Q3T9S7 · Q3T9S7_MOUSE
- ProteinPyruvate carboxylase
- GenePcx
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1179 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic activity
- hydrogencarbonate + pyruvate + ATP = oxaloacetate + ADP + phosphate + H+
Cofactor
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 153 | ATP (UniProtKB | ChEBI) | |||
Binding site | 237 | ATP (UniProtKB | ChEBI) | |||
Binding site | 272 | ATP (UniProtKB | ChEBI) | |||
Active site | 329 | ||||
Binding site | 573 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 645 | substrate | |||
Binding site | 742 | Mn2+ (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 772 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 774 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 909 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | pyruvate carboxylase activity | |
Biological Process | gluconeogenesis | |
Biological Process | lipid metabolic process | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate carboxylase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3T9S7
Organism-specific databases
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 742 | N6-carboxylysine | |||
Modified residue | 1145 | N6-biotinyllysine | |||
Proteomic databases
PTM databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length1,179
- Mass (Da)129,860
- Last updated2005-10-11 v1
- Checksum6B90E57D3F48C50F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK172320 EMBL· GenBank· DDBJ | BAE42943.1 EMBL· GenBank· DDBJ | mRNA |