Reviewed, UniProtKB/Swiss-Prot P00925 (ENO2_YEAST)

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

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 2610 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	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 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 electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	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

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 2		PRO_0000134063
Sites
	Active site	160	1	By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Metal binding	321	1	Magnesium By similarity
Amino acid modifications
	Modified residue	10	1	Phosphoserine
	Modified residue	40	1	Phosphoserine
	Modified residue	188	1	Phosphoserine
	Modified residue	205	1	Phosphoserine
	Modified residue	221	1	Phosphothreonine
	Modified residue	324	1	Phosphothreonine
	Modified residue	326	1	Phosphothreonine
	Modified residue	373	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P00925-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 04599565F58A7643	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

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. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
2-D gel databases
SWISS-2DPAGE	P00925.
COMPLUYEAST-2DPAGE	P00925.
Proteomic databases
PeptideAtlas	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.
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
LinkHub	P00925.
NextBio	982438.

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:	November 25, 2008
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)