Q0AXG1 · PYRB_SYNWW
- ProteinAspartate carbamoyltransferase catalytic subunit
- GenepyrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids312 (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 = N-carbamoyl-L-aspartate + phosphate + H+
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 | 58 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 59 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 86 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 108 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 136 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 139 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 169 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 223 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 264 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 265 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 lineageBacteria > Bacillota > Clostridia > Eubacteriales > Syntrophomonadaceae > Syntrophomonas
Accessions
- Primary accessionQ0AXG1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000000023 | 1-312 | Aspartate carbamoyltransferase catalytic subunit | |||
Sequence: MKLDRKDLLGLRDLSREETELILNTAIPMKDVICRDIKKVPTLRGKALVTVFYENSTRTRTSFELAGKYLSADTVNLSVSTSSVQKGESLRDTIKTIEVMGFDLMVMRHAMSGTPHYVARNTRMRVINAGDGANEHPTQALLDMYTIKEKKGTLESLKVAIVGDILHSRVARSNIYGLSKFGCDIRVVGPATLMPPGIEKLGVKSYYSLDEAINGVDVINILRIQRERQVSGLFPSLDEYAQLYMLSPQTLARAKDDVLVLHPGPINRGVEISSELADSAQALINEQVTNGVAIRMALLFLMMGGGRDEITY |
Interaction
Subunit
Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length312
- Mass (Da)34,503
- Last updated2006-10-17 v1
- Checksum31244E2C5C5C8A68
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000448 EMBL· GenBank· DDBJ | ABI68593.1 EMBL· GenBank· DDBJ | Genomic DNA |