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Reviewed, UniProtKB/Swiss-Prot P00924 (ENO1_YEAST)

Last modified June 16, 2009. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1
Gene names
Name: ENO1
Synonyms: ENOA, HSP48
Ordered Locus Names: YGR254W
ORF Names: G9160
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Ref.10

Miscellaneous

Present with 76700 molecules/cell in log phase SD medium. Ref.13

Sequence similarities

Belongs to the enolase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKC1P245831EBI-6468,EBI-9860

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 437436Enolase 1
PRO_0000134062

Regions

Region373 – 3764Substrate binding

Sites

Active site2121Proton donor Probable
Active site3461Proton acceptor
Metal binding2471Magnesium Ref.22
Metal binding2961Magnesium Ref.22
Metal binding3211Magnesium Ref.22
Binding site1601Substrate
Binding site1691Substrate
Binding site2961Substrate
Binding site3211Substrate
Binding site3971Substrate

Amino acid modifications

Modified residue101Phosphoserine Ref.11 Ref.14 Ref.16 Ref.18
Modified residue141Phosphoserine Ref.18
Modified residue371Phosphoserine Ref.18
Modified residue401Phosphoserine Ref.18
Modified residue411Phosphothreonine Ref.18
Modified residue961Phosphoserine Ref.18
Modified residue1041Phosphoserine Ref.18 Ref.17
Modified residue1191Phosphoserine Ref.16
Modified residue1431Phosphoserine Ref.18
Modified residue1881Phosphoserine Ref.14 Ref.18 Ref.17 Ref.15
Modified residue3241Phosphothreonine Ref.18
Modified residue4041Phosphoserine Ref.16 Ref.17

Experimental info

Mutagenesis401S → A: Reduces activity by 99.9%.
Mutagenesis1601H → A, F or N: Reduces activity by 99%. Ref.9 Ref.12
Mutagenesis1691E → Q: Reduces Kcat over 100000-fold.
Mutagenesis2081N → A: Reduces activity by 44%. Ref.12
Mutagenesis2121E → Q: Reduces Kcat over 100000-fold.
Mutagenesis3461K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. Ref.8
Sequence conflict2421V → I in CAA67616. Ref.2
Sequence conflict2421V → I in CAA97283. Ref.2

Secondary structure

............................................................................. 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00924-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5E874ABDFA495E17

FASTA43746,802
        10         20         30         40         50         60 
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK 

        70         80         90        100        110        120 
GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR 

       130        140        150        160        170        180 
AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF 

       190        200        210        220        230        240 
AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG 

       250        260        270        280        290        300 
KVKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA 

       310        320        330        340        350        360 
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA 

       370        380        390        400        410        420 
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 

       430 
GDNAVFAGEN FHHGDKL 

« Hide

References

« Hide 'large scale' references
[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: 6256394] [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: 9133741] [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. expand/collapse author list , 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: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"The amino acid sequence of yeast enolase."
Chin C.C.Q., Brewer J.M., Wold F.
J. Biol. Chem. 256:1377-1384(1981) [PubMed: 7005235] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-437.
[5]Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., Hughes G.J., Appel R.D., Deshusses J., Hochstrasser D.F.
Submitted (AUG-1995) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: ATCC 26786 / X2180-1A.
[6]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-47.
Strain: ATCC 204508 / S288c.
[7]"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: 7737086] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-79.
Strain: ATCC 38531 / Y41.
[8]"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: 8634301] [Abstract]
Cited for: MUTAGENESIS OF LYS-346.
[9]"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: 11027610] [Abstract]
Cited for: MUTAGENESIS OF HIS-160.
[10]"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: 11502169] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, MASS SPECTROMETRY.
[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: 13678299] [Abstract]
Cited for: MUTAGENESIS OF HIS-160 AND ASN-208.
[13]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-188, MASS SPECTROMETRY.
[15]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY.
[16]"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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-119 AND SER-404, MASS SPECTROMETRY.
[17]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-188 AND SER-404, MASS SPECTROMETRY.
[18]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-37; SER-40; THR-41; SER-96; SER-104; SER-143; SER-188 AND THR-324, MASS SPECTROMETRY.
[19]"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: 3374614] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[20]"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: 2645275] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[21]"Refined structure of yeast apo-enolase at 2.25-A resolution."
Stec B., Lebioda L.
J. Mol. Biol. 211:235-248(1990) [PubMed: 2405163] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[22]"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: 8605183] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS.
[23]"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: 9376357] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
[24]"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: 12054465] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-40 IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE ANALOG.
[25]"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: 12846578] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-212 AND MUTANT GLN-169.
+Additional computationally mapped references.

Cross-references

Sequence databases

J01322 Genomic DNA. Translation: AAA88712.1.
X99228 Genomic DNA. Translation: CAA67616.1.
Z73039 Genomic DNA. Translation: CAA97283.1.
PIRNOBY. S64586.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EBGX-ray2.10A/B2-436[»]
1EBHX-ray1.90A/B2-436[»]
1ELSX-ray2.40A2-436[»]
1L8PX-ray2.10A/B/C/D2-437[»]
1NELX-ray2.60A2-436[»]
1ONEX-ray1.80A/B2-437[»]
1P43X-ray1.80A/B2-437[»]
1P48X-ray2.00A/B2-437[»]
2AL1X-ray1.50A/B2-436[»]
2AL2X-ray1.85A/B1-437[»]
2ONEX-ray2.00A/B2-437[»]
3ENLX-ray2.25A2-437[»]
4ENLX-ray1.90A2-436[»]
5ENLX-ray2.20A2-436[»]
6ENLX-ray2.20A2-436[»]
7ENLX-ray2.20A2-436[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5561N.
IntActP00924. 29 interactions.

2-D gel databases

SWISS-2DPAGEP00924.
COMPLUYEAST-2DPAGEP00924.

Proteomic databases

PeptideAtlasP00924.
PRIDEP00924.

Genome annotation databases

EnsemblYGR254W. Saccharomyces cerevisiae. [Contig view]
GenomeReviewsGene locus YGR254W in contig Y13135_GR.
KEGGsce:YGR254W.

Organism-specific databases

CYGDYGR254w.
SGDS000003486. ENO1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP00924.

Enzyme and pathway databases

BRENDA4.2.1.11. 250.

Gene expression databases

ArrayExpressP00924.
GermOnlineYGR254W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000941. Enolase.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
ProDomPD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO1_YEAST
AccessionPrimary (citable) accession number: P00924
Secondary accession number(s): P99013
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents