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A0A0A0NKV8 · A0A0A0NKV8_STRRN

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site9-12NADP+ (UniProtKB | ChEBI)
Binding site37-38NADP+ (UniProtKB | ChEBI)
Binding site97phosphate (UniProtKB | ChEBI)
Active site127Acyl-thioester intermediate
Binding site154substrate
Binding site157-158NADP+ (UniProtKB | ChEBI)
Binding site246substrate
Active site253Proton acceptor
Binding site320NADP+ (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
    • ORF names
      D3C57_111690

Organism names

Accessions

  • Primary accession
    A0A0A0NKV8

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-117Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    341
  • Mass (Da)
    36,129
  • Last updated
    2015-02-04 v1
  • MD5 Checksum
    6078F4412EBB368393D1884D54D1279F
MRIGIVGATGQVGGVMRRVLAERDFPAEQLRLFASARSAGRTLPWRGTEITVEDAATADYSGLDIVLFSAGGATSRALAEKVAAQGPVVIDNSSAWRMDPEVPLVVAEVNPHAAVDRPKGIIANPNCTTMAAMPVLRPLHTEAGLTALVATTYQAVSGSGLSGVAELDGQIRKTADRAAELTHDGAAVEFPEPGVYARPIAFNVLPMAGKIVDDGRFETDEEQKLRNESRKILEIPELKVSGTCVRVPVFTGHSLQVNARFERPISVERAYELLAAAPGVALSEIPTPLQAAGQDPSYVGRIRVDETVEHGLALFLSNDNLRKGAALNAVQIAELVAADLT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QYCY01000001
EMBL· GenBank· DDBJ
RLV79041.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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