A0A2N4U3C2 · A0A2N4U3C2_9BURK

  • 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.

TypeIDPosition(s)Description
Binding site11-14NADP+ (UniProtKB | ChEBI)
Binding site74NADP+ (UniProtKB | ChEBI)
Binding site103phosphate (UniProtKB | ChEBI)
Active site136Acyl-thioester intermediate
Binding site163substrate
Binding site166-167NADP+ (UniProtKB | ChEBI)
Binding site242substrate
Binding site245phosphate (UniProtKB | ChEBI)
Binding site273substrate
Active site280Proton acceptor
Binding site356NADP+ (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
      CR159_12905

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JR1/69-3-13
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Pollutimonas

Accessions

  • Primary accession
    A0A2N4U3C2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-123Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    376
  • Mass (Da)
    40,723
  • Last updated
    2018-04-25 v1
  • Checksum
    D8FEBD82DE9B6049
MNQVVGLVGWRGMVGSVLMQRMRDENDFSLFEPVFFSTSNAGGAAPAWAEGAGPLQDAYDIDALKKLPIILTAQGGDYTSAVYPKLRAAGWPGVWIDAASTLRMADDAIIVLDPVNRPVIDAALERGVKNFVGGNCTVSCMLMGLSGLFNNDLIEWMSSMTYQAASGGGAQHMRELLTQFGALNAAVKLQLDDPASAILDIDRGVLNMQQDPNLPREHFGVPLGGNLIPWIDKDLGNGMSREEWKAEAETNKILGRGAAFGTAPTPIDGLCVRIGAMRCHSQALTIKLKRDVPLDEISDMLREGSEWAKVIPNERDITMQQLTPVAVTGTLDIPVGRLRKMSMGPEYLSAFTVGDQLLWGAAEPLRRMLRITLGEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDNW01000010
EMBL· GenBank· DDBJ
PLC49497.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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