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Reviewed, UniProtKB/Swiss-Prot P0AFG8 (ODP1_ECOLI)

Last modified November 3, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1
Gene names
Name: aceE
Ordered Locus Names: b0114, JW0110
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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).

Catalytic activity

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

Cofactor

Magnesium.

Thiamine pyrophosphate.

Subunit structure

Homodimer.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 887886Pyruvate dehydrogenase E1 component
PRO_0000162243

Sites

Metal binding2311Magnesium
Metal binding2611Magnesium
Metal binding2631Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue7161N6-acetyllysine Ref.7

Experimental info

Sequence conflict1461P → R Ref.1
Sequence conflict1461P → R Ref.2
Sequence conflict2761Missing Ref.1
Sequence conflict2761Missing Ref.2

Secondary structure

1 ............................................................................................................................................ 887
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P0AFG8-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7FB3811DE11BDD02

FASTA88799,668
        10         20         30         40         50         60 
MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY 

        70         80         90        100        110        120 
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV 

       130        140        150        160        170        180 
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH 

       190        200        210        220        230        240 
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK 

       250        260        270        280        290        300 
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD 

       310        320        330        340        350        360 
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL 

       370        380        390        400        410        420 
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH 

       430        440        450        460        470        480 
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ 

       490        500        510        520        530        540 
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS 

       550        560        570        580        590        600 
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY 

       610        620        630        640        650        660 
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD 

       670        680        690        700        710        720 
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI 

       730        740        750        760        770        780 
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP 

       790        800        810        820        830        840 
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH 

       850        860        870        880 
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA

« Hide

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References

« Hide 'large scale' references
[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: 6343085] [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: 8202364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 8262214] [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: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[7]"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: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, MASS SPECTROMETRY.
[8]"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: 11955070] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

V01498 Genomic DNA. Translation: CAA24740.1.
U00096 Genomic DNA. Translation: AAC73225.1.
AP009048 Genomic DNA. Translation: BAB96684.2.
S67363 Genomic DNA. Translation: AAB29357.1.
PIRDEECPV. B64734.
RefSeqAP_000775.1.
NP_414656.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1L8AX-ray1.85A/B2-887[»]
1RP7X-ray2.09A/B1-887[»]
2G25X-ray2.10A/B2-886[»]
2G28X-ray1.85A/B2-886[»]
2G67X-ray2.32A/B2-886[»]
2IEAX-ray1.85A/B2-887[»]
2QTAX-ray1.85A/B2-887[»]
2QTCX-ray1.77A/B2-887[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0AFG8. 103 interactions.
STRINGP0AFG8.

2-D gel databases

SWISS-2DPAGEP0AFG8.
2DBase-EcoliP0AFG8.
ECO2DBASEF099.0. 6TH EDITION.

Proteomic databases

PRIDEP0AFG8.

Genome annotation databases

GeneID944834.
GenomeReviewsGene locus JW0110 in contig AP009048_GR.
Gene locus b0114 in contig U00096_GR.
KEGGecj:JW0110.
eco:b0114.

Organism-specific databases

EchoBASEEB0023.
EcoGeneEG10024. aceE.
CMRSearch...

Phylogenomic databases

HOGENOMP0AFG8.
OMAREISTTQ.

Enzyme and pathway databases

BioCycEcoCyc:E1P-MON.
MetaCyc:E1P-MON.

Gene expression databases

GenevestigatorP0AFG8.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF00456. Transketolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameODP1_ECOLI
AccessionPrimary (citable) accession number: P0AFG8
Secondary accession number(s): P06958, P78049, Q53382
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents