Reviewed,
UniProtKB/Swiss-Prot Q8DPS0 (ENO_STRR6)
Last modified
February 9, 2010.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Enolase EC=4.2.1.11 Alternative name(s): 2-phosphoglycerate dehydratase 2-phospho-D-glycerate hydro-lyase | ||||
| Gene names |
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| Organism | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 171101 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 434 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence By similarity. HAMAP MF_00318 |
| Catalytic activity | 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP MF_00318 |
| Cofactor | Magnesium. Required for catalysis and for stabilizing the dimer By similarity. HAMAP MF_00318 |
| Enzyme regulation | The covalent binding to the substrate of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP MF_00318 |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP MF_00318 |
| Subunit structure | Homooctamer By similarity. HAMAP MF_00318 |
| Subcellular location | Cytoplasm. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface, probably in complex with plasminogen By similarity. HAMAP MF_00318 |
| Sequence similarities | Belongs to the enolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis Virulence |
| Cellular component | Cytoplasm Secreted |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: HAMAP pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-SubCell phosphopyruvate hydratase complexInferred from electronic annotation. Source: InterPro |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 434 | 434 | Enolase HAMAP MF_00318 | PRO_0000133981 | |||||
Regions | |||||||||
| Region | 370 – 373 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 205 | 1 | Proton donor By similarity | ||||||
| Active site | 343 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 242 | 1 | Magnesium By similarity | ||||||
| Metal binding | 291 | 1 | Magnesium By similarity | ||||||
| Metal binding | 318 | 1 | Magnesium By similarity | ||||||
| Binding site | 155 | 1 | Substrate By similarity | ||||||
| Binding site | 164 | 1 | Substrate By similarity | ||||||
| Binding site | 291 | 1 | Substrate By similarity | ||||||
| Binding site | 318 | 1 | Substrate By similarity | ||||||
| Binding site | 394 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 285 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | "Genome of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. Glass J.I.J. Bacteriol. 183:5709-5717(2001) [PubMed: 11544234] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE007317 Genomic DNA. Translation: AAK99840.1. |
| PIR | D98001. |
| RefSeq | NP_358630.1. |
3D structure databases | |
| SMR | Q8DPS0. Positions 1-432. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8DPS0. |
Genome annotation databases | |
| GeneID | 934109. |
| GenomeReviews | Gene locus spr1036 in contig AE007317_GR. |
| KEGG | spr:spr1036. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0148. |
| HOGENOM | HBG726599. |
| OMA | DIAVGTN. |
| PhylomeDB | Q8DPS0. |
Enzyme and pathway databases | |
| BioCyc | SPNE171101:SPR1036-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00318. Enolase. [Tree] |
| InterPro | IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view] |
| 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 | ENO_STRR6 | ||||||||
| Accession | Primary (citable) accession number: Q8DPS0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


