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UniProtKB/Swiss-Prot entry P0AFG8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODP1_ECOLI
Primary accession number P0AFG8
Secondary accession numbers P06958 P78049 Q53382
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 40)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
OrderedLocusNames: b0114, JW0110
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6343085 [NCBI, ExPASy, EBI, Israel, Japan]
Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.;
"The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component.";
Eur. J. Biochem. 133:155-162(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/nar/22.9.1637; PubMed=8202364 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 145 AND 275.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
STRAIN=K12;
DOI=10.1016/0014-5793(93)81605-Y; PubMed=8262214 [NCBI, ExPASy, EBI, Israel, Japan]
Haydon D.J., Quail M.A., Guest J.R.;
"A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene.";
FEBS Lett. 336:43-47(1993).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
[8]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
DOI=10.1021/bi0118557; PubMed=11955070 [NCBI, ExPASy, EBI, Israel, Japan]
Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., Jordan F., Guest J.R., Furey W.;
"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution.";
Biochemistry 41:5213-5221(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01498; CAA24740.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73225.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96684.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S67363; AAB29357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64734; DEECPV.
RefSeq AP_000775.1; -.
NP_414656.1; -.
3D structure databases
PDB
1L8A; X-ray; 1.85 A; A/B=1-887.[ExPASy / RCSB / EBI]
1RP7; X-ray; 2.09 A; A/B=1-887.[ExPASy / RCSB / EBI]
2G25; X-ray; 2.10 A; A/B=1-887.[ExPASy / RCSB / EBI]
2G28; X-ray; 1.85 A; A/B=1-887.[ExPASy / RCSB / EBI]
2G67; X-ray; 2.32 A; A/B=1-887.[ExPASy / RCSB / EBI]
2IEA; X-ray; 1.85 A; A/B=2-887.[ExPASy / RCSB / EBI]
2QTA; X-ray; 1.85 A; A/B=2-887.[ExPASy / RCSB / EBI]
2QTC; X-ray; 1.77 A; A/B=2-887.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1L8A; -.
1RP7; -.
2G25; -.
2G28; -.
2G67; -.
2IEA; -.
2QTA; -.
2QTC; -.
ModBase P0AFG8.
Protein-protein interaction databases
IntAct P0AFG8; -.
Enzyme and pathway databases
BioCyc EcoCyc:E1P-MON; -.
MetaCyc:E1P-MON; -.
2D gel databases
SWISS-2DPAGE P0AFG8; -.
2DBase-Ecoli P0AFG8; -.
ECO2DBASE F099.0; 6TH EDITION.
Organism-specific databases
EchoBASE EB0023; -.
EcoGene EG10024; aceE.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR004660; 2-oxoA_DHase_E1.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF00456; Transketolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
BLOCKS P0AFG8.
ProtoNet P0AFG8.
Genome annotation databases
GeneID 944834; -.
GenomeReviews U00096_GR; b0114.
AP009048_GR; JW0110.
KEGG ecj:JW0110; -.
eco:b0114; -.
Phylogenomic databases
HOGENOM P0AFG8; -.
Genome annotation databases
CMR P0AFG8; b0114.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Magnesium; Metal-binding; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   887  886     Pyruvate dehydrogenase E1 component. PRO_0000162243
METAL   231   231        Magnesium. 
METAL   261   261        Magnesium. 
METAL   263   263        Magnesium; via carbonyl oxygen. 
MOD_RES   716   716        N6-acetyllysine. 
CONFLICT   146   146        P -> R (in Ref. 1 and 2). 
CONFLICT   276   276        Missing (in Ref. 1 and 2). 
HELIX   66    68  3      
HELIX   76    99  24      
HELIX   109   124  16      
STRAND   131   133  3      
STRAND   137   139  3      
HELIX   142   144  3      
HELIX   145   154  10      
HELIX   160   163  4      
TURN   181   183  3      
TURN   185   187  3      
HELIX   197   214  18      
STRAND   225   230  6      
HELIX   232   235  4      
HELIX   237   240  4      
HELIX   243   248  6      
STRAND   254   260  7      
STRAND   262   264  3      
STRAND   267   269  3      
HELIX   275   285  11      
STRAND   289   293  5      
HELIX   299   305  7      
HELIX   310   317  8      
HELIX   320   327  8      
HELIX   331   337  7      
HELIX   339   341  3      
HELIX   343   346  4      
TURN   347   351  5      
HELIX   354   358  5      
HELIX   363   365  3      
HELIX   367   379  13      
STRAND   385   390  6      
TURN   393   396  4      
HELIX   416   424  9      
TURN   431   433  3      
HELIX   434   436  3      
HELIX   447   457  11      
TURN   458   460  3      
HELIX   479   482  4      
HELIX   483   486  4      
HELIX   495   506  12      
TURN   510   512  3      
HELIX   513   515  3      
STRAND   516   522  7      
HELIX   525   527  3      
HELIX   530   536  7      
STRAND   565   567  3      
HELIX   572   583  12      
HELIX   585   588  4      
STRAND   594   600  7      
HELIX   601   603  3      
HELIX   605   617  13      
STRAND   623   628  6      
TURN   631   633  3      
TURN   635   637  3      
TURN   639   641  3      
HELIX   646   650  5      
STRAND   656   659  4      
HELIX   664   679  16      
STRAND   687   691  5      
TURN   704   706  3      
HELIX   707   712  6      
STRAND   715   731  17      
HELIX   733   735  3      
HELIX   736   750  15      
STRAND   752   758  7      
HELIX   762   778  17      
HELIX   788   792  5      
STRAND   798   801  4      
HELIX   807   810  4      
HELIX   811   815  5      
STRAND   821   824  4      
HELIX   835   841  7      
HELIX   846   859  14      
HELIX   865   874  10      
TURN   884   886  3      
Sequence information
Length: 887 AA [This is the length of the unprocessed precursor] Molecular weight: 99668 Da [This is the MW of the unprocessed precursor] CRC64: 7FB3811DE11BDD02 [This is a checksum on the sequence]
        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 

P0AFG8 in FASTA format

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