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Q9ZDL2 · DHAS_RICPR

Function

function

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site13-16NADP+ (UniProtKB | ChEBI)
Binding site41-42NADP+ (UniProtKB | ChEBI)
Binding site101phosphate (UniProtKB | ChEBI)
Active site132Acyl-thioester intermediate
Binding site159substrate
Binding site162-163NADP+ (UniProtKB | ChEBI)
Binding site187NADP+ (UniProtKB | ChEBI)
Binding site216phosphate (UniProtKB | ChEBI)
Binding site237substrate
Active site244Proton acceptor
Binding site317NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionaspartate-semialdehyde dehydrogenase activity
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Molecular Functionprotein dimerization activity
Biological Process'de novo' L-methionine biosynthetic process
Biological Processdiaminopimelate biosynthetic process
Biological Processisoleucine biosynthetic process
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processthreonine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate-semialdehyde dehydrogenase
  • EC number
  • Short names
    ASA dehydrogenase
    ; ASADH
  • Alternative names
    • Aspartate-beta-semialdehyde dehydrogenase

Gene names

    • Name
      asd
    • Ordered locus names
      RP316

Organism names

Accessions

  • Primary accession
    Q9ZDL2

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001413881-338Aspartate-semialdehyde dehydrogenase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    338
  • Mass (Da)
    37,668
  • Last updated
    1999-05-01 v1
  • MD5 Checksum
    210E1AAAEDB939D23C43AF3AC19767D7
MTKKYNIAVIGATGNVGRETLNILAERHFPINKIYAIASDNSLGREVRFGEKILHINSIKIFNFHDIEIAFFCAGSNVSKEFIPKATSCNCIVIDKTSLFRADNQVPLIVPEVNLSTLKEFNTKNIIANPNCIVIPLVVVLKPLDNEIKIKRVVISTYQSVSGAGKAGMDELYNQTKSKYVFRENNPKKFPKQIAFNLFPYIGDLNKDGYTSEETKIAFELNKIMGNHFKTSVTSVRVPVFIGHAISVNIEFSDKIYAKDVEEILQDADGIVTISNNNGLAYISPIEVVGEDAVYVSRIRNDLSKDNTINLWITCDNLRKGAALNSVQIAEALINNYL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ235271
EMBL· GenBank· DDBJ
CAA14776.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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