P21599 · KPYK2_ECOLI
- ProteinPyruvate kinase II
- GenepykA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids480 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.
Catalytic activity
- ATP + pyruvate = ADP + H+ + phosphoenolpyruvateThis reaction proceeds in the backward direction.
Cofactor
Protein has several cofactor binding sites:
Activity regulation
Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36 | substrate | ||||
Sequence: R | ||||||
Binding site | 38 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 38-41 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NFSH | ||||||
Binding site | 40 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 70 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 77 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 160 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 223 | substrate | ||||
Sequence: K | ||||||
Site | 223 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 225 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 251 | substrate | ||||
Sequence: G | ||||||
Binding site | 252 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | substrate | ||||
Sequence: D | ||||||
Binding site | 284 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | pyruvate kinase complex | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | kinase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | potassium ion binding | |
Molecular Function | pyruvate kinase activity | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate kinase II
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP21599
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000112073 | 2-480 | Pyruvate kinase II | |||
Sequence: SRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAKLGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPADVVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKADIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDIILASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAEVMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDNVEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALYRGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE | ||||||
Modified residue | 351 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P21599 | lnt P23930 | 3 | EBI-368956, EBI-556569 | |
BINARY | P21599 | malX P19642 | 4 | EBI-368956, EBI-556578 | |
BINARY | P21599 | pykA P21599 | 3 | EBI-368956, EBI-368956 | |
BINARY | P21599 | usg P08390 | 3 | EBI-368956, EBI-548921 | |
BINARY | P21599 | yggR P52052 | 4 | EBI-368956, EBI-552531 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length480
- Mass (Da)51,357
- Last updated2007-01-23 v3
- ChecksumC37F004C374D27E9
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 20 | in Ref. 7; AA sequence | ||||
Sequence: R → C | ||||||
Sequence conflict | 43 | in Ref. 7; AA sequence | ||||
Sequence: S → G | ||||||
Sequence conflict | 323 | in Ref. 6; AAA96707 | ||||
Sequence: A → R | ||||||
Sequence conflict | 383 | in Ref. 6; AAA96707 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M63703 EMBL· GenBank· DDBJ | AAA24473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74924.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA15662.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M77039 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M87660 EMBL· GenBank· DDBJ | AAA96707.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift |