Reviewed,
UniProtKB/Swiss-Prot Q8KG25 (ENO2_CHLTE)
Last modified
February 9, 2010.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (2) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Enolase 2 EC=4.2.1.11 Alternative name(s): 2-phosphoglycerate dehydratase 2 2-phospho-D-glycerate hydro-lyase 2 | ||||||
| Gene names |
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| Organism | Chlorobium tepidum [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1097 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum |
Protein attributes
| Sequence length | 437 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 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 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 |
| 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 By similarity. HAMAP MF_00318 |
| Sequence similarities | Belongs to the enolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| 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 |
| 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 – 437 | 437 | Enolase 2 HAMAP MF_00318 | PRO_0000133869 | |||||
Regions | |||||||||
| Region | 376 – 379 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 204 | 1 | Proton donor By similarity | ||||||
| Active site | 349 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 251 | 1 | Magnesium By similarity | ||||||
| Metal binding | 297 | 1 | Magnesium By similarity | ||||||
| Metal binding | 324 | 1 | Magnesium By similarity | ||||||
| Binding site | 154 | 1 | Substrate By similarity | ||||||
| Binding site | 163 | 1 | Substrate By similarity | ||||||
| Binding site | 297 | 1 | Substrate By similarity | ||||||
| Binding site | 324 | 1 | Substrate By similarity | ||||||
| Binding site | 349 | 1 | Substrate (covalent); in inhibited form By similarity | ||||||
| Binding site | 400 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 291 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.  Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006470 Genomic DNA. Translation: AAM71393.1. |
| RefSeq | NP_661051.1. |
3D structure databases | |
| SMR | Q8KG25. Positions 2-435. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1007040. |
| GenomeReviews | Gene locus CT0145 in contig AE006470_GR. |
| KEGG | cte:CT0145. |
| NMPDR | fig|194439.1.peg.145. |
| TIGR | CT0145. |
Phylogenomic databases | |
| HOGENOM | HBG726599. |
| OMA | DIAVGTN. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:CT_0145-MONOMER. |
| BRENDA | 4.2.1.11. 189605. |
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 | ENO2_CHLTE | ||||||||
| Accession | Primary (citable) accession number: Q8KG25 | ||||||||
| 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 |
