Q9Y927 (ENO_AERPE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 78.
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 EC=4.2.1.11 Alternative name(s): 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase | ||||
| Gene names |
| ||||
| Organism | Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272557 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum |
Protein attributes
| Sequence length | 432 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. |
| 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 archaeal 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 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred 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: 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 – 432 | 432 | Enolase HAMAP MF_00318 | PRO_0000134019 | |||||
Regions | |||||||||
| Region | 367 – 370 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 210 | 1 | Proton donor By similarity | ||||||
| Active site | 340 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 247 | 1 | Magnesium By similarity | ||||||
| Metal binding | 288 | 1 | Magnesium By similarity | ||||||
| Metal binding | 315 | 1 | Magnesium By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
| Binding site | 167 | 1 | Substrate By similarity | ||||||
| Binding site | 288 | 1 | Substrate By similarity | ||||||
| Binding site | 315 | 1 | Substrate By similarity | ||||||
| Binding site | 340 | 1 | Substrate (covalent); in inhibited form By similarity | ||||||
| Binding site | 391 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. Kikuchi H.DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000002 Genomic DNA. Translation: BAA81473.1. |
| PIR | A72477. |
| RefSeq | NP_148623.1. NC_000854.2. |
3D structure databases | |
| ProteinModelPortal | Q9Y927. |
| SMR | Q9Y927. Positions 3-427. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1445431. |
| GenomeReviews | Gene locus APE_2458 in contig BA000002_GR. |
| KEGG | ape:APE_2458. |
| NMPDR | fig|272557.1.peg.1731. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG726599. |
| OMA | EAWSYFY. |
Enzyme and pathway databases | |
| BioCyc | APER272557:APE2458-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00318. Enolase. [Tree] |
| 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 | ENO_AERPE | ||||||||
| Accession | Primary (citable) accession number: Q9Y927 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with