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P00924

- ENO1_YEAST

UniProt

P00924 - ENO1_YEAST

Protein

Enolase 1

Gene

ENO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Magnesium. Required for catalysis and for stabilizing the dimer.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei160 – 1601Substrate2 Publications
    Binding sitei169 – 1691Substrate2 Publications
    Active sitei212 – 2121Proton donorCurated
    Metal bindingi247 – 2471Magnesium1 Publication
    Metal bindingi296 – 2961Magnesium1 Publication
    Binding sitei296 – 2961Substrate2 Publications
    Metal bindingi321 – 3211Magnesium1 Publication
    Binding sitei321 – 3211Substrate2 Publications
    Active sitei346 – 3461Proton acceptor
    Binding sitei397 – 3971Substrate2 Publications

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphopyruvate hydratase activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. gluconeogenesis Source: SGD
    2. glycolytic process Source: SGD
    3. regulation of vacuole fusion, non-autophagic Source: SGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YGR254W-MONOMER.
    BRENDAi4.2.1.11. 984.
    SABIO-RKP00924.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enolase 1 (EC:4.2.1.11)
    Alternative name(s):
    2-phospho-D-glycerate hydro-lyase 1
    2-phosphoglycerate dehydratase 1
    Gene namesi
    Name:ENO1
    Synonyms:ENOA, HSP48
    Ordered Locus Names:YGR254W
    ORF Names:G9160
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000003486. ENO1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. fungal-type vacuole Source: SGD
    2. mitochondrion Source: SGD
    3. phosphopyruvate hydratase complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401S → A: Reduces activity by 99.9%.
    Mutagenesisi160 – 1601H → A, F or N: Reduces activity by 99%. 2 Publications
    Mutagenesisi169 – 1691E → Q: Reduces Kcat over 100000-fold.
    Mutagenesisi208 – 2081N → A: Reduces activity by 44%. 1 Publication
    Mutagenesisi212 – 2121E → Q: Reduces Kcat over 100000-fold.
    Mutagenesisi346 – 3461K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. 1 Publication

    Protein family/group databases

    Allergomei786. Sac c Enolase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 437436Enolase 1PRO_0000134062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191Phosphoserine1 Publication
    Modified residuei138 – 1381PhosphoserineBy similarity
    Modified residuei188 – 1881PhosphoserineBy similarity
    Modified residuei313 – 3131PhosphothreonineBy similarity
    Modified residuei324 – 3241PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP00924.
    PeptideAtlasiP00924.
    PRIDEiP00924.

    2D gel databases

    COMPLUYEAST-2DPAGEP00924.
    SWISS-2DPAGEP00924.
    UCD-2DPAGEP00924.

    Expressioni

    Gene expression databases

    GenevestigatoriP00924.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKC1P245832EBI-6468,EBI-9860

    Protein-protein interaction databases

    BioGridi33505. 57 interactions.
    DIPiDIP-5561N.
    IntActiP00924. 18 interactions.
    MINTiMINT-574648.
    STRINGi4932.YGR254W.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Beta strandi18 – 269
    Beta strandi29 – 346
    Beta strandi43 – 453
    Helixi57 – 593
    Helixi63 – 719
    Helixi73 – 808
    Helixi87 – 9812
    Beta strandi100 – 1023
    Turni104 – 1063
    Helixi108 – 12518
    Helixi130 – 1389
    Beta strandi145 – 1473
    Beta strandi152 – 1565
    Helixi158 – 1603
    Beta strandi161 – 1644
    Beta strandi169 – 1735
    Helixi180 – 20223
    Helixi204 – 2074
    Beta strandi213 – 2153
    Helixi222 – 23615
    Turni239 – 2413
    Beta strandi243 – 2475
    Helixi250 – 2534
    Turni261 – 2644
    Helixi270 – 2723
    Helixi276 – 28914
    Beta strandi292 – 2965
    Helixi304 – 3118
    Turni312 – 3143
    Beta strandi316 – 3216
    Turni322 – 3265
    Helixi328 – 3369
    Beta strandi341 – 3455
    Helixi347 – 3504
    Helixi353 – 36513
    Beta strandi369 – 3735
    Helixi383 – 3908
    Beta strandi394 – 3974
    Helixi404 – 42017
    Helixi421 – 4233
    Beta strandi424 – 4263
    Helixi428 – 4303
    Helixi434 – 4363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EBGX-ray2.10A/B2-437[»]
    1EBHX-ray1.90A/B2-437[»]
    1ELSX-ray2.40A2-437[»]
    1L8PX-ray2.10A/B/C/D2-437[»]
    1NELX-ray2.60A2-437[»]
    1ONEX-ray1.80A/B2-437[»]
    1P43X-ray1.80A/B2-437[»]
    1P48X-ray2.00A/B2-437[»]
    2AL1X-ray1.50A/B2-437[»]
    2AL2X-ray1.85A/B2-437[»]
    2ONEX-ray2.00A/B2-437[»]
    2XGZX-ray1.80A/B2-437[»]
    2XH0X-ray1.70A/B/C/D2-437[»]
    2XH2X-ray1.80A/B/C/D2-437[»]
    2XH4X-ray1.70A/B/C/D2-437[»]
    2XH7X-ray1.80A/B2-437[»]
    3ENLX-ray2.25A2-437[»]
    4ENLX-ray1.90A2-437[»]
    5ENLX-ray2.20A2-437[»]
    6ENLX-ray2.20A2-437[»]
    7ENLX-ray2.20A2-437[»]
    ProteinModelPortaliP00924.
    SMRiP00924. Positions 2-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00924.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni373 – 3764Substrate binding

    Sequence similaritiesi

    Belongs to the enolase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00550000074560.
    HOGENOMiHOG000072174.
    KOiK01689.
    OMAiTHARELP.
    OrthoDBiEOG7JHMFP.

    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.

    P00924-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR    50
    DGDKSKWMGK GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT 100
    ANKSKLGANA ILGVSLAASR AAAAEKNVPL YKHLADLSKS KTSPYVLPVP 150
    FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEALRIGSEV YHNLKSLTKK 200
    RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KIKIGLDCAS 250
    SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA 300
    EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI 350
    GTLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA 400
    PARSERLAKL NQLLRIEEEL GDNAVFAGEN FHHGDKL 437
    Length:437
    Mass (Da):46,816
    Last modified:October 5, 2010 - v3
    Checksum:i69F45214DBD375BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421I → V in AAA88712. (PubMed:6256394)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01322 Genomic DNA. Translation: AAA88712.1.
    X99228 Genomic DNA. Translation: CAA67616.1.
    Z73039 Genomic DNA. Translation: CAA97283.1.
    BK006941 Genomic DNA. Translation: DAA08345.1.
    PIRiS64586. NOBY.
    RefSeqiNP_011770.3. NM_001181383.3.

    Genome annotation databases

    EnsemblFungiiYGR254W; YGR254W; YGR254W.
    GeneIDi853169.
    KEGGisce:YGR254W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01322 Genomic DNA. Translation: AAA88712.1 .
    X99228 Genomic DNA. Translation: CAA67616.1 .
    Z73039 Genomic DNA. Translation: CAA97283.1 .
    BK006941 Genomic DNA. Translation: DAA08345.1 .
    PIRi S64586. NOBY.
    RefSeqi NP_011770.3. NM_001181383.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EBG X-ray 2.10 A/B 2-437 [» ]
    1EBH X-ray 1.90 A/B 2-437 [» ]
    1ELS X-ray 2.40 A 2-437 [» ]
    1L8P X-ray 2.10 A/B/C/D 2-437 [» ]
    1NEL X-ray 2.60 A 2-437 [» ]
    1ONE X-ray 1.80 A/B 2-437 [» ]
    1P43 X-ray 1.80 A/B 2-437 [» ]
    1P48 X-ray 2.00 A/B 2-437 [» ]
    2AL1 X-ray 1.50 A/B 2-437 [» ]
    2AL2 X-ray 1.85 A/B 2-437 [» ]
    2ONE X-ray 2.00 A/B 2-437 [» ]
    2XGZ X-ray 1.80 A/B 2-437 [» ]
    2XH0 X-ray 1.70 A/B/C/D 2-437 [» ]
    2XH2 X-ray 1.80 A/B/C/D 2-437 [» ]
    2XH4 X-ray 1.70 A/B/C/D 2-437 [» ]
    2XH7 X-ray 1.80 A/B 2-437 [» ]
    3ENL X-ray 2.25 A 2-437 [» ]
    4ENL X-ray 1.90 A 2-437 [» ]
    5ENL X-ray 2.20 A 2-437 [» ]
    6ENL X-ray 2.20 A 2-437 [» ]
    7ENL X-ray 2.20 A 2-437 [» ]
    ProteinModelPortali P00924.
    SMRi P00924. Positions 2-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33505. 57 interactions.
    DIPi DIP-5561N.
    IntActi P00924. 18 interactions.
    MINTi MINT-574648.
    STRINGi 4932.YGR254W.

