B8GF03 · PYRB_METPE
- ProteinAspartate carbamoyltransferase catalytic subunit
- GenepyrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids298 (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 | 50 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 79 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 100 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 128 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 131 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 160 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 221 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 260 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 261 | 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 > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanomicrobiales > Methanoregulaceae > Methanosphaerula
Accessions
- Primary accessionB8GF03
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000116150 | 1-298 | Aspartate carbamoyltransferase catalytic subunit | |||
Sequence: MKDFISIRDFDRAAIDRLIAEAERIDHHQYDPLEMKGKILALLFFEPSTRTRMSFEAAMARLGGTSLTLSSFEASSMAKGETLADTIRVVSGYVDAIVLRHPREGAARLASEVSSVPVINAGDGAGQHPSQTLLDLYTIRQSMPIDGINIGLLGDLRYGRTTHSLTYALSLYDAVIHTVAPAGLNLPSGLVHELRELGTEVIEHEQIEDVIKELDVLYVTRIQRERFPDTASYFNVASSYRITPELLRGTKEHMVVLHPLPRVDEIDPRVDKMKNARYFEQSHNGVPVRMAMLKQVIA |
Interaction
Subunit
Heterooligomer of catalytic and regulatory chains.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length298
- Mass (Da)33,265
- Last updated2009-03-03 v1
- Checksum755EFA648CD1F53E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001338 EMBL· GenBank· DDBJ | ACL17809.1 EMBL· GenBank· DDBJ | Genomic DNA |