Enolase 2 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P00925 (ENO2_YEAST)

Last modified June 16, 2009. Version 100. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Enolase 2
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 2
    2-phospho-D-glycerate hydro-lyase 2

Gene names

Name:	ENO2
Synonyms:	ENOB
Ordered Locus Names:	YHR174W

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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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.

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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.
Miscellaneous	Present with 2610 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the enolase family.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	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 internal side of plasma membrane 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 soluble 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...

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Binary interactions

With	Entry	#Exp.	IntAct
	P43582	1	EBI-6475,EBI-22766
AUS1	Q08409	1	EBI-6475,EBI-35723
ESS1	P22696	1	EBI-6475,EBI-6679
PRP40	P33203	1	EBI-6475,EBI-701
RSP5	P39940	1	EBI-6475,EBI-16219
SET2	P46995	1	EBI-6475,EBI-16985
SSM4	P40318	1	EBI-6475,EBI-18208
URN1	Q06525	1	EBI-6475,EBI-35138

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3 Ref.4

Chain

2 – 437

436

Enolase 2

PRO_0000134063

Sites

Active site

160

By similarity

Metal binding

247

Magnesium By similarity

Metal binding

296

Magnesium By similarity

Metal binding

321

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.7 Ref.9

Modified residue

Phosphoserine Ref.10

Modified residue

188

Phosphoserine Ref.9 Ref.10

Modified residue

205

Phosphoserine Ref.10

Modified residue

221

Phosphothreonine Ref.10

Modified residue

324

Phosphothreonine Ref.11

Modified residue

326

Phosphothreonine Ref.11

Modified residue

373

Phosphoserine Ref.10

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Sequences

Sequence

Length

Mass (Da)

Tools

P00925-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 04599565F58A7643
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FASTA

437

46,914

        10         20         30         40         50         60 
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DEDKSKWMGK 

        70         80         90        100        110        120 
GVMNAVNNVN NVIAAAFVKA NLDVKDQKAV DDFLLSLDGT ANKSKLGANA ILGVSMAAAR 

       130        140        150        160        170        180 
AAAAEKNVPL YQHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF 

       190        200        210        220        230        240 
AEAMRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG 

       250        260        270        280        290        300 
KVKIGLDCAS SEFFKDGKYD LDFKNPESDK SKWLTGVELA DMYHSLMKRY PIVSIEDPFA 

       310        320        330        340        350        360 
EDDWEAWSHF FKTAGIQIVA DDLTVTNPAR IATAIEKKAA DALLLKVNQI GTLSESIKAA 

       370        380        390        400        410        420 
QDSFAANWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 

       430 
GDKAVYAGEN FHHGDKL

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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]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	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.
[4]	"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." Norbeck J., Blomberg A. FEMS Microbiol. Lett. 137:1-8(1996) [PubMed: 8935650] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Strain: ATCC 38531 / Y41.
[5]	"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 16-24; 57-60; 89-103; 290-298 AND 424-432. Strain: ATCC 38531 / Y41.
[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 127-139 AND 244-255. Strain: ATCC 204508 / S288c.
[7]	"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.
[8]	"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].
[9]	"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.
[10]	"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-40; SER-188; SER-205; THR-221 AND SER-373, MASS SPECTROMETRY.
[11]	"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 THR-324 AND THR-326, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	J01323 Genomic DNA. Translation: AAA88713.1. U00027 Genomic DNA. Translation: AAB68019.1.
PIR	NOBY2. A01148.
RefSeq	NP_012044.1.
3D structure databases
HSSP	HSSP built from PDB template 4ENL based on UniProtKB P00924.
SMR	P00925. Positions 2-437.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4777N.
IntAct	P00925. 71 interactions.
2-D gel databases
SWISS-2DPAGE	P00925.
COMPLUYEAST-2DPAGE	P00925.
Proteomic databases
PeptideAtlas	P00925.
PRIDE	P00925.
Genome annotation databases
Ensembl	YHR174W. Saccharomyces cerevisiae. [Contig view]
GeneID	856579.
GenomeReviews	Gene locus YHR174W in contig U00093_GR.
KEGG	sce:YHR174W.
NMPDR	fig\|4932.3.peg.3209.
Organism-specific databases
CYGD	YHR174w.
SGD	S000001217. ENO2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00925.
OMA	P00925. PTDAPTF.
Enzyme and pathway databases
BRENDA	4.2.1.11. 250.
Gene expression databases
GermOnline	YHR174W. 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...
Other Resources
NextBio	982438.

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Entry information

Entry name

ENO2_YEAST

Accession

Primary (citable) accession number: P00925
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 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents