Reviewed, UniProtKB/Swiss-Prot P00924 (ENO1_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from expression pattern. Source: SGD glycolysis Inferred from mutant phenotype. Source: SGD regulation of vacuole fusion, non-autophagic Inferred from direct assay. Source: SGD
Cellular component	fungal-type vacuole Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD phosphopyruvate hydratase complex Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PKC1	P24583	1	EBI-6468,EBI-9860

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4 Ref.5

Chain

2 – 437

436

Enolase 1

PRO_0000134062

Regions

Region

373 – 376

4

Substrate binding

Sites

Active site

212

1

Proton donor Probable

Active site

346

1

Proton acceptor

Metal binding

247

1

Magnesium Ref.22

Metal binding

296

1

Magnesium Ref.22

Metal binding

321

1

Magnesium Ref.22

Binding site

160

1

Substrate

Binding site

169

1

Substrate

Binding site

296

1

Substrate

Binding site

321

1

Substrate

Binding site

397

1

Substrate

Amino acid modifications

Modified residue

10

1

Phosphoserine Ref.11 Ref.14 Ref.16 Ref.18

Modified residue

14

1

Phosphoserine Ref.18

Modified residue

37

1

Phosphoserine Ref.18

Modified residue

40

1

Phosphoserine Ref.18

Modified residue

41

1

Phosphothreonine Ref.18

Modified residue

96

1

Phosphoserine Ref.18

Modified residue

104

1

Phosphoserine Ref.18 Ref.17

Modified residue

119

1

Phosphoserine Ref.16

Modified residue

143

1

Phosphoserine Ref.18

Modified residue

188

1

Phosphoserine Ref.14 Ref.18 Ref.17 Ref.15

Modified residue

324

1

Phosphothreonine Ref.18

Modified residue

404

1

Phosphoserine Ref.16 Ref.17

Experimental info

Mutagenesis

40

1

S → A: Reduces activity by 99.9%.

Mutagenesis

160

1

H → A, F or N: Reduces activity by 99%. Ref.9 Ref.12

Mutagenesis

169

1

E → Q: Reduces Kcat over 100000-fold.

Mutagenesis

208

1

N → A: Reduces activity by 44%. Ref.12

Mutagenesis

212

1

E → Q: Reduces Kcat over 100000-fold.

Mutagenesis

346

1

K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. Ref.8

Sequence conflict

242

1

V → I in CAA67616. Ref.2

Sequence conflict

242

1

V → I in CAA97283. Ref.2

Secondary structure

1

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437

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

18 – 26

9

Beta strand

29 – 34

6

Helix

57 – 59

3

Helix

63 – 71

9

Helix

73 – 80

8

Helix

87 – 98

12

Turn

104 – 106

3

Helix

108 – 126

19

Helix

130 – 138

9

Beta strand

143 – 147

5

Beta strand

152 – 156

5

Helix

158 – 160

3

Beta strand

161 – 164

4

Beta strand

169 – 173

5

Helix

180 – 202

23

Helix

204 – 207

4

Helix

222 – 236

15

Turn

239 – 241

3

Beta strand

243 – 247

5

Helix

250 – 253

4

Turn

261 – 264

4

Turn

270 – 272

3

Helix

276 – 289

14

Beta strand

292 – 296

5

Helix

304 – 314

11

Beta strand

316 – 321

6

Turn

322 – 326

5

Helix

328 – 336

9

Beta strand

341 – 345

5

Helix

347 – 350

4

Helix

353 – 365

13

Beta strand

369 – 373

5

Helix

383 – 390

8

Beta strand

394 – 397

4

Helix

404 – 420

17

Helix

421 – 423

3

Beta strand

424 – 426

3

Helix

428 – 430

3

Helix

434 – 436

3

Sequences

	Sequence		Length	Mass (Da)
	P00924-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5E874ABDFA495E17	FASTA	437	46,802
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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

PIR

NOBY. S64586.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EBG	X-ray	2.10	A/B	2-436	[»]
1EBH	X-ray	1.90	A/B	2-436	[»]
1ELS	X-ray	2.40	A	2-436	[»]
1L8P	X-ray	2.10	A/B/C/D	2-437	[»]
1NEL	X-ray	2.60	A	2-436	[»]
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	2-436	[»]
2AL2	X-ray	1.85	A/B	1-437	[»]
2ONE	X-ray	2.00	A/B	2-437	[»]
3ENL	X-ray	2.25	A	2-437	[»]
4ENL	X-ray	1.90	A	2-436	[»]
5ENL	X-ray	2.20	A	2-436	[»]
6ENL	X-ray	2.20	A	2-436	[»]
7ENL	X-ray	2.20	A	2-436	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5561N.

IntAct

P00924. 29 interactions.

2-D gel databases

SWISS-2DPAGE

P00924.

COMPLUYEAST-2DPAGE

P00924.

Proteomic databases

PeptideAtlas

P00924.

PRIDE

P00924.

Genome annotation databases

Ensembl

YGR254W. Saccharomyces cerevisiae. [Contig view]

GenomeReviews

Gene locus YGR254W in contig Y13135_GR.

KEGG

sce:YGR254W.

Organism-specific databases

CYGD

YGR254w.

SGD

S000003486. ENO1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00924.

Enzyme and pathway databases

BRENDA

4.2.1.11. 250.

Gene expression databases

ArrayExpress

P00924.

GermOnline

YGR254W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000941. Enolase.
[Graphical view]

PANTHER

PTHR11902. Enolase. 1 hit.

Pfam

PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

ProDom

PD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ENO1_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)