P77983 (KPYK1_SALTY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
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 I EC=2.7.1.40 Alternative name(s): PK-1 | ||||
| Gene names |
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| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 99287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 470 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 | Belongs to type I PK; fructose 1,6-bisphosphate-activated. |
| 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 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 – 470 | 470 | Pyruvate kinase I | PRO_0000112072 | |||||
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 | 222 | 1 | Magnesium By similarity | ||||||
| Metal binding | 246 | 1 | Magnesium By similarity | ||||||
| Binding site | 32 | 1 | Substrate By similarity | ||||||
| Binding site | 245 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 246 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 278 | 1 | Substrate By similarity | ||||||
| Site | 220 | 1 | Transition state stabilizer By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 142 | 1 | V → C in CAA68205. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12." Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W. J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X99945 Genomic DNA. Translation: CAA68205.1. AE006468 Genomic DNA. Translation: AAL20302.1. |
| RefSeq | NP_460343.1. NC_003197.1. |
3D structure databases | |
| ProteinModelPortal | P77983. |
| SMR | P77983. Positions 1-470. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 99287.STM1378. |
Proteomic databases | |
| PaxDb | P77983. |
| PRIDE | P77983. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL20302; AAL20302; STM1378. |
| GeneID | 1252896. |
| KEGG | stm:STM1378. |
| PATRIC | 32381237. VBISalEnt20916_1461. |
Phylogenomic databases | |
| eggNOG | COG0469. |
| HOGENOM | HOG000021559. |
| KO | K00873. |
| OMA | VKMMATI. |
| ProtClustDB | PRK09206. |
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. 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 | KPYK1_SALTY | ||||||||
| Accession | Primary (citable) accession number: P77983 | ||||||||
| 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
