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P00924 (ENO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase 1

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
Gene names
Name:ENO1
Synonyms:ENOA, HSP48
Ordered Locus Names:YGR254W
ORF Names:G9160
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [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. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

Homodimer.

Subcellular location

Cytoplasm Ref.11.

Miscellaneous

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

Sequence similarities

Belongs to the enolase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKC1P245832EBI-6468,EBI-9860

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 437436Enolase 1 HAMAP-Rule MF_00318
PRO_0000134062

Regions

Region373 – 3764Substrate binding HAMAP-Rule MF_00318

Sites

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

Amino acid modifications

Modified residue1191Phosphoserine Ref.14
Modified residue1381Phosphoserine By similarity
Modified residue1881Phosphoserine By similarity
Modified residue3131Phosphothreonine By similarity
Modified residue3241Phosphothreonine By similarity

Experimental info

Mutagenesis401S → A: Reduces activity by 99.9%.
Mutagenesis1601H → A, F or N: Reduces activity by 99%. Ref.10 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.9
Sequence conflict2421I → V in AAA88712. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00924 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 69F45214DBD375BE

FASTA43746,816
        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 
KIKIGLDCAS 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] [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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]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.
[7]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01322 Genomic DNA. Translation: AAA88712.1.
X99228 Genomic DNA. Translation: CAA67616.1.
Z73039 Genomic DNA. Translation: CAA97283.1.
BK006941 Genomic DNA. Translation: DAA08345.1.
PIRNOBY. S64586.
RefSeqNP_011770.3. NM_001181383.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00924.
SMRP00924. Positions 2-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33505. 57 interactions.
DIPDIP-5561N.
IntActP00924. 18 interactions.
MINTMINT-574648.
STRING4932.YGR254W.

Protein family/group databases

Allergome786. Sac c Enolase.

2D gel databases

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

Proteomic databases

MaxQBP00924.
PeptideAtlasP00924.
PRIDEP00924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR254W; YGR254W; YGR254W.
GeneID853169.
KEGGsce:YGR254W.

Organism-specific databases

SGDS000003486. ENO1.

Phylogenomic databases

GeneTreeENSGT00550000074560.
HOGENOMHOG000072174.
KOK01689.
OMATHARELP.
OrthoDBEOG7JHMFP.

Enzyme and pathway databases

BioCycYEAST:YGR254W-MONOMER.
BRENDA4.2.1.11. 984.
SABIO-RKP00924.
UniPathwayUPA00109; UER00187.

Gene expression databases

GenevestigatorP00924.

Family and domain databases

Gene3D3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
SUPFAMSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00924.
NextBio973288.

Entry information

Entry nameENO1_YEAST
AccessionPrimary (citable) accession number: P00924
Secondary accession number(s): D6VV34, P99013
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways