SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AFG8

- ODP1_ECOLI

UniProt

P0AFG8 - ODP1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyruvate dehydrogenase E1 component

Gene
aceE, b0114, JW0110
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

Magnesium.
Thiamine pyrophosphate.

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. protein binding Source: IntAct
  4. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  5. 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 – 683
Helixi76 – 9924
Helixi109 – 12416
Beta strandi131 – 1333
Beta strandi137 – 1393
Helixi142 – 1443
Helixi145 – 15410
Helixi160 – 1634
Turni181 – 1833
Turni185 – 1873
Helixi197 – 21418
Beta strandi225 – 2306
Helixi232 – 2354
Helixi237 – 2404
Helixi243 – 2486
Beta strandi254 – 2607
Beta strandi262 – 2643
Beta strandi265 – 2695
Helixi275 – 28511
Beta strandi289 – 2935
Helixi299 – 3057
Helixi310 – 3178
Helixi320 – 3267
Helixi331 – 3377
Beta strandi339 – 3424
Helixi343 – 3464
Turni347 – 3515
Helixi354 – 3585
Helixi363 – 3653
Helixi367 – 37913
Beta strandi385 – 3906
Turni393 – 3964
Turni398 – 4003
Turni401 – 4033
Helixi407 – 4093
Helixi416 – 4249
Helixi431 – 4344
Helixi447 – 45812
Helixi479 – 4824
Helixi483 – 4864
Helixi495 – 50612
Turni510 – 5156
Beta strandi516 – 5227
Helixi525 – 5273
Helixi530 – 5367
Turni549 – 5524
Beta strandi553 – 5553
Beta strandi565 – 5673
Helixi572 – 58312
Helixi585 – 5884
Beta strandi594 – 6007
Helixi601 – 6033
Helixi605 – 61713
Beta strandi623 – 6286
Turni631 – 6333
Turni635 – 6373
Turni639 – 6413
Helixi646 – 6505
Beta strandi656 – 6594
Helixi664 – 67916
Beta strandi687 – 6915
Turni704 – 7063
Helixi707 – 7126
Beta strandi715 – 7206
Beta strandi723 – 7319
Helixi733 – 7353
Helixi736 – 75015
Beta strandi752 – 7587
Helixi762 – 77817
Helixi788 – 7925
Beta strandi798 – 8014
Helixi807 – 8104
Helixi811 – 8155
Beta strandi817 – 8193
Beta strandi821 – 8244
Helixi835 – 8417
Helixi846 – 85914
Beta strandi861 – 8633
Helixi865 – 87410
Turni884 – 8863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0AFG8.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2609.
HOGENOMiHOG000115215.
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

MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN    50
VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK 100
DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA 150
RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI 200
GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK 250
LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 300
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA 350
DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA 400
AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT 450
YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV 500
RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD 550
REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 600
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS 650
LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP 700
AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY 750
GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA 800
STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV 850
VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA 887
Length:887
Mass (Da):99,668
Last modified:January 23, 2007 - v2
Checksum:i7FB3811DE11BDD02
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461P → R in CAA24740. 1 Publication
Sequence conflicti276 – 2761Missing in CAA24740. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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.
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: July 9, 2014
This is version 97 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

Similar proteinsi