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P0AFG8

- ODP1_ECOLI

UniProt

P0AFG8 - ODP1_ECOLI

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Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi231 – 2311Magnesium
Metal bindingi261 – 2611Magnesium
Metal bindingi263 – 2631Magnesium; via carbonyl oxygen

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW
  3. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  4. pyruvate dehydrogenase activity Source: EcoliWiki

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10024. aceE.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 887886Pyruvate dehydrogenase E1 componentPRO_0000162243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei716 – 7161N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AFG8.
PRIDEiP0AFG8.

2D gel databases

SWISS-2DPAGEP0AFG8.

Expressioni

Gene expression databases

GenevestigatoriP0AFG8.

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

BioGridi849234. 1 interaction.
DIPiDIP-9039N.
IntActiP0AFG8. 104 interactions.
MINTiMINT-1261483.
STRINGi511145.b0114.

Structurei

Secondary structure

1
887
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 683Combined sources
Helixi76 – 9924Combined sources
Helixi109 – 12416Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi137 – 1393Combined sources
Helixi142 – 1443Combined sources
Helixi145 – 15410Combined sources
Helixi160 – 1634Combined sources
Turni181 – 1833Combined sources
Turni185 – 1873Combined sources
Helixi197 – 21418Combined sources
Beta strandi225 – 2306Combined sources
Helixi232 – 2354Combined sources
Helixi237 – 2404Combined sources
Helixi243 – 2486Combined sources
Beta strandi254 – 2607Combined sources
Beta strandi262 – 2643Combined sources
Beta strandi265 – 2695Combined sources
Helixi275 – 28511Combined sources
Beta strandi289 – 2935Combined sources
Helixi299 – 3057Combined sources
Helixi310 – 3178Combined sources
Helixi320 – 3267Combined sources
Helixi331 – 3377Combined sources
Beta strandi339 – 3424Combined sources
Helixi343 – 3464Combined sources
Turni347 – 3515Combined sources
Helixi354 – 3585Combined sources
Helixi363 – 3653Combined sources
Helixi367 – 37913Combined sources
Beta strandi385 – 3906Combined sources
Turni393 – 3964Combined sources
Turni398 – 4003Combined sources
Turni401 – 4033Combined sources
Helixi407 – 4093Combined sources
Helixi416 – 4249Combined sources
Helixi431 – 4344Combined sources
Helixi447 – 45812Combined sources
Helixi479 – 4824Combined sources
Helixi483 – 4864Combined sources
Helixi495 – 50612Combined sources
Turni510 – 5156Combined sources
Beta strandi516 – 5227Combined sources
Helixi525 – 5273Combined sources
Helixi530 – 5367Combined sources
Turni549 – 5524Combined sources
Beta strandi553 – 5553Combined sources
Beta strandi565 – 5673Combined sources
Helixi572 – 58312Combined sources
Helixi585 – 5884Combined sources
Beta strandi594 – 6007Combined sources
Helixi601 – 6033Combined sources
Helixi605 – 61713Combined sources
Beta strandi623 – 6286Combined sources
Turni631 – 6333Combined sources
Turni635 – 6373Combined sources
Turni639 – 6413Combined sources
Helixi646 – 6505Combined sources
Beta strandi656 – 6594Combined sources
Helixi664 – 67916Combined sources
Beta strandi687 – 6915Combined sources
Turni704 – 7063Combined sources
Helixi707 – 7126Combined sources
Beta strandi715 – 7206Combined sources
Beta strandi723 – 7319Combined sources
Helixi733 – 7353Combined sources
Helixi736 – 75015Combined sources
Beta strandi752 – 7587Combined sources
Helixi762 – 77817Combined sources
Helixi788 – 7925Combined sources
Beta strandi798 – 8014Combined sources
Helixi807 – 8104Combined sources
Helixi811 – 8155Combined sources
Beta strandi817 – 8193Combined sources
Beta strandi821 – 8244Combined sources
Helixi835 – 8417Combined sources
Helixi846 – 85914Combined sources
Beta strandi861 – 8633Combined sources
Helixi865 – 87410Combined sources
Turni884 – 8863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 57-887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG8.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2609.
HOGENOMiHOG000115215.
InParanoidiP0AFG8.
KOiK00163.
OMAiKGIYKLD.
OrthoDBiEOG6BW4TW.
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/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view]
PfamiPF00456. Transketolase_N. 2 hits.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461P → R in CAA24740. (PubMed:6343085)Curated
Sequence conflicti276 – 2761Missing in CAA24740. (PubMed:6343085)Curated

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.
YP_488417.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73225; AAC73225; b0114.
BAB96684; BAB96684; BAB96684.
GeneIDi12932309.
944834.
KEGGiecj:Y75_p0111.
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 .
PIRi B64734. DEECPV.
RefSeqi NP_414656.1. NC_000913.3.
YP_488417.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L8A X-ray 1.85 A/B 2-887 [» ]
1RP7 X-ray 2.09 A/B 2-887 [» ]
2G25 X-ray 2.10 A/B 2-887 [» ]
2G28 X-ray 1.85 A/B 2-887 [» ]
2G67 X-ray 2.32 A/B 2-887 [» ]
2IEA X-ray 1.85 A/B 2-887 [» ]
2QTA X-ray 1.85 A/B 2-887 [» ]
2QTC X-ray 1.77 A/B 2-887 [» ]
DisProti DP00427.
ProteinModelPortali P0AFG8.
SMRi P0AFG8. Positions 57-887.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849234. 1 interaction.
DIPi DIP-9039N.
IntActi P0AFG8. 104 interactions.
MINTi MINT-1261483.
STRINGi 511145.b0114.

2D gel databases

SWISS-2DPAGE P0AFG8.

Proteomic databases

PaxDbi P0AFG8.
PRIDEi P0AFG8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73225 ; AAC73225 ; b0114 .
BAB96684 ; BAB96684 ; BAB96684 .
GeneIDi 12932309.
944834.
KEGGi ecj:Y75_p0111.
eco:b0114.
PATRICi 32115329. VBIEscCol129921_0116.

Organism-specific databases

EchoBASEi EB0023.
EcoGenei EG10024. aceE.

Phylogenomic databases

eggNOGi COG2609.
HOGENOMi HOG000115215.
InParanoidi P0AFG8.
KOi K00163.
OMAi KGIYKLD.
OrthoDBi EOG6BW4TW.
PhylomeDBi P0AFG8.

Enzyme and pathway databases

BioCyci EcoCyc:E1P-MONOMER.
ECOL316407:JW0110-MONOMER.
MetaCyc:E1P-MONOMER.
SABIO-RK P0AFG8.

Miscellaneous databases

EvolutionaryTracei P0AFG8.
PROi P0AFG8.

Gene expression databases

Genevestigatori P0AFG8.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view ]
Pfami PF00456. Transketolase_N. 2 hits.
[Graphical view ]
PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00759. aceE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component."
    Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.
    Eur. J. Biochem. 133:155-162(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 145 AND 275.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene."
    Haydon D.J., Quail M.A., Guest J.R.
    FEBS Lett. 336:43-47(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    Strain: K12.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  9. "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution."
    Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W.
    Biochemistry 41:5213-5221(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

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 26, 2014
This is version 100 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

External Data

Dasty 3