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Protein

Enolase 1

Gene

ENL-1

Organism
Entamoeba histolytica
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Mg2+ is required for catalysis and for stabilizing the dimer.By similarity

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, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (CL6EHI_008200), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase 1 (ENL-1)
  5. Pyruvate kinase (CL6EHI_098420)
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 sitei156SubstrateBy similarity1
Binding sitei165SubstrateBy similarity1
Active sitei208Proton donorBy similarity1
Metal bindingi243MagnesiumBy similarity1
Metal bindingi296MagnesiumBy similarity1
Binding sitei296SubstrateBy similarity1
Metal bindingi322MagnesiumBy similarity1
Binding sitei322SubstrateBy similarity1
Active sitei347Proton acceptorBy similarity1
Binding sitei398SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKiP51555.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase 1 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene namesi
Name:ENL-1
OrganismiEntamoeba histolytica
Taxonomic identifieri5759 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001340801 – 436Enolase 1Add BLAST436

Proteomic databases

PRIDEiP51555.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi5759.rna_EHI_130700-1.

Structurei

Secondary structure

1436
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 – 77Combined sources5
Helixi85 – 96Combined sources12
Turni102 – 104Combined sources3
Helixi106 – 123Combined sources18
Helixi128 – 136Combined sources9
Beta strandi145 – 152Combined sources8
Helixi154 – 156Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi163 – 169Combined sources7
Helixi176 – 198Combined sources23
Helixi200 – 203Combined sources4
Helixi218 – 232Combined sources15
Turni235 – 237Combined sources3
Beta strandi239 – 243Combined sources5
Helixi246 – 249Combined sources4
Turni252 – 255Combined sources4
Beta strandi256 – 258Combined sources3
Turni259 – 262Combined sources4
Helixi265 – 267Combined sources3
Helixi270 – 272Combined sources3
Helixi276 – 289Combined sources14
Beta strandi292 – 297Combined sources6
Helixi304 – 313Combined sources10
Turni314 – 316Combined sources3
Beta strandi317 – 322Combined sources6
Turni323 – 327Combined sources5
Helixi329 – 338Combined sources10
Beta strandi342 – 346Combined sources5
Helixi348 – 350Combined sources3
Helixi354 – 366Combined sources13
Beta strandi370 – 374Combined sources5
Helixi384 – 391Combined sources8
Beta strandi395 – 398Combined sources4
Helixi405 – 421Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QTPX-ray1.90A/B1-436[»]
ProteinModelPortaliP51555.
SMRiP51555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni374 – 377Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
OMAiFAPNIMS.

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.
IPR034390. Enolase-like_superfamily.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
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.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P51555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIQKVHARE ILDSRGNPTI EVEITTGKGM FRSCVPSGAS TGVHEAVELR
60 70 80 90 100
DGDKKRYGGK GVLKAVENVN TIIGPALLGK NVLNQAELDE MMIKLDGTNN
110 120 130 140 150
KGKLGANAIL GCSMSICRAA AAEKGLPLYK YLAELTGHKE MTMPVPCFNV
160 170 180 190 200
INGGAHAGNA LAMQEFMICP TGATNFHEAL RMAAETYQCL KVVIKAKYGQ
210 220 230 240 250
DATNVGDEGG FAPNVSGARE ALDLLVEAIA KAGYTGKIEI AMDCAASEFY
260 270 280 290 300
NEETKKYDLG KKIPADKKDP SLVKDVDGLI AEYVDYGKHY PIASIEDPFA
310 320 330 340 350
EDDWAAWNKF TVEHGNFQIV GDDLLVTNPA RVQMAMDKNA CNSVLIKVNQ
360 370 380 390 400
IGTLTETFKT IKMAQEKGWG VMASHRSGET EDTFIADLVV GLNCKQIKTG
410 420 430
APCRSERLCK YNQLMRIEEE LGNIPYAGKN WRNSTA
Length:436
Mass (Da):47,327
Last modified:October 1, 1996 - v1
Checksum:iBFBA693A65B44289
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09736 mRNA. Translation: AAA80166.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09736 mRNA. Translation: AAA80166.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QTPX-ray1.90A/B1-436[»]
ProteinModelPortaliP51555.
SMRiP51555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5759.rna_EHI_130700-1.

Proteomic databases

PRIDEiP51555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
OMAiFAPNIMS.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
SABIO-RKiP51555.

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.
IPR034390. Enolase-like_superfamily.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
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.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENO1_ENTHI
AccessioniPrimary (citable) accession number: P51555
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 12, 2017
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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

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.