Reviewed,
UniProtKB/Swiss-Prot Q4L739 (KPYK_STAHJ)
Last modified
June 16, 2009.
Version 27.
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 | Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279808 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 586 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 By similarity. Potassium By similarity. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. |
| Sequence similarities | Belongs to the pyruvate kinase family. In the C-terminal section; belongs to the PEP-utilizing enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW phosphorylationInferred from electronic annotation. Source: InterPro |
| 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)
Sequences
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References
| [1] | "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AP006716 Genomic DNA. Translation: BAE04536.1. | |
| RefSeq | YP_253142.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3481929. |
| GenomeReviews | Gene locus SH1227 in contig AP006716_GR. |
| KEGG | sha:SH1227. |
| NMPDR | fig|279808.3.peg.2549. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q4L739. |
| OMA | Q4L739. ATESGYT. |
Enzyme and pathway databases | |
| BioCyc | SHAE279808:SH1227-MON. |
Family and domain databases | |
| InterPro | IPR008279. PEP_mobile. 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:3.50.30.10. PEP_mobile. 1 hit. 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 | PF00391. PEP-utilizers. 1 hit. 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_STAHJ | ||||||||
| Accession | Primary (citable) accession number: Q4L739 | ||||||||
| 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 |

Clusters with


