Q8P8J2 · AOTC_XANCP
- ProteinN-acetylornithine carbamoyltransferase
- GeneargF'
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids339 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- carbamoyl phosphate + N2-acetyl-L-ornithine = H+ + N2-acetyl-L-citrulline + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Carboxylation at Lys-302 increases the catalytic activity of the enzyme (PubMed:20695527).
Is potently inhibited by N(alpha)-acetyl-N(delta)-phosphonoacetyl-L-ornithine (PALAO) (PubMed:16585758).
Is potently inhibited by N(alpha)-acetyl-N(delta)-phosphonoacetyl-L-ornithine (PALAO) (PubMed:16585758).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.01 mM | carbamoyl phosphate | |||||
1.05 mM | N2-acetyl-L-ornithine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
65.28 μmol/min/mg | towards N2-acetyl-L-ornithine | ||||
50.68 μmol/min/mg | towards carbamoyl phosphate |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Xanthomonas
Accessions
- Primary accessionQ8P8J2
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 92 | Generates an enzyme capable of carbamoylation of N-succinyl-L-ornithine while losing its ability to use N-acetyl-L-ornithine as substrate, thus converting it from a N-acetylornithine transcarbamylase (AOTCase) to a N-succinylornithine transcarbamylase (SOTCase). | ||||
Sequence: E → A, P, S, or V | ||||||
Mutagenesis | 302 | Significant decrease in enzymatic activity. | ||||
Sequence: K → A, E, or R |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000113268 | 1-339 | N-acetylornithine carbamoyltransferase | |||
Sequence: MSLKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRTRTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVLGRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPCQELAHALALQEHFGTPDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMGMDVTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVYAKSWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRNVKATDAVMDSPNCIAIDEAENRLHVQKAIMAALVGQSRP | ||||||
Modified residue | 302 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)37,873
- Last updated2002-10-01 v1
- Checksum8FEFBA16773A00D5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE008922 EMBL· GenBank· DDBJ | AAM41528.1 EMBL· GenBank· DDBJ | Genomic DNA |