D3DYW9 · D3DYW9_METRM

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 site10-13NADP+ (UniProtKB | ChEBI)
Binding site37-38NADP+ (UniProtKB | ChEBI)
Binding site109phosphate (UniProtKB | ChEBI)
Active site148Acyl-thioester intermediate
Binding site175substrate
Binding site178-179NADP+ (UniProtKB | ChEBI)
Binding site201substrate
Binding site204phosphate (UniProtKB | ChEBI)
Binding site234substrate
Active site241Proton acceptor
Binding site328-329NADP+ (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
      mru_1669

Organism names

Accessions

  • Primary accession
    D3DYW9

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-129Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    349
  • Mass (Da)
    38,336
  • Last updated
    2010-03-23 v1
  • Checksum
    30B76E17D60ABB69
MVKVGVLGATGMVGQRFIQLLADHPDFEIAALAASSRSAGKKYEDATTWYMNDEMPESVRDIKVIETDPAHMDKDVEIVFSSLPADFAAKVEPEYAKDFVVASNASAMRMKKDIPLVIPEVNPQFLDMIEAQQKNNNWDGFIVTNPNCSTIALTLTLKPIYDNFNINRIYVSTMQAVSGAGYNGVPSMAILDNLVPYIGGEEEKMESETLHLLGSLDGDEVVPANFSLSASCHRVPVIDGHTEAVFVELDEEADIDKIKKTMADFRGLPQELGLHSAPEQPVIVKEEDDRPQPRMDRMAYGGMAATVGRLRKDQAFDNSFKYVLVGHNTIRGAAGASILNAELINKQIL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001719
EMBL· GenBank· DDBJ
ADC47519.1
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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