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Protein

Enolase 2

Gene

ENO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
  4. Enolase 2 (ENO2), Enolase-related protein 2 (ERR2), Enolase-related protein 3 (ERR3), Enolase-related protein 1 (ERR1), Enolase 1 (ENO1)
  5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei160 – 1601By similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Metal bindingi296 – 2961MagnesiumBy similarity
Metal bindingi321 – 3211MagnesiumBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: SGD
  • glycolytic process Source: SGD
  • regulation of vacuole fusion, non-autophagic Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YHR174W-MONOMER.
YEAST:YHR174W-MONOMER.
BRENDAi4.2.1.11. 984.
SABIO-RKP00925.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase 2 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2
2-phosphoglycerate dehydratase 2
Gene namesi
Name:ENO2
Synonyms:ENOB
Ordered Locus Names:YHR174W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR174W.
SGDiS000001217. ENO2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: SGD
  • fungal-type vacuole Source: SGD
  • mitochondrion Source: SGD
  • phosphopyruvate hydratase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 437436Enolase 2PRO_0000134063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei188 – 1881PhosphoserineCombined sources
Modified residuei313 – 3131PhosphothreonineCombined sources
Modified residuei324 – 3241PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00925.
PeptideAtlasiP00925.
PRIDEiP00925.
TopDownProteomicsiP00925.

2D gel databases

COMPLUYEAST-2DPAGEP00925.
SWISS-2DPAGEP00925.
UCD-2DPAGEP00925.

PTM databases

iPTMnetiP00925.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-6475,EBI-16219

Protein-protein interaction databases

BioGridi36607. 167 interactions.
DIPiDIP-4777N.
IntActiP00925. 70 interactions.
MINTiMINT-8285263.

Structurei

3D structure databases

ProteinModelPortaliP00925.
SMRiP00925. Positions 2-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
InParanoidiP00925.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG7JHMFP.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR
60 70 80 90 100
DEDKSKWMGK GVMNAVNNVN NVIAAAFVKA NLDVKDQKAV DDFLLSLDGT
110 120 130 140 150
ANKSKLGANA ILGVSMAAAR AAAAEKNVPL YQHLADLSKS KTSPYVLPVP
160 170 180 190 200
FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEAMRIGSEV YHNLKSLTKK
210 220 230 240 250
RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KVKIGLDCAS
260 270 280 290 300
SEFFKDGKYD LDFKNPESDK SKWLTGVELA DMYHSLMKRY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FKTAGIQIVA DDLTVTNPAR IATAIEKKAA DALLLKVNQI
360 370 380 390 400
GTLSESIKAA QDSFAANWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA
410 420 430
PARSERLAKL NQLLRIEEEL GDKAVYAGEN FHHGDKL
Length:437
Mass (Da):46,914
Last modified:January 23, 2007 - v2
Checksum:i04599565F58A7643
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01323 Genomic DNA. Translation: AAA88713.1.
U00027 Genomic DNA. Translation: AAB68019.1.
BK006934 Genomic DNA. Translation: DAA06866.1.
PIRiA01148. NOBY2.
RefSeqiNP_012044.1. NM_001179305.1.

Genome annotation databases

EnsemblFungiiYHR174W; YHR174W; YHR174W.
GeneIDi856579.
KEGGisce:YHR174W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01323 Genomic DNA. Translation: AAA88713.1.
U00027 Genomic DNA. Translation: AAB68019.1.
BK006934 Genomic DNA. Translation: DAA06866.1.
PIRiA01148. NOBY2.
RefSeqiNP_012044.1. NM_001179305.1.

3D structure databases

ProteinModelPortaliP00925.
SMRiP00925. Positions 2-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36607. 167 interactions.
DIPiDIP-4777N.
IntActiP00925. 70 interactions.
MINTiMINT-8285263.

PTM databases

iPTMnetiP00925.

2D gel databases

COMPLUYEAST-2DPAGEP00925.
SWISS-2DPAGEP00925.
UCD-2DPAGEP00925.

Proteomic databases

MaxQBiP00925.
PeptideAtlasiP00925.
PRIDEiP00925.
TopDownProteomicsiP00925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR174W; YHR174W; YHR174W.
GeneIDi856579.
KEGGisce:YHR174W.

Organism-specific databases

EuPathDBiFungiDB:YHR174W.
SGDiS000001217. ENO2.

Phylogenomic databases

GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
InParanoidiP00925.
KOiK01689.
OMAiNFRNPRI.
OrthoDBiEOG7JHMFP.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:YHR174W-MONOMER.
YEAST:YHR174W-MONOMER.
BRENDAi4.2.1.11. 984.
SABIO-RKP00925.

Miscellaneous databases

NextBioi982438.
PROiP00925.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: ATCC 26786 / X2180-1A.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
    Strain: ATCC 38531 / Y41.
  6. "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 16-24; 57-60; 89-103; 290-298 AND 424-432.
    Strain: ATCC 38531 / Y41.
  7. Cited for: PROTEIN SEQUENCE OF 127-139 AND 244-255.
    Strain: ATCC 204508 / S288c.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 THR-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND THR-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENO2_YEAST
AccessioniPrimary (citable) accession number: P00925
Secondary accession number(s): D3DLC2, P99013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2610 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.