A0A1F2P9M6 · A0A1F2P9M6_9EURY

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 site10-13NADP+ (UniProtKB | ChEBI)
Binding site37-38NADP+ (UniProtKB | ChEBI)
Binding site111phosphate (UniProtKB | ChEBI)
Active site150Acyl-thioester intermediate
Binding site176substrate
Binding site179-180NADP+ (UniProtKB | ChEBI)
Binding site202substrate
Binding site205phosphate (UniProtKB | ChEBI)
Binding site235substrate
Active site242Proton acceptor
Binding site323-324NADP+ (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
      SCAL_000608

Organism names

  • Taxonomic identifier
  • Strain
    • BOX2
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanosarcinales > Methanosarcinales incertae sedis > ANME-2 cluster > Candidatus Syntrophoarchaeum

Accessions

  • Primary accession
    A0A1F2P9M6

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-131Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    347
  • Mass (Da)
    38,134
  • Last updated
    2017-01-18 v1
  • Checksum
    DB4C647122C93D0C
MIKVGVLGATGAVGQRFIQILSEHPWFEITELLASERSAGKKYRDATKWLIETALPEDLKTMEVKLARPESLKNSDIELLFSAIPANIAKKTEVEFAEAGFTVASNAAAHRMDADVPLVIPEVNRDHLALIEVQQRKRGWDGCIITNPNCSTIVMTMTLKPLMQFGIKHVRVATMQAISGAGYTGLPAMAIHDNVIPFIGGEEGKMETEPLKILGELDGDVVKPANFKISASCHRVPVIDGHTEAIWVEFTSDPSVSEIKKAFYDFRREIESPTSPEMPIMVMEEEDRPQPRLDRDLGRGMTVSVGRIRADSMGLKYIAMGHNTIRGAVGASVLNAEVFAVERGIVK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LYOS01000002
EMBL· GenBank· DDBJ
OFV67968.1
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