A0A8B6LEM0 · A0A8B6LEM0_9BURK
- ProteinPhosphoenolpyruvate carboxykinase [GTP]
- GenepckG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic activity
- GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Cofactor
Note: Binds 1 Mn2+ ion per subunit.
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 83 | substrate | ||||
Sequence: R | ||||||
Binding site | 222-224 | substrate | ||||
Sequence: YGG | ||||||
Binding site | 231 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 251 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 273 | substrate | ||||
Sequence: S | ||||||
Binding site | 274-279 | GTP (UniProtKB | ChEBI) | ||||
Sequence: ACGKTN | ||||||
Active site | 275 | |||||
Sequence: C | ||||||
Binding site | 300 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 393-395 | substrate | ||||
Sequence: NAR | ||||||
Binding site | 395 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 426 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 523-526 | GTP (UniProtKB | ChEBI) | ||||
Sequence: YGEN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | GTP binding | |
Molecular Function | kinase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | phosphoenolpyruvate carboxykinase (GTP) activity | |
Biological Process | cellular response to glucose stimulus | |
Biological Process | gluconeogenesis | |
Biological Process | glycerol biosynthetic process from pyruvate | |
Biological Process | propionate catabolic process | |
Biological Process | response to lipid | |
Biological Process | response to starvation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoenolpyruvate carboxykinase [GTP]
- EC number
- Short namesPEP carboxykinase ; PEPCK
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Variovorax
Accessions
- Primary accessionA0A8B6LEM0
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-243 | Phosphoenolpyruvate carboxykinase GTP-utilising N-terminal | ||||
Sequence: WVADMAALCKPESIHWCDGSSEEYERLCQQMVEAGTLKKLNPAKRPNSYLASSDPGDVARVEDRTFICAPRKEDAGPTNNWMAPADMRATLQPLFDGSMKGRTMYVVPFSMGPLGSPIAHIGIELSDSPYVAVNMKIMTRMGKAVYDVLGADGDFVPCVHTVGAPLEPGQKDVSWPCNKTKYIVHYPETREIWSYGSGYGGNALLGKKCFALRIASNMGR | ||||||
Domain | 247-608 | Phosphoenolpyruvate carboxykinase C-terminal P-loop | ||||
Sequence: WLAEHMLILGVTNPAGRKYHVAAAFPSACGKTNFAMLIPPAGFEGWKVTTIGDDIAWIKPGADGKLHAINPEAGYFGVAPGTNTLTNPNCMASLDRDVIFTNVALTDDGDVWWEGMSEPPAHAIDWQGKDWTPAIARETGAKAAHPNARFTVAATNNPALDDAWDDPKGVAIDAFIFGGRRSTTVPLVTEARDWVEGVYMAATMGSETTAAAAGQQGVVRRDPFAMLPFAGYNMSDYFQHWLDLGKKLEASDARLPKIYTTNWFRKGEDGKFVWPGYGENMRVLKWMIDRVEQKAEGVEHVFGVSPRYEDLDWTGLDFSARQFDTVTSIDKAAWHAELKLHAELFQQLAHHLPKELPAIKAA |
Sequence similarities
Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length615
- Mass (Da)67,400
- Last updated2021-09-29 v1
- ChecksumF36B39C81A9D7326