Q89AI8 (KPYK_BUCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 73.
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 | Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224915 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › ![]() |
Protein attributes
| Sequence length | 479 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + pyruvate = ADP + phosphoenolpyruvate. |
| Cofactor | Magnesium By similarity. Potassium By similarity. |
| Enzyme regulation | Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK By similarity. |
| 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 Potassium Pyruvate |
| Molecular function | Kinase Transferase |
| Technical term | Allosteric enzyme 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 – 479 | 479 | Pyruvate kinase | PRO_0000112060 | |||||
Sites | |||||||||
| Metal binding | 38 | 1 | Potassium By similarity | ||||||
| Metal binding | 40 | 1 | Potassium By similarity | ||||||
| Metal binding | 70 | 1 | Potassium By similarity | ||||||
| Metal binding | 225 | 1 | Magnesium By similarity | ||||||
| Metal binding | 252 | 1 | Magnesium By similarity | ||||||
| Binding site | 36 | 1 | Substrate By similarity | ||||||
| Binding site | 251 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 252 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 284 | 1 | Substrate By similarity | ||||||
| Site | 223 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016826 Genomic DNA. Translation: AAO27022.1. |
| RefSeq | NP_777917.1. NC_004545.1. |
3D structure databases | |
| ProteinModelPortal | Q89AI8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224915.bbp297. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAO27022; AAO27022; bbp_297. |
| GeneID | 1058264. |
| KEGG | bab:bbp297. |
| PATRIC | 21245381. VBIBucAph80364_0293. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0469. |
| KO | K00873. |
| OMA | SHTICIA. |
Enzyme and pathway databases | |
| BioCyc | BAPH224915:GJ9D-297-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 | IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KPYK_BUCBP | ||||||||
| Accession | Primary (citable) accession number: Q89AI8 | ||||||||
| 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
