Reviewed,
UniProtKB/Swiss-Prot Q10208 (KPYK_SCHPO)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 | Schizosaccharomyces pombe (Fission yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4896 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + pyruvate = ADP + phosphoenolpyruvate. |
| Cofactor | Magnesium. Potassium. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. |
| Subunit structure | Homotetramer By similarity. |
| 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 | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytosol Inferred from direct assay. Source: GeneDB_SPombe |
| 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 – 509 | 509 | Pyruvate kinase | PRO_0000112118 | |||||
Sites | |||||||||
| Active site | 247 | 1 | By similarity | ||||||
| Metal binding | 249 | 1 | Magnesium Potential | ||||||
| Metal binding | 270 | 1 | Magnesium Potential | ||||||
| Metal binding | 271 | 1 | Magnesium Potential | ||||||
| Binding site | 344 | 1 | ADP Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 29 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 63 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 281 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 412 | 1 | Phosphoserine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 391 | 1 | A → R in CAA62490. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe; implications for quaternary structure and regulation of the enzyme." Nairn J., Smith S., Allison P.J., Rigden D., Fothergill-Gilmore L.A., Price N.C. FEMS Microbiol. Lett. 134:221-226(1995) [PubMed: 8586271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972. |
| [3] | "Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-63; SER-281 AND SER-412, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| X91008 mRNA. Translation: CAA62490.1. CU329670 Genomic DNA. Translation: CAA93349.1. | |
| PIR | T38890. T45166. |
| RefSeq | NP_594346.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A3W based on UniProtKB P00549. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2543557. |
| KEGG | spo:SPAC4H3.10c. |
| NMPDR | fig|4896.1.peg.4316. |
Organism-specific databases | |
| GeneDB_Spombe | SPAC4H3.10c. |
Phylogenomic databases | |
| OMA | Q10208. WIPGSGH. |
Enzyme and pathway databases | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-002453-MON. |
| BRENDA | 2.7.1.40. 653. |
Gene expression databases | |
| ArrayExpress | Q10208. |
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_SCHPO | ||||||||
| Accession | Primary (citable) accession number: Q10208 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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