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UniProtKB/Swiss-Prot entry P0A6P9


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

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Entry information
Entry name ENO_ECOLI
Primary accession number P0A6P9
Secondary accession numbers P08324 Q2MA53
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 43)
Name and origin of the protein
Protein name Enolase
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase
2-phospho-D-glycerate hydro-lyase
Gene name
Name: eno
OrderedLocusNames: b2779, JW2750
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 / JM109 / ATCC 53323;
Klein M., Freudl R.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
PubMed=3514618 [NCBI, ExPASy, EBI, Israel, Japan]
Weng M., Makaroff C.A., Zalkin H.;
"Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase.";
J. Biol. Chem. 261:5568-5574(1986).
[5]
PROTEIN SEQUENCE OF 2-16, AND FUNCTION IN DEGRADOSOME.
DOI=10.1038/381169a0; PubMed=8610017 [NCBI, ExPASy, EBI, Israel, Japan]
Py B., Higgins C.F., Krisch H.M., Carpousis A.J.;
"A DEAD-box RNA helicase in the Escherichia coli RNA degradosome.";
Nature 381:169-172(1996).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
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]
PROTEIN SEQUENCE OF 2-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1006/jmbi.1998.1726; PubMed=9600841 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[8]
PRELIMINARY CHARACTERIZATION, AND PHOSPHORYLATION.
STRAIN=K12 / JA200;
DOI=10.1016/0300-9084(89)90116-8; PubMed=2513001 [NCBI, ExPASy, EBI, Israel, Japan]
Dannelly H.K., Duclos B., Cozzone A.J., Reeves H.C.;
"Phosphorylation of Escherichia coli enolase.";
Biochimie 71:1095-1100(1989).
[9]
SUBSTRATE BINDING AT LYS-342, INACTIVATION, SECRETION OF SUBSTRATE-BOUND ENOLASE, AND MUTAGENESIS OF GLU-168; GLU-209 AND LYS-342.
DOI=10.1016/j.jmb.2003.12.082; PubMed=15003462 [NCBI, ExPASy, EBI, Israel, Japan]
Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S., Giard J.-C., Hartke A., Auffray Y., Deutscher J.;
"Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?";
J. Mol. Biol. 337:485-496(2004).
[10]
ROLE IN MRNA TURNOVER.
DOI=10.1073/pnas.0308747101; PubMed=14981237 [NCBI, ExPASy, EBI, Israel, Japan]
Bernstein J.A., Lin P.-H., Cohen S.N., Lin-Chao S.;
"Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.";
Proc. Natl. Acad. Sci. U.S.A. 101:2758-2763(2004).
[11]
ROLE IN THE DECAY OF GLUCOSE TRANSPORTER MRNA.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1111/j.1365-2958.2004.04329.x; PubMed=15522087 [NCBI, ExPASy, EBI, Israel, Japan]
Morita T., Kawamoto H., Mizota T., Inada T., Aiba H.;
"Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli.";
Mol. Microbiol. 54:1063-1075(2004).
[12]
SUBCELLULAR LOCATION.
STRAIN=PB103;
DOI=10.1073/pnas.0610491104; PubMed=17242352 [NCBI, ExPASy, EBI, Israel, Japan]
Taghbalout A., Rothfield L.;
"RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 104:1667-1672(2007).
[13]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND SUBUNIT.
DOI=10.1006/jmbi.2001.5065; PubMed=11676541 [NCBI, ExPASy, EBI, Israel, Japan]
Kuhnel K., Luisi B.F.;
"Crystal structure of the Escherichia coli RNA degradosome component enolase.";
J. Mol. Biol. 313:583-592(2001).
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E.
DOI=10.1016/j.jmb.2006.02.012; PubMed=16516921 [NCBI, ExPASy, EBI, Israel, Japan]
Chandran V., Luisi B.F.;
"Recognition of enolase in the Escherichia coli RNA degradosome.";
J. Mol. Biol. 358:8-15(2006).
Comments
  • FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.
  • CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
  • ENZYME REGULATION: The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
  • PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
  • SUBUNIT: Homodimer. Interacts with the C-terminal region of the endoribonuclease RNase E in the RNA degradosome.
  • INTERACTION:
    Self; NbExp=1; IntAct=EBI-368855, EBI-368855;
    P21513:rne; NbExp=1; IntAct=EBI-368855, EBI-549958;
  • SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Secreted. Cell surface. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the bacterial cell surface.
  • PTM: Phosphorylated on serine residue(s).
  • SIMILARITY: Belongs to the enolase family.
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
X82400; CAA57795.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U29580; AAA69289.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75821.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76853.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12843; AAA24486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G65059; NOEC.
RefSeq AP_003345.1; -.
NP_417259.1; -.
