Q3TCQ3 · Q3TCQ3_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
- ATP + hydrogencarbonate + pyruvate = ADP + H+ + oxaloacetate + phosphate
Cofactor
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 153 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 237 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 272 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 329 | |||||
Sequence: R | ||||||
Binding site | 573 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 645 | substrate | ||||
Sequence: R | ||||||
Binding site | 742 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 772 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 774 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 909 | substrate | ||||
Sequence: T |
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 accessionQ3TCQ3
Organism-specific databases
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 742 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1145 | N6-biotinyllysine | ||||
Sequence: K |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-487 | Biotin carboxylation | ||||
Sequence: PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYKNAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPE | ||||||
Domain | 157-354 | ATP-grasp | ||||
Sequence: RAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYKNAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSE | ||||||
Domain | 564-833 | Pyruvate carboxyltransferase | ||||
Sequence: LLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVF | ||||||
Domain | 1110-1179 | Lipoyl-binding | ||||
Sequence: KGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE |
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,179
- Mass (Da)129,831
- Last updated2005-10-11 v1
- Checksum0108D0B6863AA676