A0A1V4XDX2 · A0A1V4XDX2_9BACT

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 site12-15NADP+ (UniProtKB | ChEBI)
Binding site40-41NADP+ (UniProtKB | ChEBI)
Binding site100phosphate (UniProtKB | ChEBI)
Active site131Acyl-thioester intermediate
Binding site158substrate
Binding site161-162NADP+ (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
      asd2
    • Synonyms
      asd
    • ORF names
      A4E67_01142

Organism names

Accessions

  • Primary accession
    A0A1V4XDX2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-120Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    37,461
  • Last updated
    2017-06-07 v1
  • Checksum
    8387E418BA89934E
MRTYRVAVVGATGAVGNEMISILEERDFPVGELRLLASERSIGKELEFKGKAYPVQVLKEDSFEGIEIGLFSAGGSISQRFAPFAAKAGCVVIDNTAAFRYEPDIPLVVPEVNPGKIADYKNRRIIANPNCSTIQMVVALKPIHDAVRIKRIVVSTYQSVSGTGKKAMDELIDQTRALLSFKEPVAKVYPYQIAFNCLPQIDIFLENGYTKEEMKMVWETKKIFGDESIAVTATTVRVPVLRAHSESVNIETEKKITAAEVRELLRKAPGVVVVDDPAKREYPLAINAAGKDATYVGRIREDESIPNGINLWIVSDNLRKGAALNAIQIAEIYAREYLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MVQS01000206
EMBL· GenBank· DDBJ
OPY07792.1
EMBL· GenBank· DDBJ
Genomic DNA

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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