P32044 (KPYK_THEAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 86.
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 | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP] | ||
| Taxonomic identifier | 273075 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › ![]() |
Protein attributes
| Sequence length | 544 AA. |
| Sequence status | Complete. |
| 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. |
| Sequence similarities | Belongs to the pyruvate kinase family. |
| Caution | Ref.2 has published some partial sequence, these sequences do not originate from T.acidophilum, rather they seem to be contaminated with human samples. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Reference 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 – 544 | 544 | Pyruvate kinase | PRO_0000112129 | |||||
Sites | |||||||||
| Metal binding | 33 | 1 | Potassium By similarity | ||||||
| Metal binding | 61 | 1 | Potassium By similarity | ||||||
| Metal binding | 204 | 1 | Magnesium By similarity | ||||||
| Metal binding | 228 | 1 | Magnesium By similarity | ||||||
| Binding site | 31 | 1 | Substrate By similarity | ||||||
| Binding site | 227 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 228 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 260 | 1 | Substrate By similarity | ||||||
| Site | 202 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W. Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165. |
| [2] | "Purification and properties of pyruvate kinase from Thermoplasma acidophilum." Potter S., Fothergill-Gilmore L.A. FEMS Microbiol. Lett. 73:235-239(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL445065 Genomic DNA. Translation: CAC12025.1. |
| RefSeq | NP_394355.1. NC_002578.1. |
3D structure databases | |
| ProteinModelPortal | P32044. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 273075.Ta0896. |
Proteomic databases | |
| PRIDE | P32044. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAC12025; CAC12025; CAC12025. |
| GeneID | 1456432. |
| KEGG | tac:Ta0896. |
Phylogenomic databases | |
| eggNOG | COG0469. |
| HOGENOM | HOG000021559. |
| KO | K00873. |
| OMA | NSGYTAR. |
| ProtClustDB | PRK05826. |
Enzyme and pathway databases | |
| 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 | IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. 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 | PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view] |
| PRINTS | PR01050. PYRUVTKNASE. |
| SUPFAM | 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_THEAC | ||||||||
| Accession | Primary (citable) accession number: P32044 | ||||||||
| 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
