A0A011Q1P8 · A0A011Q1P8_9PROT

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.

TypeIDPosition(s)Description
Binding site10-13NADP+ (UniProtKB | ChEBI)
Binding site74NADP+ (UniProtKB | ChEBI)
Binding site103phosphate (UniProtKB | ChEBI)
Active site136Acyl-thioester intermediate
Binding site163substrate
Binding site166-167NADP+ (UniProtKB | ChEBI)
Binding site243substrate
Binding site246phosphate (UniProtKB | ChEBI)
Binding site274substrate
Active site281Proton acceptor
Binding site357NADP+ (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
      AW12_02619

Organism names

Accessions

  • Primary accession
    A0A011Q1P8

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-123Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    376
  • Mass (Da)
    40,673
  • Last updated
    2014-06-11 v1
  • Checksum
    B7BB2173A048AD88
MRTLGLVGWRGMVGSVLLQRMVDEGDFEHVEPHFFSTSAVGGRAPAIAGKEAGTLHDAMSIETLSRMDIIITCQGGDYTKEVFPRLRAAGWQGHWIDAASTLRMHDEAVIILDPVNLEVIRSALGKGGCNWIGGNCTVSLMLMGLGGLFRHDLVEWISAMTYQAASGAGAQNMRELLQQMGALHDAVRAQLADPAAAILDIDRRVAETMRSPDFPTGNFRQTALAGSLIPWIDVPVEGGQSKEEWKGGAECNKILGRPAFRSPGSIPVDGLCVRIGAMRCHAQGLTIKLRRDVPLDEIADIIAQGNAWVKVVANEREASERQLTPAAVSGTLTIPVGRLHKLAMGPEYLAAFTVGDQLLWGAAEPLRRMLRILLED

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JEMZ01000169
EMBL· GenBank· DDBJ
EXI83157.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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