Q9HKM2 · PYRB_THEAC
- ProteinAspartate carbamoyltransferase catalytic subunit
- GenepyrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids305 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.
Catalytic activity
- carbamoyl phosphate + L-aspartate = H+ + N-carbamoyl-L-aspartate + phosphate
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 56 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 57 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 85 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 106 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 134 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 137 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 167 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 227 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 266 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 267 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | amino acid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate carbamoyltransferase catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Candidatus Thermoplasmatota > Thermoplasmata > Thermoplasmatales > Thermoplasmataceae > Thermoplasma
Accessions
- Primary accessionQ9HKM2
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000113261 | 1-305 | Aspartate carbamoyltransferase catalytic subunit | |||
Sequence: MLKNRSVVSIEDVDIDDLNDLFDLSDSMLKTIEKGGSTDLLRNRIMATLFYEPSTRTRLSFESAMHRLGGSVITVSDVKTSSVAKGETLADTIRMASSYSDIIVIRHPLEGAARLASKFANKPVINAGDGSGQHPTQTILDLYTIKRETGSIDGKTITMVGDLRYGRTIHSLIIALSRFDVRINLVSPQILKLPEYVLTKIGDRSRIMEYDDLSKVIEDTDVLYVTRIQKERFSDQNEYQSVIGSYSVDRDLVSRMKKDAIIMHPLPRIDEIKPEVDELPQARYFKQAYYGVPVRMALIYRILGD |
Proteomic databases
Interaction
Subunit
Heterooligomer of catalytic and regulatory chains.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length305
- Mass (Da)34,398
- Last updated2001-03-01 v1
- Checksum9CD3D48571A7D718
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL445064 EMBL· GenBank· DDBJ | CAC11715.1 EMBL· GenBank· DDBJ | Genomic DNA |