Reviewed,
UniProtKB/Swiss-Prot P22360 (KPYK_EMENI)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate kinase Short name=PK EC=2.7.1.40 | ||||||
| Gene names |
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| Organism | Emericella nidulans (Aspergillus nidulans) | ||||||
| Taxonomic identifier | 162425 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 526 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | ATP + pyruvate = ADP + phosphoenolpyruvate. |
| Cofactor | Magnesium. Potassium. |
| Enzyme regulation | Regulated by phosphoenolpyruvate substrate and allosteric effectors such as fructose 1,6 diphosphate and magnesium. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. |
| Subunit structure | Homotetramer. |
| Sequence similarities | Belongs to the pyruvate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate |
| Molecular function | Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Allosteric enzyme |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW potassium ion bindingInferred from electronic annotation. Source: InterPro pyruvate kinase 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 – 526 | 526 | Pyruvate kinase | PRO_0000112113 | |||||
Sites | |||||||||
| Active site | 254 | 1 | By similarity | ||||||
| Metal binding | 256 | 1 | Magnesium Potential | ||||||
| Metal binding | 277 | 1 | Magnesium Potential | ||||||
| Metal binding | 278 | 1 | Magnesium Potential | ||||||
| Binding site | 351 | 1 | ADP Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 36 | 1 | Phosphoserine Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 88 | 1 | Q → A in AAA33320. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structure of the Aspergillus nidulans pyruvate kinase gene." de Graaff L., Visser J. Curr. Genet. 14:553-560(1988) [PubMed: 3072099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WG096. |
| [2] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| M36918 Genomic DNA. Translation: AAA33320.1. AACD01000089 Genomic DNA. Translation: EAA62391.1. | |
| PIR | S27364. |
| RefSeq | XP_662814.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1E0T based on UniProtKB P14178. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2871501. |
| KEGG | ani:AN5210.2. |
Enzyme and pathway databases | |
| BRENDA | 2.7.1.40. 3859. |
Family and domain databases | |
| InterPro | IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. [Graphical view] |
| Gene3D | G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit. |
| PANTHER | PTHR11817. Pyruvate_kinase. 1 hit. |
| Pfam | PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view] |
| PRINTS | PR01050. PYRUVTKNASE. |
| ProDom | PD001009. Pyruvate_kinase. 2 hits. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01064. pyruv_kin. 1 hit. |
| PROSITE | PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_EMENI | ||||||||
| Accession | Primary (citable) accession number: P22360 Secondary accession number(s): Q5B2M0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


