F0M8W2 · F0M8W2_PSEPM
- ProteinPyruvate carboxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1131 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
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
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 200 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 235 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 296 | |||||
Sequence: R | ||||||
Binding site | 537 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 609 | substrate | ||||
Sequence: R | ||||||
Binding site | 707 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 736 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 738 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 871 | 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
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate carboxylase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Pseudarthrobacter
Accessions
- Primary accessionF0M8W2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 707 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1097 | N6-biotinyllysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-454 | Biotin carboxylation | ||||
Sequence: MFSKVLVANRGEIAIRAFRAGYELGAKTVAVFPQEDRNSIHRQKADEAYLIGEEGHPVRAYLDVDEVVRVAKESGADAIYPGYGFLSENPDLARAAKAAGITFVGPPAEVLELAGNKVAALKAARDAGVPVLKSSAPSKDLDELIAAADEIGFPIFAKAVAGGGGRGMRRVDTREALPEALQSAMREADAAFGDPTMFLEQAVLRPRHIEVQILADAQGNVMHLFERDCSIQRRHQKVIEIAPAPNLDENIRQALYRDAVKFAQALNYVNAGTVEFLVDTVGERAGQHVFIEMNPRIQVEHTVTEEVTDVDLVQAQMRIAAGETLADLGLSQDTVRLRGAALQSRITTEDPANGFRPDVGKITGYRSAGGAGVRLDGGTVYSGAEISPHFDSMLVKLTCRGRDYPSAVARARRALAEFRIRGVSTNISFLQAVLDDPDFIAGDVATSFIDERPQ | ||||||
Domain | 121-321 | ATP-grasp | ||||
Sequence: LKAARDAGVPVLKSSAPSKDLDELIAAADEIGFPIFAKAVAGGGGRGMRRVDTREALPEALQSAMREADAAFGDPTMFLEQAVLRPRHIEVQILADAQGNVMHLFERDCSIQRRHQKVIEIAPAPNLDENIRQALYRDAVKFAQALNYVNAGTVEFLVDTVGERAGQHVFIEMNPRIQVEHTVTEEVTDVDLVQAQMRIAA | ||||||
Domain | 528-797 | Pyruvate carboxyltransferase | ||||
Sequence: VAVTDTTFRDAHQSLLATRVRTRDLVAAGPAVTALMPELLSVEAWGGATYDVALRFLGEDPWDRLAALRAAMPNVCIQMLLRGRNTVGYTPYPEEVTEAFVNEAAATGIDIFRIFDALNDVSQMAPAIRAVRATGTAVAEVALCYTGDMLDPEEKLYTLDYYLELAQRIVDAGAHILAIKDMAGLLRPAAAAKLVSALRERFDLPVHLHTHDTAGGQLATLLAAVDAGVDAVDVASASLAGTTSQPSASALVAALAHTPRDTGLSLAAVS | ||||||
Domain | 1057-1131 | Lipoyl-binding | ||||
Sequence: KADPGQPGQVAAPFAGAVTVTVKPGDEVKAGDTVATIEAMKMEASITTPVAGKVSRLAISAVEQVEGGDLLLVVE |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,131
- Mass (Da)121,405
- Last updated2011-05-03 v1
- ChecksumD3C302CB351FF197
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002379 EMBL· GenBank· DDBJ | ADX72697.1 EMBL· GenBank· DDBJ | Genomic DNA |