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P00924

- ENO1_YEAST

UniProt

P00924 - ENO1_YEAST

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Protein

Enolase 1

Gene
ENO1, ENOA, HSP48, YGR254W, G9160
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601Substrate
Binding sitei169 – 1691Substrate
Active sitei212 – 2121Proton donor Inferred
Metal bindingi247 – 2471Magnesium
Metal bindingi296 – 2961Magnesium
Binding sitei296 – 2961Substrate
Metal bindingi321 – 3211Magnesium
Binding sitei321 – 3211Substrate
Active sitei346 – 3461Proton acceptor
Binding sitei397 – 3971Substrate

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
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.
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
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 1UniRule annotationPRO_0000134062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine By similarity
Modified residuei188 – 1881Phosphoserine By similarity
Modified residuei313 – 3131Phosphothreonine By similarity
Modified residuei324 – 3241Phosphothreonine By 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.

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.

Miscellaneous databases

EvolutionaryTraceiP00924.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the enolase family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421I → V in AAA88712. 1 Publication

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

« 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: June 11, 2014
This is version 166 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.

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

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