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Protein

Enolase 1

Gene

ENO1

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

Functioni

Miscellaneous

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

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 1 (ERR1), Enolase-related protein 3 (ERR3), 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

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YGR254W-MONOMER
BRENDAi4.2.1.11 984
SABIO-RKiP00924
UniPathwayiUPA00109; UER00187

Protein family/group databases

MoonProtiP00924

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP00924
PRIDEiP00924
TopDownProteomicsiP00924

2D gel databases

COMPLUYEAST-2DPAGEiP00924
SWISS-2DPAGEiP00924
UCD-2DPAGEiP00924

PTM databases

CarbonylDBiP00924
iPTMnetiP00924

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SSB1P114843EBI-6468,EBI-8627

Protein-protein interaction databases

BioGridi33505, 133 interactors
DIPiDIP-5561N
IntActiP00924, 105 interactors
MINTiP00924
STRINGi4932.YGR254W

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

GeneTreeiENSGT00910000144064
HOGENOMiHOG000072174
InParanoidiP00924
KOiK01689
OMAiEFMIIPV
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
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SFLDiSFLDG00178 enolase, 1 hit
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiENO1_YEAST
AccessioniPrimary (citable) accession number: P00924
Secondary accession number(s): D6VV34, P99013
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: April 25, 2018
This is version 204 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health