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Protein

Enolase 1

Gene

ENO1

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)DescriptionActionsGraphical viewLength
Binding sitei160Substrate2 Publications1
Binding sitei169Substrate2 Publications1
Active sitei212Proton donorCurated1
Metal bindingi247Magnesium1 Publication1
Metal bindingi296Magnesium1 Publication1
Binding sitei296Substrate2 Publications1
Metal bindingi321Magnesium1 Publication1
Binding sitei321Substrate2 Publications1
Active sitei346Proton acceptor1
Binding sitei397Substrate2 Publications1

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

BioCyciYEAST:YGR254W-MONOMER.
BRENDAi4.2.1.11. 984.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP00924.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase 1 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
Gene namesi
Name:ENO1
Synonyms:ENOA, HSP48
Ordered Locus Names:YGR254W
ORF Names:G9160
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR254W.
SGDiS000003486. ENO1.

Subcellular locationi

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • mitochondrion Source: SGD
  • phosphopyruvate hydratase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40S → A: Reduces activity by 99.9%. 1
Mutagenesisi160H → A, F or N: Reduces activity by 99%. 2 Publications1
Mutagenesisi169E → Q: Reduces Kcat over 100000-fold. 1
Mutagenesisi208N → A: Reduces activity by 44%. 1 Publication1
Mutagenesisi212E → Q: Reduces Kcat over 100000-fold. 1
Mutagenesisi346K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. 1 Publication1

Protein family/group databases

Allergomei786. Sac c Enolase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001340622 – 437Enolase 1Add BLAST436

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei119PhosphoserineCombined sources1
Modified residuei138PhosphoserineBy similarity1
Modified residuei188PhosphoserineBy similarity1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei313PhosphothreonineBy similarity1
Modified residuei324PhosphothreonineBy similarity1
Cross-linki358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00924.
PRIDEiP00924.
TopDownProteomicsiP00924.

2D gel databases

COMPLUYEAST-2DPAGEP00924.
SWISS-2DPAGEP00924.
UCD-2DPAGEP00924.

PTM databases

iPTMnetiP00924.

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PKC1P245832EBI-6468,EBI-9860

Protein-protein interaction databases

BioGridi33505. 64 interactors.
DIPiDIP-5561N.
IntActiP00924. 19 interactors.
MINTiMINT-574648.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi18 – 26Combined sources9
Beta strandi29 – 34Combined sources6
Beta strandi43 – 45Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 71Combined sources9
Helixi73 – 80Combined sources8
Helixi87 – 98Combined sources12
Beta strandi100 – 102Combined sources3
Turni104 – 106Combined sources3
Helixi108 – 125Combined sources18
Helixi130 – 138Combined sources9
Beta strandi145 – 147Combined sources3
Beta strandi152 – 156Combined sources5
Helixi158 – 160Combined sources3
Beta strandi161 – 164Combined sources4
Beta strandi169 – 173Combined sources5
Helixi180 – 202Combined sources23
Helixi204 – 207Combined sources4
Beta strandi213 – 215Combined sources3
Helixi222 – 236Combined sources15
Turni239 – 241Combined sources3
Beta strandi243 – 247Combined sources5
Helixi250 – 253Combined sources4
Turni261 – 264Combined sources4
Helixi270 – 272Combined sources3
Helixi276 – 289Combined sources14
Beta strandi292 – 296Combined sources5
Helixi304 – 311Combined sources8
Turni312 – 314Combined sources3
Beta strandi316 – 321Combined sources6
Turni322 – 326Combined sources5
Helixi328 – 336Combined sources9
Beta strandi341 – 345Combined sources5
Helixi347 – 350Combined sources4
Helixi353 – 365Combined sources13
Beta strandi369 – 373Combined sources5
Helixi383 – 390Combined sources8
Beta strandi394 – 397Combined sources4
Helixi404 – 420Combined sources17
Helixi421 – 423Combined sources3
Beta strandi424 – 426Combined sources3
Helixi428 – 430Combined sources3
Helixi434 – 436Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBGX-ray2.10A/B2-437[»]
1EBHX-ray1.90A/B2-437[»]
1ELSX-ray2.40A2-437[»]
1L8PX-ray2.10A/B/C/D2-437[»]
1NELX-ray2.60A2-437[»]
1ONEX-ray1.80A/B2-437[»]
1P43X-ray1.80A/B2-437[»]
1P48X-ray2.00A/B2-437[»]
2AL1X-ray1.50A/B2-437[»]
2AL2X-ray1.85A/B2-437[»]
2ONEX-ray2.00A/B2-437[»]
2XGZX-ray1.80A/B2-437[»]
2XH0X-ray1.70A/B/C/D2-437[»]
2XH2X-ray1.80A/B/C/D2-437[»]
2XH4X-ray1.70A/B/C/D2-437[»]
2XH7X-ray1.80A/B2-437[»]
3ENLX-ray2.25A2-437[»]
4ENLX-ray1.90A2-437[»]
5ENLX-ray2.20A2-437[»]
6ENLX-ray2.20A2-437[»]
7ENLX-ray2.20A2-437[»]
ProteinModelPortaliP00924.
SMRiP00924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00924.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 376Substrate binding4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
InParanoidiP00924.
KOiK01689.
OMAiDSFDATW.
OrthoDBiEOG092C2W5X.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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.

