Q6FTW6 (ENO1_CANGA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Enolase 1 EC=4.2.1.11 Alternative name(s): 2-phospho-D-glycerate hydro-lyase 1 2-phosphoglycerate dehydratase 1 | ||||
| Gene names |
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| Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome] | ||||
| Taxonomic identifier | 284593 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces |
Protein attributes
| Sequence length | 438 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 By similarity. |
| Sequence similarities | Belongs to the enolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| 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: InterPro 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 – 438 | 438 | Enolase 1 | PRO_0000134044 | |||||
Regions | |||||||||
| Region | 373 – 376 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 212 | 1 | Proton donor By similarity | ||||||
| Active site | 346 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 247 | 1 | Magnesium By similarity | ||||||
| Metal binding | 296 | 1 | Magnesium By similarity | ||||||
| Metal binding | 321 | 1 | Magnesium By similarity | ||||||
| Binding site | 160 | 1 | Substrate By similarity | ||||||
| Binding site | 169 | 1 | Substrate By similarity | ||||||
| Binding site | 296 | 1 | Substrate By similarity | ||||||
| Binding site | 321 | 1 | Substrate By similarity | ||||||
| Binding site | 397 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR380952 Genomic DNA. Translation: CAG59252.1. |
| RefSeq | XP_446328.1. XM_446328.1. |
3D structure databases | |
| ProteinModelPortal | Q6FTW6. |
| SMR | Q6FTW6. Positions 2-438. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2887972. |
| GenomeReviews | Gene locus CAGL0F08261g in contig CR380952_GR. |
| KEGG | cgr:CAGL0F08261g. |
Phylogenomic databases | |
| eggNOG | fuNOG04478. |
| HOGENOM | HBG726599. |
| OMA | KDPTEQT. |
| OrthoDB | EOG48WG9D. |
Family and domain databases | |
| InterPro | IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view] |
| KO | K01689. |
| 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. |
| TIGRFAMs | TIGR01060. Eno. 1 hit. |
| PROSITE | PS00164. ENOLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ENO1_CANGA | ||||||||
| Accession | Primary (citable) accession number: Q6FTW6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with