    Protein family/group databases

    Allergomei 786. Sac c Enolase.

    2D gel databases

    COMPLUYEAST-2DPAGE P00924.
    SWISS-2DPAGE P00924.
    UCD-2DPAGE P00924.

    Proteomic databases

    MaxQBi P00924.
    PeptideAtlasi P00924.
    PRIDEi P00924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR254W ; YGR254W ; YGR254W .
    GeneIDi 853169.
    KEGGi sce:YGR254W.

    Organism-specific databases

    SGDi S000003486. ENO1.

    Phylogenomic databases

    GeneTreei ENSGT00550000074560.
    HOGENOMi HOG000072174.
    KOi K01689.
    OMAi THARELP.
    OrthoDBi EOG7JHMFP.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00187 .
    BioCyci YEAST:YGR254W-MONOMER.
    BRENDAi 4.2.1.11. 984.
    SABIO-RK P00924.

    Miscellaneous databases

    EvolutionaryTracei P00924.
    NextBioi 973288.

    Gene expression databases

    Genevestigatori P00924.

    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. "The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes."
      Holland M.J., Holland J.P., Thill G.P., Jackson K.A.
      J. Biol. Chem. 256:1385-1395(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
      Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
      Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The amino acid sequence of yeast enolase."
      Chin C.C.Q., Brewer J.M., Wold F.
      J. Biol. Chem. 256:1377-1384(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-437.
    6. Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: ATCC 26786 / X2180-1A.
    7. Cited for: PROTEIN SEQUENCE OF 30-47.
      Strain: ATCC 204508 / S288c.
    8. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
      Norbeck J., Blomberg A.
      Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 69-79.
      Strain: ATCC 38531 / Y41.
    9. "Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants."
      Poyner R.R., Laughlin L.T., Sowa G.A., Reed G.H.
      Biochemistry 35:1692-1699(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-346.
    10. "The H159A mutant of yeast enolase 1 has significant activity."
      Brewer J.M., Holland M.J., Lebioda L.
      Biochem. Biophys. Res. Commun. 276:1199-1202(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-160.
    11. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
      Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
      Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases."
      Brewer J.M., Glover C.V., Holland M.J., Lebioda L.
      J. Protein Chem. 22:353-361(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-160 AND ASN-208.
    13. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor."
      Lebioda L., Stec B.
      Nature 333:683-686(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    17. "The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology."
      Lebioda L., Stec B., Brewer J.M.
      J. Biol. Chem. 264:3685-3693(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    18. "Refined structure of yeast apo-enolase at 2.25-A resolution."
      Stec B., Lebioda L.
      J. Mol. Biol. 211:235-248(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    19. "A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8-A resolution."
      Larsen T.M., Wedekind J.E., Rayment I., Reed G.H.
      Biochemistry 35:4349-4358(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS.
    20. "Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0-A resolution."
      Zhang E., Brewer J.M., Minor W., Carreira L.A., Lebioda L.
      Biochemistry 36:12526-12534(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
    21. "Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase."
      Poyner R.R., Larsen T.M., Wong S.-W., Reed G.H.
      Arch. Biochem. Biophys. 401:155-163(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-40 IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE ANALOG.
    22. "Reverse protonation is the key to general acid-base catalysis in enolase."
      Sims P.A., Larsen T.M., Poyner R.R., Cleland W.W., Reed G.H.
      Biochemistry 42:8298-8306(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-212 AND MUTANT GLN-169.

    Entry informationi

    Entry nameiENO1_YEAST
    AccessioniPrimary (citable) accession number: P00924
    Secondary accession number(s): D6VV34, P99013
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 76700 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3