Q9PEN0 · AOTC_XYLFA
- ProteinN-acetylornithine carbamoyltransferase
- GeneargF'
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids336 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N2-acetyl-L-ornithine to produce N2-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
Catalytic activity
- N2-acetyl-L-ornithine + carbamoyl phosphate = N2-acetyl-L-citrulline + phosphate + H+This reaction proceeds in the forward direction.
Activity regulation
Carboxylation at Lys-302 increases the catalytic activity of the enzyme.
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 49-52 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: SMRT | ||||||
Binding site | 77 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits | ||||
Sequence: W | ||||||
Site | 92 | Key residue in conferring substrate specificity for N-acetyl-L-ornithine versus N-succinyl-L-ornithine | ||||
Sequence: E | ||||||
Binding site | 112 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: R | ||||||
Binding site | 144 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 148-151 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: HPCQ | ||||||
Binding site | 252 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 294-295 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: CL | ||||||
Binding site | 295 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 322 | carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | amino acid binding | |
Molecular Function | N-acetylornithine carbamoyltransferase activity | |
Molecular Function | ornithine carbamoyltransferase activity | |
Biological Process | arginine biosynthetic process via ornithine | |
Biological Process | citrulline biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylornithine carbamoyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Xylella
Accessions
- Primary accessionQ9PEN0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000113269 | 1-336 | N-acetylornithine carbamoyltransferase | |||
Sequence: MALKHFLNTQDWSCSELNALLTQARAFKHNKLGNGLKGKSIALVFFNASMRTRSSFELGAFQLGGHAIVLQPGKDAWPIEFDTGTVMEAETEEHICEVARVLGHYVDLIGVRAFPKFLDWTYDRQDIVLNGFAKYSPVPVINMETITHPCQELAHIMALQEHFGTTDLRGKKYVLTWTYHPKPLNTAVANSALTIATRLGMDVTLLCPTPDYVLDERYIDWAQQNIADTGSTFQVSHDIDNAYRGADVIYAKSWGALPFFGNWAMEKPIRDQYRHFIVDEAKMALTNNAVFSHCLPLRRNVKATDAVMDGPNCIAIHEAGNRLHVQKAIMAALASQ | ||||||
Modified residue | 302 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)37,623
- Last updated2000-10-01 v1
- Checksum5B909F441AA37438
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE003849 EMBL· GenBank· DDBJ | AAF83808.1 EMBL· GenBank· DDBJ | Genomic DNA |