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 + H(2)O.
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.
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
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from expression pattern. Source: SGD glycolysis Inferred from electronic annotation. Source: InterPro 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 electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Inferred from electronic annotation. Source: InterPro 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

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

Metal binding

296

1

Magnesium

Metal binding

321

1

Magnesium

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

Modified residue

14

1

Phosphoserine

Modified residue

37

1

Phosphoserine

Modified residue

40

1

Phosphoserine

Modified residue

41

1

Phosphothreonine

Modified residue

96

1

Phosphoserine

Modified residue

104

1

Phosphoserine

Modified residue

119

1

Phosphoserine

Modified residue

143

1

Phosphoserine

Modified residue

188

1

Phosphoserine

Modified residue

324

1

Phosphothreonine

Modified residue

404

1

Phosphoserine

Experimental info

Mutagenesis

40

1

S → A: Reduces activity by 99.9%

Mutagenesis

160

1

H → A, F or N: Reduces activity by 99%

Mutagenesis

169

1

E → Q: Reduces Kcat over 100000-fold

Mutagenesis

208

1

N → A: Reduces activity by 44%

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

Sequence conflict

242

1

V → I in CAA67616 and CAA97283. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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) [