A0A1Q8SVT1 · A0A1Q8SVT1_9GAMM

  • Protein
    Aspartate-semialdehyde dehydrogenase
  • Gene
    asd
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site10-13NADP+ (UniProtKB | ChEBI)
Binding site37-38NADP+ (UniProtKB | ChEBI)
Binding site73NADP+ (UniProtKB | ChEBI)
Binding site102phosphate (UniProtKB | ChEBI)
Active site135Acyl-thioester intermediate
Binding site162substrate
Binding site165-166NADP+ (UniProtKB | ChEBI)
Binding site241substrate
Binding site244phosphate (UniProtKB | ChEBI)
Binding site268substrate
Active site275Proton acceptor
Binding site351NADP+ (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
      BTW07_04995

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SMB35
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Salinicola

Accessions

  • Primary accession
    A0A1Q8SVT1

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-122Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    371
  • Mass (Da)
    39,882
  • Last updated
    2017-04-12 v1
  • Checksum
    E24F7E867BE6526E
MLKVGFVGWRGMVGSVLMQRMLDDNDFAGLEPVFFSTSQAGQAGPNIGVDVPALKDANDIESLKTMDVIVTCQGGDYTGAVYQPLRQAGWKGYWIDAASTLRMAEESTIVLDPVNRHVIDAQLAKGARTFVGGNCTVSLMLMGLGGLFEANMVEWMTSMTYQAASGSGAKHMRELLSQMGALHSAVASDLATPSSAILDIDRDVTAAMRGGEFPVDNFGAPLAGSLLPWIDKAMDNGQSKEEWKGGVETNKILATGANPIPIDGLCVRIGAMRSHSQAFTIKLRQDVPLDEIEDRLARHNDWAKVVPNEKDATLEQLTPAAVSGTLTVPVGRLRKLSMGGEYLTAFSVGDQLLWGAAEPLKRMLKIVREQA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MSDO01000004
EMBL· GenBank· DDBJ
OLO05442.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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