O93918 · PYC_ASPTE
- ProteinPyruvate carboxylase
- Genepyc
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1193 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Pyruvate carboxylase 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
Protein has several cofactor binding sites:
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 243 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 278 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 335 | |||||
Sequence: R | ||||||
Binding site | 587-591 | substrate | ||||
Sequence: RDAHQ | ||||||
Binding site | 588 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 660 | substrate | ||||
Sequence: R | ||||||
Binding site | 756 | a divalent metal cation (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 786 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 788 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 921 | 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
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionO93918
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000146820 | 1-1193 | Pyruvate carboxylase | |||
Sequence: MAAPYRQPEEAVDDSEFIDDHHDHLRDTVHHRLRANSAIMQFQKILVANRGEIPIRIFRTAHELSLQTVAIFSHEDRLSMHRQKADEAYMIGHRGQYTPVGAYLAADEIVKIALEHGVHLIHPGYGFLSENADFARKVEKAGMVFVGPTPDTIDSLGDKVSARQLAIRCNVPVVPGTEGPVERYEEVKAFTDTYGFPIIIKAAFGGGGRGMRVVRNQADLRDSFERATSEARSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLFERDCSVQRRHQKVVEVAPAKDLPTDVRDRILSDAVKLAKSVNYRNAGTAEFLVDQQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGATLEQLGLTQDRISTRGFAIQCRITTEDPSKGFSPDTGKIEVYRSAGGNGVRLDGGNGFAGAIITPHYDSMLVKCTCRGSTYEIARRKVVRALVEFRIRGVKTNIPFLTSLLSHPTFVDGNCWTTFIDDTPELFALVGSQNRAQKLLAYLGDVAVNGSSIKGQMGEPKFKGEIIKPKLLDAQGKPLDVSQPCTKGWKQIIDQEGPVAFAKAVRANKGCLIMDTTWRDAHQSLLATRVRTIDLLNIAHETSHALSNAYSLECWGGATFDVAMRFLYEDPWDRLRKMRKAVPNIPFQMLLRGANGVAYSSLPDNAIYHFCKNAKKCGVDIFRVFDALNDIDQLEVGIKAVHAAEGVVEATVCYSGDMLNPKKKYNLEYYLALVDKIVALKPHVLGIKDMAGVLKPQAARLLVGSIRERYPDLPIHVHTHDSAGTGVASMIACAQAGADAVDAATDSMSGMTSQPSIGAILASLEGTEHDPGLNSAHVRALDSYWAQLRLLYSPFEANLTGPDPEVYEHEIPGGQLTNLIFQASQLGLGQQWAETKKAYEVANDLLGDIVKVTPTSKVVGDLAQFIVSNKLSAQDVVDRAAELDFPGSVLEFLEGLMGQPFGGFPEPLRSRALRNRRKLDKRPGLYLEPLDLAAIKNQIREQFGSATEYDVASYAMYPKVFEDYKKFVQKYGDLSVLPTRYFLAKPEIGEEFHVELEKGKVLILKLLAIGPLSEQTGQREVFYEVNGEVRQVSIDDKKASIDNTARPKADVGDSSQVGAPMSGVVVEIRVHDGLEVKKGDPLAVLSAMKMEMVISAPHSGKVSGLLVKEGDSVDGQDLVCKITKA | ||||||
Modified residue | 756 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1157 | N6-biotinyllysine | ||||
Sequence: K |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-493 | Biotin carboxylation | ||||
Sequence: QFQKILVANRGEIPIRIFRTAHELSLQTVAIFSHEDRLSMHRQKADEAYMIGHRGQYTPVGAYLAADEIVKIALEHGVHLIHPGYGFLSENADFARKVEKAGMVFVGPTPDTIDSLGDKVSARQLAIRCNVPVVPGTEGPVERYEEVKAFTDTYGFPIIIKAAFGGGGRGMRVVRNQADLRDSFERATSEARSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLFERDCSVQRRHQKVVEVAPAKDLPTDVRDRILSDAVKLAKSVNYRNAGTAEFLVDQQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGATLEQLGLTQDRISTRGFAIQCRITTEDPSKGFSPDTGKIEVYRSAGGNGVRLDGGNGFAGAIITPHYDSMLVKCTCRGSTYEIARRKVVRALVEFRIRGVKTNIPFLTSLLSHPTFVDGNCWTTFIDDTPE | ||||||
Domain | 163-360 | ATP-grasp | ||||
Sequence: RQLAIRCNVPVVPGTEGPVERYEEVKAFTDTYGFPIIIKAAFGGGGRGMRVVRNQADLRDSFERATSEARSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLFERDCSVQRRHQKVVEVAPAKDLPTDVRDRILSDAVKLAKSVNYRNAGTAEFLVDQQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAA | ||||||
Domain | 579-847 | Pyruvate carboxyltransferase | ||||
Sequence: CLIMDTTWRDAHQSLLATRVRTIDLLNIAHETSHALSNAYSLECWGGATFDVAMRFLYEDPWDRLRKMRKAVPNIPFQMLLRGANGVAYSSLPDNAIYHFCKNAKKCGVDIFRVFDALNDIDQLEVGIKAVHAAEGVVEATVCYSGDMLNPKKKYNLEYYLALVDKIVALKPHVLGIKDMAGVLKPQAARLLVGSIRERYPDLPIHVHTHDSAGTGVASMIACAQAGADAVDAATDSMSGMTSQPSIGAILASLEGTEHDPGLNSAHVR | ||||||
Domain | 1116-1191 | Biotinyl-binding | ||||
Sequence: KADVGDSSQVGAPMSGVVVEIRVHDGLEVKKGDPLAVLSAMKMEMVISAPHSGKVSGLLVKEGDSVDGQDLVCKIT |
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,193
- Mass (Da)131,222
- Last updated1999-05-01 v1
- Checksum6E24E000CE793206