A0A286CG34 · A0A286CG34_9ACTN

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.

Type
IDPosition(s)Description
Binding site9-12NADP+ (UniProtKB | ChEBI)
Binding site37-38NADP+ (UniProtKB | ChEBI)
Binding site93phosphate (UniProtKB | ChEBI)
Active site123Acyl-thioester intermediate
Binding site150substrate
Binding site153-154NADP+ (UniProtKB | ChEBI)
Binding site242substrate
Active site249Proton acceptor
Binding site316NADP+ (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
      SAMN06272727_2675

Organism names

  • Taxonomic identifier
  • Strain
    • Ag82_G6-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A286CG34

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-113Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    338
  • Mass (Da)
    35,739
  • Last updated
    2017-11-22 v1
  • Checksum
    6AE13D6A9FB71F7A
MRVGIVGATGQVGTVMRRILKERNFPVTELRLFASARSAGSQLDGVTVEDAATADYTGLDIVLFSAGGATSKALAEKVASQGAVVIDNSSAWRKHPEVPLVVSEVNPHAIKDRPKGIIANPNCTTMAAMPVLRPLHDEAGLEALVVATYQAVSGSGLAGVAELHGQTQKVVADAEKLTHDGEAVDFPEPGVYKRPIAFNVLPLAGNIVDDGLNETDEEQKLRNESRKILEIPELKVSGTCVRVPVFSGHSLQVNARFARPISPERATELLADAPGVVVTDIPTPLQAAGKDPSYVGRIRRDETVDNGLALFVSNDNLRKGAALNAIQIAELVAAELKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
OCNA01000001
EMBL· GenBank· DDBJ
SOD45349.1
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.
FeedbackHelp