P22360 · KPYK_EMENI
- ProteinPyruvate kinase
- GenepkiA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids526 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- ATP + pyruvate = ADP + H+ + phosphoenolpyruvate
Cofactor
Protein has several cofactor binding sites:
Activity regulation
Regulated by phosphoenolpyruvate substrate and allosteric effectors such as fructose 1,6 diphosphate and magnesium.
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 | 63 | substrate | ||||
Sequence: R | ||||||
Binding site | 65 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 65-68 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NFSH | ||||||
Binding site | 67 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 98 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 99 | K+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 105 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 191 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 254 | Transition state stabilizer | ||||
Sequence: K | ||||||
Binding site | 256 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 279 | substrate | ||||
Sequence: G | ||||||
Binding site | 280 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 280 | substrate | ||||
Sequence: D | ||||||
Binding site | 312 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP 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
- EC number
- Short namesPK
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionP22360
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000112113 | 1-526 | Pyruvate kinase | |||
Sequence: MAASSSLDHLSNRMKLEWHSKLNTEMVPAKNFRRTSIICTIGPKTNSVEKINALRRAGLNVVRMNFSHGSYEYHQSVIDHAREAEKQQAGRPVAIALDTKGPEIRTGNTVGDKDIPIKAGHEMNISTDEQYATASDDQNMYVDYKNITKVISAGKLIYVDDGILSFEVLEVVDDKTLRVRCLNNGNISSRKGVNLPGTDVDLPALSEKDISDLKFGVKNKVDMVFASFIRRGSDIRHIREVLGEEGREIQIIAKIENQQGVNNFDEILEETDGVMVARGDLGIEIPAPKVFIAQKMMIAKCNIKGKPVICATQMLESMTYNPRPTRAEVSDVANAVLDGADCVMLSGETAKGNYPCEAVTMMSETCLLAEVAIPHFNVFDELRNLAPRPTDTVESIAMAAVSASLELNAGAIVVLTTSGNTARMISKYRPVCPIIMVSRNPAATRYSHLYRGVWPFYFPEKKPDFNVKIWQEDVDRRLKWGINHGLKLGIINKGDNIVCVQGWRGGMGHTNTVRVVPAEENLGLSE | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Length526
- Mass (Da)58,133
- Last updated2007-05-01 v2
- ChecksumBCD3A6F35F5D28B2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 88 | in Ref. 1; AAA33320 | ||||
Sequence: Q → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M36918 EMBL· GenBank· DDBJ | AAA33320.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AACD01000089 EMBL· GenBank· DDBJ | EAA62391.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BN001305 EMBL· GenBank· DDBJ | CBF81089.1 EMBL· GenBank· DDBJ | Genomic DNA |