303. 14 interactors.
849234. 1 interactor.
DIPiDIP-9039N.
IntActiP0AFG8. 104 interactors.
MINTiMINT-1261483.
STRINGi511145.b0114.

Structurei

Secondary structure

1887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi66 – 68Combined sources3
Helixi76 – 99Combined sources24
Helixi109 – 124Combined sources16
Beta strandi131 – 133Combined sources3
Beta strandi137 – 139Combined sources3
Helixi142 – 144Combined sources3
Helixi145 – 154Combined sources10
Helixi160 – 163Combined sources4
Turni181 – 183Combined sources3
Turni185 – 187Combined sources3
Helixi197 – 214Combined sources18
Beta strandi225 – 230Combined sources6
Helixi232 – 235Combined sources4
Helixi237 – 240Combined sources4
Helixi243 – 248Combined sources6
Beta strandi254 – 260Combined sources7
Beta strandi262 – 264Combined sources3
Beta strandi265 – 269Combined sources5
Helixi275 – 285Combined sources11
Beta strandi289 – 293Combined sources5
Helixi299 – 305Combined sources7
Helixi310 – 317Combined sources8
Helixi320 – 326Combined sources7
Helixi331 – 337Combined sources7
Beta strandi339 – 342Combined sources4
Helixi343 – 346Combined sources4
Turni347 – 351Combined sources5
Helixi354 – 358Combined sources5
Helixi363 – 365Combined sources3
Helixi367 – 379Combined sources13
Beta strandi385 – 390Combined sources6
Turni393 – 396Combined sources4
Turni398 – 400Combined sources3
Turni401 – 403Combined sources3
Helixi407 – 409Combined sources3
Helixi416 – 424Combined sources9
Helixi431 – 434Combined sources4
Helixi447 – 458Combined sources12
Helixi479 – 482Combined sources4
Helixi483 – 486Combined sources4
Helixi495 – 506Combined sources12
Turni510 – 515Combined sources6
Beta strandi516 – 522Combined sources7
Helixi525 – 527Combined sources3
Helixi530 – 536Combined sources7
Turni549 – 552Combined sources4
Beta strandi553 – 555Combined sources3
Beta strandi565 – 567Combined sources3
Helixi572 – 583Combined sources12
Helixi585 – 588Combined sources4
Beta strandi594 – 600Combined sources7
Helixi601 – 603Combined sources3
Helixi605 – 617Combined sources13
Beta strandi623 – 628Combined sources6
Turni631 – 633Combined sources3
Turni635 – 637Combined sources3
Turni639 – 641Combined sources3
Helixi646 – 650Combined sources5
Beta strandi656 – 659Combined sources4
Helixi664 – 679Combined sources16
Beta strandi687 – 691Combined sources5
Turni704 – 706Combined sources3
Helixi707 – 712Combined sources6
Beta strandi715 – 720Combined sources6
Beta strandi723 – 731Combined sources9
Helixi733 – 735Combined sources3
Helixi736 – 750Combined sources15
Beta strandi752 – 758Combined sources7
Helixi762 – 778Combined sources17
Helixi788 – 792Combined sources5
Beta strandi798 – 801Combined sources4
Helixi807 – 810Combined sources4
Helixi811 – 815Combined sources5
Beta strandi817 – 819Combined sources3
Beta strandi821 – 824Combined sources4
Helixi835 – 841Combined sources7
Helixi846 – 859Combined sources14
Beta strandi861 – 863Combined sources3
Helixi865 – 874Combined sources10
Turni884 – 886Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP0AFG8.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105DAQ. Bacteria.
COG2609. LUCA.
HOGENOMiHOG000115215.
InParanoidiP0AFG8.
KOiK00163.
OMAiGFVPQRR.
PhylomeDBiP0AFG8.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 5 hits.
PfamiPF00456. Transketolase_N. 1 hit.
[Graphical view]
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.
PATRICi32115329. VBIEscCol129921_0116.

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.
MINTiMINT-1261483.
STRINGi511145.b0114.

2D gel databases

SWISS-2DPAGEP0AFG8.

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.
PATRICi32115329. VBIEscCol129921_0116.

Organism-specific databases

EchoBASEiEB0023.
EcoGeneiEG10024. aceE.

Phylogenomic databases

eggNOGiENOG4105DAQ. Bacteria.
COG2609. LUCA.
HOGENOMiHOG000115215.
InParanoidiP0AFG8.
KOiK00163.
OMAiGFVPQRR.
PhylomeDBiP0AFG8.

Enzyme and pathway databases

BioCyciEcoCyc:E1P-MONOMER.
ECOL316407:JW0110-MONOMER.
MetaCyc:E1P-MONOMER.
BRENDAi1.2.4.1. 2026.
SABIO-RKP0AFG8.

Miscellaneous databases

EvolutionaryTraceiP0AFG8.
PROiP0AFG8.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 5 hits.
PfamiPF00456. Transketolase_N. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 115 of the entry and version 2 of the sequence. [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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.