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P0A6P9

- ENO_ECOLI

UniProt

P0A6P9 - ENO_ECOLI

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Protein
Enolase
Gene
eno, b2779, JW2750
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.1 Publication

Cofactori

Magnesium. Required for catalysis and for stabilizing the dimer.2 Publications

Enzyme regulationi

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. Inhibited by fluoride ion.2 Publications

pH dependencei

Optimum pH is 8.1.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sitei120 – 1201Interaction with RNase E
Binding sitei159 – 1591Substrate By similarity
Binding sitei168 – 1681Substrate By similarity
Active sitei209 – 2091Proton donor By similarity
Metal bindingi246 – 2461Magnesium
Metal bindingi290 – 2901Magnesium
Binding sitei290 – 2901Substrate By similarity
Metal bindingi317 – 3171Magnesium
Binding sitei317 – 3171Substrate By similarity
Active sitei342 – 3421Proton acceptor By similarity
Binding sitei342 – 3421Substrate (covalent); in inhibited form
Sitei376 – 3761Interaction with RNase E
Binding sitei393 – 3931Substrate By similarity
Sitei408 – 4081Interaction with RNase E

GO - Molecular functioni

  1. identical protein bindingInferred from physical interactioni PubMed 15236960PubMed 16858726 Source: IntAct
  2. magnesium ion bindingInferred from direct assayi PubMed 16516921 Source: EcoliWiki
  3. phosphopyruvate hydratase activityInferred from direct assayi PubMed 4942326 Source: EcoliWiki
  4. protein bindingInferred from physical interactioni PubMed 15236960PubMed 15690043PubMed 16139413PubMed 20729366 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. glycolytic processInferred from mutant phenotypei PubMed 410789 Source: EcoliWiki
  1. phosphopyruvate hydratase activityInferred from direct assayi PubMed 4942326 Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ENOLASE-MONOMER.
ECOL316407:JW2750-MONOMER.
MetaCyc:ENOLASE-MONOMER.
BRENDAi4.2.1.11. 2026.
SABIO-RKiP0A6P9.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene namesi
Name:eno
Ordered Locus Names:b2779, JW2750
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10258. eno.

Subcellular locationi

Cytoplasmcytoskeleton. 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 cell surface.3 Publications

GO - Cellular componenti

  1. cell surfaceInferred from electronic annotationi Source: UniProtKB-SubCell
  2. cytoskeletonInferred from electronic annotationi Source: UniProtKB-SubCell
  3. cytosolInferred from direct assayi PubMed 16858726 Source: UniProtKB
  4. extracellular regionInferred from electronic annotationi Source: UniProtKB-SubCell
  5. membraneInferred from direct assayi PubMed 16858726 Source: UniProtKB
  6. phosphopyruvate hydratase complexInferred from electronic annotationi Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Mutagenesisi168 – 1681E → Q: 5% activity; not secreted. 1 Publication
Mutagenesisi209 – 2091E → Q: 1% activity; not secreted. 1 Publication
Mutagenesisi342 – 3421K → A, Q or R: 1% activity; not secreted. 1 Publication
Mutagenesisi342 – 3421K → E: 94% activity; not secreted. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 432431EnolaseUniRule annotation
PRO_0000133882

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei257 – 2571N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated on serine residue(s).1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A6P9.
PRIDEiP0A6P9.

2D gel databases

SWISS-2DPAGEiP0A6P9.

PTM databases

PhosSiteiP010423.

Expressioni

Gene expression databases

GenevestigatoriP0A6P9.

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with the C-terminal region of the endoribonuclease RNase E. Homodimer.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-368855,EBI-368855
rneP2151315EBI-368855,EBI-549958

