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P51555 (ENO1_ENTHI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enolase 1
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene names
Name:ENL-1
OrganismEntamoeba histolytica
Taxonomic identifier5759 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Enolase 1
PRO_0000134080

Regions

Region374 – 3774Substrate binding By similarity

Sites

Active site2081Proton donor By similarity
Active site3471Proton acceptor By similarity
Metal binding2431Magnesium By similarity
Metal binding2961Magnesium By similarity
Metal binding3221Magnesium By similarity
Binding site1561Substrate By similarity
Binding site1651Substrate By similarity
Binding site2961Substrate By similarity
Binding site3221Substrate By similarity
Binding site3981Substrate By similarity

Secondary structure

1 ............................................................................ 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51555 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BFBA693A65B44289

FASTA43647,327
        10         20         30         40         50         60 
MSIQKVHARE ILDSRGNPTI EVEITTGKGM FRSCVPSGAS TGVHEAVELR DGDKKRYGGK 

        70         80         90        100        110        120 
GVLKAVENVN TIIGPALLGK NVLNQAELDE MMIKLDGTNN KGKLGANAIL GCSMSICRAA 

       130        140        150        160        170        180 
AAEKGLPLYK YLAELTGHKE MTMPVPCFNV INGGAHAGNA LAMQEFMICP TGATNFHEAL 

       190        200        210        220        230        240 
RMAAETYQCL KVVIKAKYGQ DATNVGDEGG FAPNVSGARE ALDLLVEAIA KAGYTGKIEI 

       250        260        270        280        290        300 
AMDCAASEFY NEETKKYDLG KKIPADKKDP SLVKDVDGLI AEYVDYGKHY PIASIEDPFA 

       310        320        330        340        350        360 
EDDWAAWNKF TVEHGNFQIV GDDLLVTNPA RVQMAMDKNA CNSVLIKVNQ IGTLTETFKT 

       370        380        390        400        410        420 
IKMAQEKGWG VMASHRSGET EDTFIADLVV GLNCKQIKTG APCRSERLCK YNQLMRIEEE 

       430 
LGNIPYAGKN WRNSTA

« Hide

References

[1]"The primary structure of an Entamoeba histolytica enolase."
Beanan M.J., Bailey G.B.
Mol. Biochem. Parasitol. 69:119-121(1995) [PubMed: 7723780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 30459 / HM-1:IMSS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U09736 mRNA. Translation: AAA80166.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QTPX-ray1.90A/B1-436[»]
ProteinModelPortalP51555.
SMRP51555. Positions 2-435.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. Eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO1_ENTHI
AccessionPrimary (citable) accession number: P51555
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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