Reviewed,
UniProtKB/Swiss-Prot P07322 (ENOB_CHICK)
Last modified
June 16, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Beta-enolase EC=4.2.1.11 Alternative name(s): 2-phospho-D-glycerate hydro-lyase Phosphopyruvate hydratase | ||
| Gene names |
| ||
| Organism | Gallus gallus (Chicken) | ||
| Taxonomic identifier | 9031 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 434 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. |
| Cofactor | Magnesium. Required for catalysis and for stabilizing the dimer. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. |
| Subunit structure | Homodimer. Interacts with PNKD 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 |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 434 | 433 | Beta-enolase | PRO_0000134111 | |||||
Regions | |||||||||
| Region | 370 – 373 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 210 | 1 | Proton donor By similarity | ||||||
| Active site | 343 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 245 | 1 | Magnesium By similarity | ||||||
| Metal binding | 293 | 1 | Magnesium By similarity | ||||||
| Metal binding | 318 | 1 | Magnesium By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
| Binding site | 167 | 1 | Substrate By similarity | ||||||
| Binding site | 293 | 1 | Substrate By similarity | ||||||
| Binding site | 318 | 1 | Substrate By similarity | ||||||
| Binding site | 394 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 17 | 1 | E → D AA sequence Ref.2 | ||||||
| Sequence conflict | 49 | 1 | P → L AA sequence Ref.2 | ||||||
| Sequence conflict | 94 | 1 | M → V AA sequence Ref.2 | ||||||
| Sequence conflict | 119 – 120 | 2 | CK → SH AA sequence Ref.2 | ||||||
| Sequence conflict | 209 | 1 | G → D AA sequence Ref.2 | ||||||
| Sequence conflict | 258 | 1 | H → D AA sequence Ref.2 | ||||||
| Sequence conflict | 266 – 267 | 2 | HT → DP AA sequence Ref.2 | ||||||
| Sequence conflict | 270 | 1 | Y → L AA sequence Ref.2 | ||||||
| Sequence conflict | 309 | 1 | F → S AA sequence Ref.2 | ||||||
| Sequence conflict | 323 | 1 | T → A AA sequence Ref.2 | ||||||
| Sequence conflict | 331 | 1 | G → A AA sequence Ref.2 | ||||||
| Sequence conflict | 343 | 1 | K → G AA sequence Ref.2 | ||||||
| Sequence conflict | 394 – 395 | 2 | KT → EQ AA sequence Ref.2 | ||||||
Sequences
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References
| [1] | "Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis." Tanaka M., Maeda K., Nakashima K. J. Biochem. 117:554-559(1995) [PubMed: 7629021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: White leghorn. Tissue: Muscle. |
| [2] | "The complete amino acid sequence of chicken skeletal-muscle enolase." Russell G.A., Dunbar B., Fothergill-Gilmore L.A. Biochem. J. 236:115-126(1986) [PubMed: 3539098] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-434. |
| [3] | "Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase." Gibson B.W., Daley D.J., Williams D.H. Anal. Biochem. 169:217-226(1988) [PubMed: 2898218] [Abstract] Cited for: ACETYLATION AT SER-2. |
Cross-references
Sequence databases | |
|---|---|
| D37901 mRNA. Translation: BAA07133.1. | |
| IPI | IPI00586105. |
| PIR | A23850. JC4187. |
| RefSeq | NP_990450.1. |
| UniGene | Gga.4297 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8. |
| SMR | P07322. Positions 2-431. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P07322. |
Genome annotation databases | |
| GeneID | 396016. |
| KEGG | gga:396016. |
Phylogenomic databases | |
| HOVERGEN | P07322. |
Enzyme and pathway databases | |
| BRENDA | 4.2.1.11. 4. |
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 | ENOB_CHICK | ||||||||
| Accession | Primary (citable) accession number: P07322 | ||||||||
| 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


