P00924 (ENO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

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.11.
Miscellaneous	Present with 76700 molecules/cell in log phase SD medium.
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 Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from expression pattern PubMed 3313003. Source: SGD glycolysis Inferred from mutant phenotype PubMed 6282834. Source: SGD regulation of vacuole fusion, non-autophagic Inferred from direct assay PubMed 16565073. Source: SGD
Cellular_component	fungal-type vacuole Inferred from direct assay PubMed 16565073. Source: SGD mitochondrion Inferred from direct assay PubMed 16962558. Source: SGD phosphopyruvate hydratase complex Inferred from direct assay PubMed 6282834. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Inferred from mutant phenotype PubMed 6282834. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PKC1	P24583	2	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.5 Ref.6

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.23

Metal binding

296

1

Magnesium Ref.23

Metal binding

321

1

Magnesium Ref.23

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.12 Ref.15 Ref.17 Ref.19

Modified residue

14

1

Phosphoserine Ref.19

Modified residue

37

1

Phosphoserine Ref.19

Modified residue

40

1

Phosphoserine Ref.19

Modified residue

41

1

Phosphothreonine Ref.19

Modified residue

96

1

Phosphoserine Ref.19

Modified residue

104

1

Phosphoserine Ref.18 Ref.19

Modified residue

119

1

Phosphoserine Ref.17

Modified residue

143

1

Phosphoserine Ref.19

Modified residue

188

1

Phosphoserine Ref.15 Ref.16 Ref.18 Ref.19

Modified residue

324

1

Phosphothreonine Ref.19

Modified residue

404

1

Phosphoserine Ref.17 Ref.18

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.10 Ref.13

Mutagenesis

169

1

E → Q: Reduces Kcat over 100000-fold.

Mutagenesis

208

1

N → A: Reduces activity by 44%. Ref.13

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.9

Sequence conflict

242

1

I → V in AAA88712. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

437

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

18 – 26

9

Beta strand

29 – 34

6

Beta strand

43 – 45

3

Helix

57 – 59

3

Helix

63 – 71

9

Helix

73 – 80

8

Helix

87 – 98

12

Beta strand

100 – 102

3

Turn

104 – 106

3

Helix

108 – 125

18

Helix

130 – 138

9

Beta strand

145 – 147

3

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

Beta strand

213 – 215

3

Helix

222 – 236

15

Turn

239 – 241

3

Beta strand

243 – 247

5

Helix

250 – 253

4

Turn

261 – 264

4

Helix

270 – 272

3

Helix

276 – 289

14

Beta strand

292 – 296

5

Helix

304 – 311

8

Turn

312 – 314

3

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 [UniParc]. Last modified October 5, 2010. Version 3. Checksum: 69F45214DBD375BE	FASTA	437	46,816
	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

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] [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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, MASS SPECTROMETRY. Strain: 2124.
[13]	"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.
[14]	"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].
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-188, MASS SPECTROMETRY. Strain: YAL6B.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, MASS SPECTROMETRY. Strain: ADR376.
[17]	"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-10; SER-119 AND SER-404, MASS SPECTROMETRY.
[18]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-188 AND SER-404, MASS SPECTROMETRY.
[19]	"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] [Europe PMC] [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.
[20]	"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).
[21]	"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).
[22]	"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).
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.

PIR

NOBY. S64586.

RefSeq

NP_011770.3. NM_001181383.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-436	[»]
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	2-436	[»]
5ENL	X-ray	2.20	A	2-436	[»]
6ENL	X-ray	2.20	A	2-436	[»]
7ENL	X-ray	2.20	A	2-436	[»]

ProteinModelPortal

P00924.

SMR

P00924. Positions 2-437.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5561N.

IntAct

P00924. 15 interactions.

MINT

MINT-574648.

STRING

4932.YGR254W.

Protein family/group databases

Allergome

786. Sac c Enolase.

2D gel databases

COMPLUYEAST-2DPAGE

P00924.

SWISS-2DPAGE

P00924.

UCD-2DPAGE

P00924.

Proteomic databases

PeptideAtlas

P00924.

PRIDE

P00924.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR254W; YGR254W; YGR254W.

GeneID

853169.

KEGG

sce:YGR254W.
sce:YGR261C.

Organism-specific databases

SGD

S000003486. ENO1.

Phylogenomic databases

GeneTree

ENSGT00550000074560.

HOGENOM

HOG000072174.

KO

K01689.

OMA

GELYKNF.

OrthoDB

EOG48WG9D.

Enzyme and pathway databases

BRENDA

4.2.1.11. 984.

SABIO-RK

P00924.

UniPathway

UPA00109; UER00187.

Gene expression databases

Genevestigator

P00924.

GermOnline

YGR254W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]

PANTHER

PTHR11902. PTHR11902. 1 hit.

Pfam

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

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00924.

NextBio

973288.

Entry information

Entry name

ENO1_YEAST

Accession

Primary (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:	April 3, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program