Protein-protein interaction databases

DIPiDIP-31847N.
IntActiP0A6P9. 31 interactions.
MINTiMINT-1230935.
STRINGi511145.b2779.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi3 – 1311
Beta strandi19 – 279
Beta strandi32 – 365
Beta strandi45 – 473
Helixi59 – 613
Helixi65 – 728
Helixi74 – 796
Helixi87 – 9812
Beta strandi100 – 1034
Turni104 – 1063
Helixi108 – 12518
Helixi130 – 1378
Beta strandi151 – 1555
Helixi157 – 1593
Beta strandi160 – 1634
Beta strandi166 – 1727
Helixi179 – 19921
Helixi219 – 23214
Turni238 – 2403
Beta strandi241 – 2466
Helixi249 – 2524
Beta strandi257 – 2593
Helixi261 – 2633
Beta strandi264 – 2685
Helixi270 – 28314
Beta strandi286 – 2916
Helixi298 – 30811
Turni309 – 3113
Beta strandi312 – 3176
Turni318 – 3225
Helixi324 – 3329
Beta strandi337 – 3415
Helixi343 – 3453
Helixi349 – 36113
Beta strandi365 – 3695
Helixi379 – 3868
Beta strandi390 – 3934
Helixi400 – 41617
Helixi417 – 4193
Helixi424 – 4274

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9IX-ray2.48A/B/C/D2-432[»]
2FYMX-ray1.60A/C/D/F2-432[»]
3H8AX-ray1.90A/B/C/D1-432[»]
ProteinModelPortaliP0A6P9.
SMRiP0A6P9. Positions 2-431.

Miscellaneous databases

EvolutionaryTraceiP0A6P9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Regioni5 – 3430Interaction with RNase EUniRule annotation
Regioni369 – 3724Substrate binding By similarity

Sequence similaritiesi

Belongs to the enolase family.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072173.
KOiK01689.
OMAiRSEIKGQ.
OrthoDBiEOG65J589.
PhylomeDBiP0A6P9.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6P9-1 [UniParc]FASTA

« Hide

MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE    50
LRDGDKSRFL GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT 100
ENKSKFGANA ILAVSLANAK AAAAAKGMPL YEHIAELNGT PGKYSMPVPM 150
MNIINGGEHA DNNVDIQEFM IQPVGAKTVK EAIRMGSEVF HHLAKVLKAK 200
GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD ITLAMDCAAS 250
EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG 300
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT 350
ETLAAIKMAK DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS 400
DRVAKYNQLI RIEEALGEKA PYNGRKEIKG QA 432
Length:432
Mass (Da):45,655
Last modified:January 23, 2007 - v2
Checksum:i0569036E87471B91
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti102 – 1021N → K in CAA57795. 1 Publication
Sequence conflicti102 – 1021N → K in AAA24486. 1 Publication
Sequence conflicti220 – 2201A → D in CAA57795. 1 Publication
Sequence conflicti339 – 3391I → Y in CAA57795. 1 Publication
Sequence conflicti421 – 43212PYNGR…IKGQA → RTTVVKRSKARHKTDFI in CAA57795. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82400 Genomic DNA. Translation: CAA57795.1.
U29580 Genomic DNA. Translation: AAA69289.1.
U00096 Genomic DNA. Translation: AAC75821.1.
AP009048 Genomic DNA. Translation: BAE76853.1.
M12843 mRNA. Translation: AAA24486.1.
PIRiNOEC. G65059.
RefSeqiNP_417259.1. NC_000913.3.
YP_490987.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75821; AAC75821; b2779.
BAE76853; BAE76853; BAE76853.
GeneIDi12933303.
945032.
KEGGiecj:Y75_p2716.
eco:b2779.
PATRICi32120974. VBIEscCol129921_2879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82400 Genomic DNA. Translation: CAA57795.1 .
U29580 Genomic DNA. Translation: AAA69289.1 .
U00096 Genomic DNA. Translation: AAC75821.1 .
AP009048 Genomic DNA. Translation: BAE76853.1 .
M12843 mRNA. Translation: AAA24486.1 .
PIRi NOEC. G65059.
RefSeqi NP_417259.1. NC_000913.3.
YP_490987.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E9I X-ray 2.48 A/B/C/D 2-432 [» ]
2FYM X-ray 1.60 A/C/D/F 2-432 [» ]
3H8A X-ray 1.90 A/B/C/D 1-432 [» ]
ProteinModelPortali P0A6P9.
SMRi P0A6P9. Positions 2-431.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-31847N.
IntActi P0A6P9. 31 interactions.
MINTi MINT-1230935.
STRINGi 511145.b2779.

