Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A7J9NQD0 · A0A7J9NQD0_METMI

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 site11-14NADP+ (UniProtKB | ChEBI)
Binding site38-39NADP+ (UniProtKB | ChEBI)
Binding site112phosphate (UniProtKB | ChEBI)
Active site151Acyl-thioester intermediate
Binding site178substrate
Binding site181-182NADP+ (UniProtKB | ChEBI)
Binding site204substrate
Binding site207phosphate (UniProtKB | ChEBI)
Binding site237substrate
Active site244Proton acceptor
Binding site327-328NADP+ (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
      HNP88_001474

Organism names

Accessions

  • Primary accession
    A0A7J9NQD0

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-132Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    348
  • Mass (Da)
    37,921
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    ABCDEBFFEC455177603AC5738D95CB6D
MNIKVGILGATGNVGQRFIQMLENHPVFELEALGASQRSAGKTYKDACYWYQTEPIPEEIANATVVSTDPNDKAYDDVDIVFSALPADLAKTLEPEFAKTGKYVFSNASAMRMESDVPLIVPEVNPEHFGMLEVQKSNRCSDGAIITNPNCSTIGAVISLKPIMDKFGIDLVNITTMQAISGAGYSGVPSMAILDNLVPYIGGEEEKMQTEALKILGNIEGNDFKNGNFKIGVSCNRVPVIDGHTESIFVKTTEEASPEEIAKVMDEFDPLKGLNLPSYAKPVVLREENDRPQPRLDRNTGNGMSIVVGRVRKDPIFSVKYTALEHNTIRGAAGASVLNAELFVQKYL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDUJ010000001
EMBL· GenBank· DDBJ
MBA2847290.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help