Q99TG5 (KPYK_STAAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
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: Pyruvate kinase Short name=PK EC=2.7.1.40 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 158878 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 585 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 Potassium Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: InterPro 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 – 585 | 585 | Pyruvate kinase | PRO_0000294132 | |||||
Sites | |||||||||
| Metal binding | 34 | 1 | Potassium By similarity | ||||||
| Metal binding | 36 | 1 | Potassium By similarity | ||||||
| Metal binding | 66 | 1 | Potassium By similarity | ||||||
| Metal binding | 67 | 1 | Potassium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 221 | 1 | Magnesium By similarity | ||||||
| Metal binding | 245 | 1 | Magnesium By similarity | ||||||
| Binding site | 32 | 1 | Substrate By similarity | ||||||
| Binding site | 244 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 245 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 277 | 1 | Substrate By similarity | ||||||
| Site | 219 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000017 Genomic DNA. Translation: BAB57859.1. |
| RefSeq | NP_372221.1. NC_002758.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LIU based on UniProtKB P30613. |
| ProteinModelPortal | Q99TG5. |
| SMR | Q99TG5. Positions 1-583. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158878.SAV1697. |
2D gel databases | |
| World-2DPAGE | 0002:Q99TG5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB57859; BAB57859; SAV1697. |
| GeneID | 1121672. |
| KEGG | sav:SAV1697. |
| PATRIC | 19564146. VBIStaAur52173_1751. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0469. |
| HOGENOM | HOG000021559. |
| KO | K00873. |
| OMA | NSGYTAR. |
| ProtClustDB | CLSK885504. |
Enzyme and pathway databases | |
| BioCyc | SAUR158878:GJJ5-1713-MONOMER. |
| UniPathway | UPA00109; UER00188. |
Family and domain databases | |
| Gene3D | 2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit. |
| InterPro | IPR008279. PEP-util_enz_mobile_dom. IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view] |
| PANTHER | PTHR11817. PTHR11817. 1 hit. |
| Pfam | PF00391. PEP-utilizers. 1 hit. PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view] |
| PRINTS | PR01050. PYRUVTKNASE. |
| SUPFAM | SSF52009. PEP_mobile. 1 hit. SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR01064. pyruv_kin. 1 hit. |
| PROSITE | PS00110. PYRUVATE_KINASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_STAAM | ||||||||
| Accession | Primary (citable) accession number: Q99TG5 | ||||||||
| 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
