V8QSF4 · V8QSF4_9BURK

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
      W822_16230

Organism names

Accessions

  • Primary accession
    V8QSF4

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

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)
    40,676
  • Last updated
    2014-02-19 v1
  • Checksum
    2A3CC90D5F76E068
MSQSVGFVGWRGMVGSVLMQRMRDEGDFAFINPVFFSTSNAGGKAPAWADGAGPLQDANDIDSLKKLPIIVTAQGGDYTTQVHGKLRSAGWDGVWIDAASTLRMKDNAVIVLDPVNRSVIDTAVAKGVKDFVGGNCTVSCMLMGLAGLFKHDLIDWMTSMTYQAASGGGAQHMRELLTQFGLLNEAVRPLLDDPASAILEIDRQVLAKQQDANLPRDMFGVPLGGSLIPWIDKDLGNGQSREEWKAEAETNKILGRGEGFGSAPIPIDGLCVRIGAMRCHSQALTIKLKKDVSIDEITDMLKEGTEWVKVVPNTRDETMQDLTPVATTGTLDIPVGRLRKMSMGPEYLSAFTVGDQLLWGAAEPLRRMLRISVGEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AYXT01000010
EMBL· GenBank· DDBJ
ETF02255.1
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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