A0A3M7QMR4 · A0A3M7QMR4_BRAPC
- ProteinPyruvate carboxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1196 (go to sequence)
- Protein existencePredicted
- 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 | 167 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 251 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 286 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 343 | |||||
Sequence: R | ||||||
Binding site | 590 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 662 | substrate | ||||
Sequence: R | ||||||
Binding site | 759 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 789 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 791 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 926 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | pyruvate carboxylase activity | |
Biological Process | gluconeogenesis | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Gnathifera > Rotifera > Eurotatoria > Monogononta > Pseudotrocha > Ploima > Brachionidae > Brachionus
Accessions
- Primary accessionA0A3M7QMR4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 759 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1161 | N6-biotinyllysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-501 | Biotin carboxylation | ||||
Sequence: PIKKLMVANRGEIAIRVFRACTELDIRTVAIYSEQDDGQVHRIKADESYLIGKGLPPVQAYLSIPEIIKIAKDNDVEAIHPGYGLLSESGEFAKACFENGIRFVGPSPDVMFRMGNKTEARKAAIEAGLKVIPGTANPISEVADAKKFAQEHGLPIIFKAAHGGGGRGMRVVRSMEELEENFQRATSEAKSAFGNGDVFIERFLEKPRHIEVQIMGDKYNNVVHLYERDCSVQRRHQKVIEIAPAPSLPVEIRDRITSDAVRLAQHVGYQNAGTVEFLLDSSGQNFFIEVNARLQVEHTVTEEITGVDLVQTQIRVAEGHSLKDLNLEQKDIKVHGSALQCRMTTEDPAKNFQPDNGRIEVYRSGEGMGIRIDSANAFTGAVITPYYDSLLVKIIAHAKDHPSACSKMIRALKEFRIRGIKTNIPYLLNVLQNKQFLEGSVDTSFIDQNPD | ||||||
Domain | 171-368 | ATP-grasp | ||||
Sequence: RKAAIEAGLKVIPGTANPISEVADAKKFAQEHGLPIIFKAAHGGGGRGMRVVRSMEELEENFQRATSEAKSAFGNGDVFIERFLEKPRHIEVQIMGDKYNNVVHLYERDCSVQRRHQKVIEIAPAPSLPVEIRDRITSDAVRLAQHVGYQNAGTVEFLLDSSGQNFFIEVNARLQVEHTVTEEITGVDLVQTQIRVAE | ||||||
Domain | 581-850 | Pyruvate carboxyltransferase | ||||
Sequence: LMLMDTTFRDAHQSLLATRVRTFDMKQIAPFVSNHFANLYSLECWGGATFDVSLRFLHECPWERLRELRKLIPNVPFQMLLRGANAVGYTNYPDNVVNEFCKLAVQNGMDVFRVFDSLNYVPNLVVGMDAVNNAGGIVEAAISYTGDVSDPTRTKYNLDYYVDVADQLVKAGAHVLSVKDMAGLLKPKATHMLIDAIRQRHPDVPIHLHTHDTAGTGVANYMAAAQAGCDIVDVAVDSMSGMTSQPSMGAVVASLQNTDRHTHIDLNSVF | ||||||
Domain | 1126-1195 | Lipoyl-binding | ||||
Sequence: KGSIGAPMPGTVIDVKCKEGDMVNKGDTLVVLSAMKMETVVKSPVSGKIVKLAVQNGQKLEGDDLLVEID |
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,196
- Mass (Da)132,829
- Last updated2019-02-13 v1
- Checksum342AB54A0C810733
Keywords
- Technical term