A0A0D6QDR4 · A0A0D6QDR4_KOMXY

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.

TypeIDPosition(s)Description
Binding site11-14NADP+ (UniProtKB | ChEBI)
Binding site39-40NADP+ (UniProtKB | ChEBI)
Binding site100phosphate (UniProtKB | ChEBI)
Active site130Acyl-thioester intermediate
Binding site157substrate
Binding site182NADP+ (UniProtKB | ChEBI)
Binding site235substrate
Active site242Proton acceptor
Binding site315NADP+ (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
      Gxy13693_239_020

Organism names

Accessions

  • Primary accession
    A0A0D6QDR4

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-120Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    36,712
  • Last updated
    2015-05-27 v1
  • Checksum
    568D06CE7E9523CF
MGYRVAVVGATGAVGREILKTLAERQFPVDEIVALASARSAGKEVSFGDKKVLKVQNLETFDFTGWDVALFSPGGAVSAVHAPRAAKAGCIVIDNTSHFRMEPDVPLVVPEVNPNDVKKARRGIIANPNCSTIQMVVALKPLHDLFTIKRVVVATYQAVAGAGKSGMDELFNQSRGSLVGDPLKAEQFTKQIAFNCIPHIDRFMDDGATKEEWKMTVETRKILDPDIAVFATCVRVPVFIGHAEAISVEFEEPVDIKRAREALREAPGVVLHDKREDGGYATPLEIVGEDATYVSRLRIDPTVPNGLGFWCVADNLRKGAALNAVQIAETMVALDLLGH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BANJ01000189
EMBL· GenBank· DDBJ
GAO01136.1
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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