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Protein

Enolase 1

Gene

ENO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
  4. Enolase 2 (ENO2), Enolase-related protein 2 (ERR2), Enolase-related protein 1 (ERR1), Enolase-related protein 3 (ERR3), Enolase 1 (ENO1)
  5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

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

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: SGD
  • glycolytic process Source: SGD
  • regulation of vacuole fusion, non-autophagic Source: SGD
Complete GO annotation...

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.
ReactomeiREACT_275254. Glycolysis.
REACT_286539. Gluconeogenesis.
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 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR254W.
SGDiS000003486. ENO1.

Subcellular locationi

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • mitochondrion Source: SGD
  • phosphopyruvate hydratase complex Source: SGD
Complete GO annotation...

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.

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi33505. 62 interactions.
DIPiDIP-5561N.
IntActiP00924. 18 interactions.
MINTiMINT-574648.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00800000124644.
HOGENOMiHOG000072174.
InParanoidiP00924.
KOiK01689.
OMAiEAYAGNQ.
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

        10         20         30         40         50
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR
60 70 80 90 100
DGDKSKWMGK GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT
110 120 130 140 150
ANKSKLGANA ILGVSLAASR AAAAEKNVPL YKHLADLSKS KTSPYVLPVP
160 170 180 190 200
FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEALRIGSEV YHNLKSLTKK
210 220 230 240 250
RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KIKIGLDCAS
260 270 280 290 300
SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI
360 370 380 390 400
GTLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA
410 420 430
PARSERLAKL NQLLRIEEEL GDNAVFAGEN FHHGDKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi33505. 62 interactions.
DIPiDIP-5561N.
IntActiP00924. 18 interactions.
MINTiMINT-574648.

Protein family/group databases

Allergomei786. Sac c Enolase.

2D gel databases

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

Proteomic databases

MaxQBiP00924.
PeptideAtlasiP00924.
PRIDEiP00924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGR254W.
SGDiS000003486. ENO1.

Phylogenomic databases

GeneTreeiENSGT00800000124644.
HOGENOMiHOG000072174.
InParanoidiP00924.
KOiK01689.
OMAiEAYAGNQ.
OrthoDBiEOG7JHMFP.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciYEAST:YGR254W-MONOMER.
BRENDAi4.2.1.11. 984.
ReactomeiREACT_275254. Glycolysis.
REACT_286539. Gluconeogenesis.
SABIO-RKP00924.

Miscellaneous databases

EvolutionaryTraceiP00924.
NextBioi973288.
PROiP00924.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.