Q8P8J2 · AOTC_XANCP

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

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).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.01 mMcarbamoyl phosphate
1.05 mMN2-acetyl-L-ornithine
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
65.28 μmol/min/mgtowards N2-acetyl-L-ornithine
50.68 μmol/min/mgtowards carbamoyl phosphate

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site49-52carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site77carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits
Site92Key residue in conferring substrate specificity for N-acetyl-L-ornithine versus N-succinyl-L-ornithine
Binding site112carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site144N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site148-151carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site252N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site294-295carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain
Binding site295N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site322carbamoyl phosphate (UniProtKB | ChEBI); ligand shared between two neighboring subunits; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionamino acid binding
Molecular FunctionN-acetylornithine carbamoyltransferase activity
Molecular Functionornithine carbamoyltransferase activity
Biological Processarginine biosynthetic process via ornithine
Biological Processcitrulline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    N-acetylornithine carbamoyltransferase
  • EC number
  • Alternative names
    • N-acetyl-L-ornithine transcarbamylase
      (AOTCase
      ; Acetylornithine transcarbamylase
      )

Gene names

    • Name
      argF'
    • Ordered locus names
      XCC2249

Organism names

Accessions

  • Primary accession
    Q8P8J2

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis92Generates 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).
Mutagenesis302Significant decrease in enzymatic activity.

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001132681-339N-acetylornithine carbamoyltransferase
Modified residue302N6-carboxylysine

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    37,873
  • Last updated
    2002-10-01 v1
  • Checksum
    8FEFBA16773A00D5
MSLKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRTRTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVLGRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPCQELAHALALQEHFGTPDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMGMDVTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVYAKSWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRNVKATDAVMDSPNCIAIDEAENRLHVQKAIMAALVGQSRP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE008922
EMBL· GenBank· DDBJ
AAM41528.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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