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P0A6P9

- ENO_ECOLI

UniProt

P0A6P9 - ENO_ECOLI

Protein

Enolase

Gene

eno

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 PublicationsUniRule annotation

    Catalytic activityi

    2-phospho-D-glycerate = phosphoenolpyruvate + H2O.1 PublicationUniRule annotation

    Cofactori

    Magnesium. Required for catalysis and for stabilizing the dimer.2 PublicationsUniRule annotation

    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 identifierActions
    Sitei120 – 1201Interaction with RNase E
    Binding sitei159 – 1591SubstrateUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Active sitei209 – 2091Proton donorUniRule annotation
    Metal bindingi246 – 2461Magnesium
    Metal bindingi290 – 2901Magnesium
    Binding sitei290 – 2901SubstrateUniRule annotation
    Metal bindingi317 – 3171Magnesium
    Binding sitei317 – 3171SubstrateUniRule annotation
    Active sitei342 – 3421Proton acceptorUniRule annotation
    Binding sitei342 – 3421Substrate (covalent); in inhibited form
    Sitei376 – 3761Interaction with RNase E
    Binding sitei393 – 3931SubstrateUniRule annotation
    Sitei408 – 4081Interaction with RNase E

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. magnesium ion binding Source: EcoliWiki
    3. phosphopyruvate hydratase activity Source: EcoliWiki
    4. protein binding Source: IntAct

    GO - Biological processi

    1. glycolytic process Source: EcoliWiki

    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-RKP0A6P9.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
    Alternative name(s):
    2-phospho-D-glycerate hydro-lyaseUniRule annotation
    2-phosphoglycerate dehydrataseUniRule annotation
    Gene namesi
    Name:enoUniRule annotation
    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.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. extracellular region Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. phosphopyruvate hydratase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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 identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 432431EnolasePRO_0000133882Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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-2DPAGEP0A6P9.

    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 PublicationsUniRule annotation

    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

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6P9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni5 – 3430Interaction with RNase EAdd
    BLAST
    Regioni369 – 3724Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the enolase family.UniRule annotation

    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]FASTAAdd to Basket

    « 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

    Experimental Info

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

    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.
    PIRiG65059. NOEC.
    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 G65059. NOEC.
    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...
    MobiDBi 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-2DPAGE 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-RK 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

    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. 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. 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. 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 informationi

    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: October 1, 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3