P00924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR
60 70 80 90 100
DGDKSKWMGK GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT
110 120 130 140 150
ANKSKLGANA ILGVSLAASR AAAAEKNVPL YKHLADLSKS KTSPYVLPVP
160 170 180 190 200
FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEALRIGSEV YHNLKSLTKK
210 220 230 240 250
RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KIKIGLDCAS
260 270 280 290 300
SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI
360 370 380 390 400
GTLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA
410 420 430
PARSERLAKL NQLLRIEEEL GDNAVFAGEN FHHGDKL
Length:437
Mass (Da):46,816
Last modified:October 5, 2010 - v3
Checksum:i69F45214DBD375BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti242I → V in AAA88712 (PubMed:6256394).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01322 Genomic DNA. Translation: AAA88712.1.
X99228 Genomic DNA. Translation: CAA67616.1.
Z73039 Genomic DNA. Translation: CAA97283.1.
BK006941 Genomic DNA. Translation: DAA08345.1.
PIRiS64586. NOBY.
RefSeqiNP_011770.3. NM_001181383.3.

Genome annotation databases

EnsemblFungiiYGR254W; YGR254W; YGR254W.
GeneIDi853169.
KEGGisce:YGR254W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01322 Genomic DNA. Translation: AAA88712.1.
X99228 Genomic DNA. Translation: CAA67616.1.
Z73039 Genomic DNA. Translation: CAA97283.1.
BK006941 Genomic DNA. Translation: DAA08345.1.
PIRiS64586. NOBY.
RefSeqiNP_011770.3. NM_001181383.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBGX-ray2.10A/B2-437[»]
1EBHX-ray1.90A/B2-437[»]
1ELSX-ray2.40A2-437[»]
1L8PX-ray2.10A/B/C/D2-437[»]
1NELX-ray2.60A2-437[»]
1ONEX-ray1.80A/B2-437[»]
1P43X-ray1.80A/B2-437[»]
1P48X-ray2.00A/B2-437[»]
2AL1X-ray1.50A/B2-437[»]
2AL2X-ray1.85A/B2-437[»]
2ONEX-ray2.00A/B2-437[»]
2XGZX-ray1.80A/B2-437[»]
2XH0X-ray1.70A/B/C/D2-437[»]
2XH2X-ray1.80A/B/C/D2-437[»]
2XH4X-ray1.70A/B/C/D2-437[»]
2XH7X-ray1.80A/B2-437[»]
3ENLX-ray2.25A2-437[»]
4ENLX-ray1.90A2-437[»]
5ENLX-ray2.20A2-437[»]
6ENLX-ray2.20A2-437[»]
7ENLX-ray2.20A2-437[»]
ProteinModelPortaliP00924.
SMRiP00924.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33505. 64 interactors.
DIPiDIP-5561N.
IntActiP00924. 19 interactors.
MINTiMINT-574648.

Protein family/group databases

Allergomei786. Sac c Enolase.

PTM databases

iPTMnetiP00924.

2D gel databases

COMPLUYEAST-2DPAGEP00924.
SWISS-2DPAGEP00924.
UCD-2DPAGEP00924.

Proteomic databases

MaxQBiP00924.
PRIDEiP00924.
TopDownProteomicsiP00924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR254W; YGR254W; YGR254W.
GeneIDi853169.
KEGGisce:YGR254W.

Organism-specific databases

EuPathDBiFungiDB:YGR254W.
SGDiS000003486. ENO1.

Phylogenomic databases

GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
InParanoidiP00924.
KOiK01689.
OMAiDSFDATW.
OrthoDBiEOG092C2W5X.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciYEAST:YGR254W-MONOMER.
BRENDAi4.2.1.11. 984.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.
SABIO-RKP00924.

Miscellaneous databases

EvolutionaryTraceiP00924.
PROiP00924.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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...

Entry informationi

Entry nameiENO1_YEAST
AccessioniPrimary (citable) accession number: P00924
Secondary accession number(s): D6VV34, P99013
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: November 2, 2016
This is version 191 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 76700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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