Q8DQ00 · Q8DQ00_STRR6

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 site11NADP+ 1 (UniProtKB | ChEBI)
Binding site11NADP+ 3 (UniProtKB | ChEBI)
Binding site11NADP+ 2 (UniProtKB | ChEBI)
Binding site11-14NADP+ (UniProtKB | ChEBI)
Binding site12NADP+ 2 (UniProtKB | ChEBI)
Binding site12NADP+ 1 (UniProtKB | ChEBI)
Binding site13NADP+ 1 (UniProtKB | ChEBI)
Binding site13NADP+ 3 (UniProtKB | ChEBI)
Binding site13NADP+ 2 (UniProtKB | ChEBI)
Binding site14NADP+ 1 (UniProtKB | ChEBI)
Binding site14NADP+ 3 (UniProtKB | ChEBI)
Binding site37NADP+ 1 (UniProtKB | ChEBI)
Binding site37NADP+ 3 (UniProtKB | ChEBI)
Binding site37NADP+ 2 (UniProtKB | ChEBI)
Binding site39NADP+ 3 (UniProtKB | ChEBI)
Binding site39NADP+ 2 (UniProtKB | ChEBI)
Binding site39-40NADP+ (UniProtKB | ChEBI)
Binding site40NADP+ 1 (UniProtKB | ChEBI)
Binding site40NADP+ 3 (UniProtKB | ChEBI)
Binding site40NADP+ 2 (UniProtKB | ChEBI)
Binding site71NADP+ 1 (UniProtKB | ChEBI)
Binding site71NADP+ 3 (UniProtKB | ChEBI)
Binding site94NADP+ 3 (UniProtKB | ChEBI)
Binding site99phosphate (UniProtKB | ChEBI)
Binding site126NADP+ 3 (UniProtKB | ChEBI)
Active site128Acyl-thioester intermediate
Binding site128NADP+ 3 (UniProtKB | ChEBI)
Binding site128NADP+ 1 (UniProtKB | ChEBI)
Binding site155substrate
Binding site158-159NADP+ (UniProtKB | ChEBI)
Binding site162NADP+ 3 (UniProtKB | ChEBI)
Binding site162NADP+ 1 (UniProtKB | ChEBI)
Binding site162NADP+ 2 (UniProtKB | ChEBI)
Binding site163NADP+ 2 (UniProtKB | ChEBI)
Binding site245substrate
Active site252Proton acceptor
Binding site325NADP+ (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
      spr0918

Organism names

Accessions

  • Primary accession
    Q8DQ00

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-119Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    358
  • Mass (Da)
    38,924
  • Last updated
    2003-03-01 v1
  • Checksum
    366715956847C96C
MGYTVAVVGATGAVGAQMIKMLEESTLPIDKIRYLASARSAGKSLKFKDQDITIEETTETAFEGVDIALFSAGSSTSAKYAPYAVKAGVVVVDNTSYFRQNPDVPLVVPEVNAHALDAHNGIIACPNCSTIQMMVALEPVRQKWGLDRIIVSTYQAVSGAGMGAILETQRELREVLNDGVKPCDLHAEILPSGGDKKHYPIAFNALPQIDVFTDNDYTYEEMKMTKETKKIMEDDSIAVSATCVRIPVLSAHSESVYIETKEVAPIEEVKAAIAAFPGAVLEDDVAHQIYPQAINAVGSRDTFVGRIRKDLDAEKGIHMWVVSDNLLKGAAWNSVQIAETLHERGLVRPTAELKFELK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE007317
EMBL· GenBank· DDBJ
AAK99722.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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