PTM databases

PhosSitei P010423.

2D gel databases

SWISS-2DPAGEi P0A6P9.

Proteomic databases

PaxDbi P0A6P9.
PRIDEi P0A6P9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75821 ; AAC75821 ; b2779 .
BAE76853 ; BAE76853 ; BAE76853 .
GeneIDi 12933303.
945032.
KEGGi ecj:Y75_p2716.
eco:b2779.
PATRICi 32120974. VBIEscCol129921_2879.

Organism-specific databases

EchoBASEi EB0254.
EcoGenei EG10258. eno.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072173.
KOi K01689.
OMAi RSEIKGQ.
OrthoDBi EOG65J589.
PhylomeDBi P0A6P9.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci EcoCyc:ENOLASE-MONOMER.
ECOL316407:JW2750-MONOMER.
MetaCyc:ENOLASE-MONOMER.
BRENDAi 4.2.1.11. 2026.
SABIO-RKi P0A6P9.

Miscellaneous databases

EvolutionaryTracei P0A6P9.
PROi P0A6P9.

Gene expression databases

Genevestigatori P0A6P9.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. Klein M., Freudl R.
    Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / JM109 / ATCC 53323.
  2. "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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase."
    Weng M., Makaroff C.A., Zalkin H.
    J. Biol. Chem. 261:5568-5574(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
  5. "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome."
    Py B., Higgins C.F., Krisch H.M., Carpousis A.J.
    Nature 381:169-172(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, SUBUNIT.
  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. "Protein identification with N and C-terminal sequence tags in proteome projects."
    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.
    J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "The purification and characterization of Escherichia coli enolase."
    Spring T.G., Wold F.
    J. Biol. Chem. 246:6797-6802(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: B.
  9. "Phosphorylation of Escherichia coli enolase."
    Dannelly H.K., Duclos B., Cozzone A.J., Reeves H.C.
    Biochimie 71:1095-1100(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY CHARACTERIZATION, PHOSPHORYLATION.
    Strain: K12 / JA200.
  10. "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.
  11. "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome."
    Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C., Krisch H.M., Carpousis A.J.
    Genes Dev. 12:2770-2781(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNASE E.
  12. "Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?"
    Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S., Giard J.-C., Hartke A., Auffray Y., Deutscher J.
    J. Mol. Biol. 337:485-496(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE BINDING AT LYS-342, ENZYME REGULATION, SECRETION OF SUBSTRATE-BOUND ENOLASE, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-168; GLU-209 AND LYS-342.
  13. "Global analysis of Escherichia coli RNA degradosome function using DNA microarrays."
    Bernstein J.A., Lin P.-H., Cohen S.N., Lin-Chao S.
    Proc. Natl. Acad. Sci. U.S.A. 101:2758-2763(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA TURNOVER.
  14. "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."
    Morita T., Kawamoto H., Mizota T., Inada T., Aiba H.
    Mol. Microbiol. 54:1063-1075(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE DECAY OF GLUCOSE TRANSPORTER MRNA.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  15. "RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton."
    Taghbalout A., Rothfield L.
    Proc. Natl. Acad. Sci. U.S.A. 104:1667-1672(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: PB103.
  16. "RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome."
    Taghbalout A., Rothfield L.
    J. Biol. Chem. 283:13850-13855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNASE E, SUBCELLULAR LOCATION.
  17. "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-257, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  18. "Crystal structure of the Escherichia coli RNA degradosome component enolase."
    Kuhnel K., Luisi B.F.
    J. Mol. Biol. 313:583-592(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.
  19. "Recognition of enolase in the Escherichia coli RNA degradosome."
    Chandran V., Luisi B.F.
    J. Mol. Biol. 358:8-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E AND MAGNESIUM IONS, SUBUNIT.
  20. "Molecular recognition between Escherichia coli enolase and ribonuclease E."
    Nurmohamed S., McKay A.R., Robinson C.V., Luisi B.F.
    Acta Crystallogr. D 66:1036-1040(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

Entry nameiENO_ECOLI
AccessioniPrimary (citable) accession number: P0A6P9
Secondary accession number(s): P08324, Q2MA53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 96 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

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