Reviewed,
UniProtKB/Swiss-Prot P51555 (ENO1_ENTHI)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Enolase 1 EC=4.2.1.11 Alternative name(s): 2-phosphoglycerate dehydratase 2-phospho-D-glycerate hydro-lyase | ||
| Gene names |
| ||
| Organism | Entamoeba histolytica | ||
| Taxonomic identifier | 5759 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba |
Protein attributes
| Sequence length | 436 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript 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 | |
| Sequence similarities | Belongs to the enolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 436 | 436 | Enolase 1 | PRO_0000134080 | |||||
Regions | |||||||||
| Region | 374 – 377 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 208 | 1 | Proton donor By similarity | ||||||
| Active site | 347 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 243 | 1 | Magnesium By similarity | ||||||
| Metal binding | 296 | 1 | Magnesium By similarity | ||||||
| Metal binding | 322 | 1 | Magnesium By similarity | ||||||
| Binding site | 156 | 1 | Substrate By similarity | ||||||
| Binding site | 165 | 1 | Substrate By similarity | ||||||
| Binding site | 296 | 1 | Substrate By similarity | ||||||
| Binding site | 322 | 1 | Substrate By similarity | ||||||
| Binding site | 398 | 1 | Substrate By similarity | ||||||
Sequences
| ||||||||||||||||||
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: HM-1:IMSS. |
Cross-references
Sequence databases | |
|---|---|
| U09736 mRNA. Translation: AAA80166.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.2.1.11. 323. |
Family and domain databases | |
| InterPro | IPR000941. Enolase. [Graphical view] |
| PANTHER | PTHR11902. Enolase. 1 hit. |
| Pfam | PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF001400. Enolase. 1 hit. |
| PRINTS | PR00148. ENOLASE. |
| ProDom | PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01060. eno. 1 hit. |
| PROSITE | PS00164. ENOLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ENO1_ENTHI | ||||||||
| Accession | Primary (citable) accession number: P51555 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


