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A0A2N4VNT8 · A0A2N4VNT8_9ENTR

  • Protein
    Acetylornithine/succinyldiaminopimelate aminotransferase
  • Gene
    argD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Involved in both the arginine and lysine biosynthetic pathways.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Note: Binds 1 pyridoxal phosphate per subunit.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 4/4.
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site105-106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site138pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site141N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site223-226pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site280N2-acetyl-L-ornithine (UniProtKB | ChEBI)
Binding site281pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionidentical protein binding
Molecular FunctionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionsuccinyldiaminopimelate transaminase activity
Biological Processarginine biosynthetic process
Biological Processarginine catabolic process
Biological Processlysine biosynthetic process via diaminopimelate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetylornithine/succinyldiaminopimelate aminotransferase
  • EC number
  • Short names
    ACOAT
    ; DapATase
    ; Succinyldiaminopimelate transferase

Gene names

    • Name
      argD
    • Synonyms
      dapC
    • ORF names
      DKC00_30925

Organism names

  • Taxonomic identifier
  • Strain
    • CAV2018
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0A2N4VNT8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue252N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    406
  • Mass (Da)
    43,447
  • Last updated
    2018-04-25 v1
  • MD5 Checksum
    5AC1F418023CD415A75BB428E1D1920A
MSQSITRNHFDEWMMPVYAPAAFIPVRGAGSRLWDQQGKEYIDFAGGIAVNALGHAHPRLVQALTDQAGKFWHTGNGYTNEPILRLAKMLIDATFADRVFFCNSGAEANEAALKLARKYAHDRFGSEKSGIVAFQNAFHGRTLFTVSAGGQPAYSRDFAPLPPQIQHAVFNDLASAKALINDQTCAVIVEPVQGEGGVVPASVEFLRGLRQLCDQHNALLIFDEVQTGVGRTGELYAYMHYGVTPDVLTTAKALGGGFPIGALLATEACASVMTVGTHGTTYGGNPLAGAVAGELLSIVNTPEVLSGVRQRHQWFCERLQAINARYGLFKEIRGLGLLIGCVLNDAWAGKAKTLSNLAAEEGVMILIAGANVVRFAPALNVSEEEVNSGLDRVERACARFLAGVSS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029432
EMBL· GenBank· DDBJ
AWL65834.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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