Q0IE17 · Q0IE17_SYNS3

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.

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 site20-23NADP+ (UniProtKB | ChEBI)
Binding site48-49NADP+ (UniProtKB | ChEBI)
Binding site108phosphate (UniProtKB | ChEBI)
Active site137Acyl-thioester intermediate
Binding site164substrate
Binding site167-168NADP+ (UniProtKB | ChEBI)
Binding site217substrate
Binding site243substrate
Active site250Proton acceptor
Binding site323NADP+ (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
    • Ordered locus names
      sync_0067

Organism names

Accessions

  • Primary accession
    Q0IE17

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-128Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    343
  • Mass (Da)
    36,736
  • Last updated
    2006-10-03 v1
  • Checksum
    0A660C6C4CA6E662
MISAAPFPNRPLTVAVLGASGAVGQELLQLLEERNFPVAELRLLASARSAGSRCSWKGQELIVQETTATAFQGVDLVLASAGGSVSKAWREAIVASGAVMVDNSSAFRMEDGVPLVVPEVNPDAAHQHQGVIANPNCTTILLSLALAPLALRRPLRRVVVSTYQSASGAGARAMDELRQLSQVVLDGGTPTSEVLPHSLAFNLFLHNSPLQANGYCEEELKMVNETRKIMGLPDLRFTATCVRVPVLRAHSEAVNVEFHEPFSVEEARSLLAAAAGVELLDDSAHNRFPMPTDVTGRDPVMVGRIRQDISEPNALEFWLCGDQIRKGAALNAIQIAELLLPSV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000435
EMBL· GenBank· DDBJ
ABI47697.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp