Q89AB8 · DHAS_BUCBP

Function

function

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.

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 site11-14NADP+ (UniProtKB | ChEBI)
Binding site38-39NADP+ (UniProtKB | ChEBI)
Binding site75NADP+ (UniProtKB | ChEBI)
Binding site104phosphate (UniProtKB | ChEBI)
Active site137Acyl-thioester intermediate
Binding site164substrate
Binding site167-168NADP+ (UniProtKB | ChEBI)
Binding site195NADP+ (UniProtKB | ChEBI)
Binding site243substrate
Binding site246phosphate (UniProtKB | ChEBI)
Binding site269substrate
Active site276Proton acceptor
Binding site352NADP+ (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
      bbp_398

Organism names

Accessions

  • Primary accession
    Q89AB8

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001413651-369Aspartate-semialdehyde dehydrogenase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    369
  • Mass (Da)
    41,494
  • Last updated
    2003-06-01 v1
  • Checksum
    8DDBA2BADF6C7516
MKKNIGLIGWRGMVGSVLVERMICENDFFHFNPIFFSTSQKNSKGPTINGEYFGVLKDAYDLDILKELDILISCQGSDYTNKVYFKLRDIGWNGYWIDAASVLRMNQDTVIILDPVNSNTIRESIDSGFKTFVGGNCTVSLMLMSLGGLFSEKLIEWITVSTYQAASGSGAKYIEELLMQMGSMYTEASGYLGNPAHSILNIEKKVRNLSCSDKFPKKNFKVPLAGSLIPWIDKKMRNGQSREEWKIQAETNKILSSNKDILIDGLCVRIGALRCHSQSFVIKLKKDISIPEIEQILLNHNSWTKVIPNRKHDTMTELTPAAVTGTLNTPVGRLRKLNIGQKYLSAFTVGDQLLWGASEPLRRMLKFLI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016826
EMBL· GenBank· DDBJ
AAO27110.1
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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