3D structure databases
PDB
1E9I; X-ray; 2.48 A; A/B/C/D=1-432.[ExPASy / RCSB / EBI]
2FYM; X-ray; 1.60 A; A/C/D/F=1-432.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9I; -.
2FYM; -.
ModBase P0A6P9.
Protein-protein interaction databases
IntAct P0A6P9; -.
PTM databases
PhosSite P0A6P9; -.
Enzyme and pathway databases
BioCyc EcoCyc:ENOLASE-MON; -.
MetaCyc:ENOLASE-MON; -.
2D gel databases
SWISS-2DPAGE P0A6P9; -.
2DBase-Ecoli P0A6P9; -.
ECO2DBASE F043.8; 6TH EDITION.
Organism-specific databases
EchoBASE EB0254; -.
EcoGene EG10258; eno.
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:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_00318; -; 1.
PBIL [Tree]
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS P0A6P9.
Genome annotation databases
GeneID 945032; -.
GenomeReviews U00096_GR; b2779.
AP009048_GR; JW2750.
KEGG ecj:JW2750; -.
eco:b2779; -.
Phylogenomic databases
HOGENOM P0A6P9; -.
Genome annotation databases
CMR P0A6P9; b2779.
Other
ProtoNet P0A6P9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   432  431     Enolase. PRO_0000133882
REGION   369   372  4     Substrate binding (By similarity). 
ACT_SITE   209   209        Proton donor (By similarity). 
ACT_SITE   342   342        Proton acceptor (By similarity). 
METAL   246   246        Magnesium. 
METAL   290   290        Magnesium. 
METAL   317   317        Magnesium. 
BINDING   159   159        Substrate (By similarity). 
BINDING   168   168        Substrate (By similarity). 
BINDING   290   290        Substrate (By similarity). 
BINDING   317   317        Substrate (By similarity). 
BINDING   342   342        Substrate (covalent); in inhibited form. 
BINDING   393   393        Substrate (By similarity). 
SITE   34    34  1     Interaction with RNase E. 
SITE   120   120  1     Interaction with RNase E. 
SITE   376   376  1     Interaction with RNase E. 
SITE   408   408  1     Interaction with RNase E. 
MOD_RES   284   284        Phosphotyrosine (By similarity). 
MUTAGEN   168   168        E->Q: 5% activity; not secreted. 
MUTAGEN   209   209        E->Q: 1% activity; not secreted. 
MUTAGEN   342   342        K->A,Q,R: 1% activity; not secreted. 
MUTAGEN   342   342        K->E: 94% activity; not secreted. 
CONFLICT   102   102        N -> K (in Ref. 1; CAA57795/AAA24486). 
CONFLICT   220   220        A -> D (in Ref. 1; CAA57795). 
CONFLICT   339   339        I -> Y (in Ref. 1; CAA57795). 
CONFLICT   421   432        PYNGRKEIKGQA -> RTTVVKRSKARHKTDFI (in Ref. 1; CAA57795). 
STRAND   3     7  5      
STRAND   10    13  4      
STRAND   19    27  9      
STRAND   32    36  5      
STRAND   45    47  3      
HELIX   59    61  3      
HELIX   65    72  8      
HELIX   74    79  6      
HELIX   87    98  12      
STRAND   100   102  3      
HELIX   108   125  18      
HELIX   130   138  9      
STRAND   151   155  5      
HELIX   157   159  3      
STRAND   160   163  4      
STRAND   166   172  7      
HELIX   179   199  21      
HELIX   219   232  14      
TURN   238   240  3      
STRAND   241   246  6      
HELIX   249   252  4      
STRAND   257   260  4      
HELIX   261   263  3      
STRAND   264   268  5      
HELIX   270   283  14      
STRAND   286   291  6      
HELIX   298   308  11      
TURN   309   311  3      
STRAND   312   317  6      
TURN   318   322  5      
HELIX   324   332  9      
STRAND   337   341  5      
TURN   343   346  4      
HELIX   349   362  14      
STRAND   365   369  5      
HELIX   379   386  8      
STRAND   390   393  4      
HELIX   400   416  17      
HELIX   417   419  3      
HELIX   424   427  4      
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 45655 Da [This is the MW of the unprocessed precursor] CRC64: 0569036E87471B91 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL 

        70         80         90        100        110        120 
GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT ENKSKFGANA ILAVSLANAK 

       130        140        150        160        170        180 
AAAAAKGMPL YEHIAELNGT PGKYSMPVPM MNIINGGEHA DNNVDIQEFM IQPVGAKTVK 

       190        200        210        220        230        240 
EAIRMGSEVF HHLAKVLKAK GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD 

       250        260        270        280        290        300 
ITLAMDCAAS EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG 

       310        320        330        340        350        360 
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT ETLAAIKMAK 

       370        380        390        400        410        420 
DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS DRVAKYNQLI RIEEALGEKA 

       430 
PYNGRKEIKG QA 

P0A6P9 in FASTA format

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