A0A2K2H6K9 · A0A2K2H6K9_9BACT

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 site9-12NADP+ (UniProtKB | ChEBI)
Binding site69NADP+ (UniProtKB | ChEBI)
Binding site98phosphate (UniProtKB | ChEBI)
Active site131Acyl-thioester intermediate
Binding site158substrate
Binding site161-162NADP+ (UniProtKB | ChEBI)
Binding site237substrate
Binding site240phosphate (UniProtKB | ChEBI)
Binding site263substrate
Active site270Proton acceptor
Binding site346NADP+ (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
      C2E25_15425

Organism names

  • Taxonomic identifier
  • Strain
    • HR-1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter

Accessions

  • Primary accession
    A0A2K2H6K9

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-118Semialdehyde dehydrogenase NAD-binding

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    366
  • Mass (Da)
    39,802
  • Last updated
    2018-03-28 v1
  • Checksum
    67DDB39E08652D5B
MNVGFIGWRGMVGSVLMQRMQEENDFAAINPVFFSTSQVGQDAPFDAGKLLDAGAIDELKKLDAVVTCQGGDYTKQVHPQLRAAGWNGIWIDAASSLRMADDAVIILDPVNREVITAALAAGKKDFIGGNCTVSLMLMALGGLFRAGLVEWLTSMTYQAASGAGAPNMRELLAQMGHLHDSVADQLADPASAILDIDRKVTAELRGNAIPSDNFGYPLAGSVLPWIDREVEDGQSREEWKGYAETNKILRSETPIPIDGICVRIGAMRCHSQALTIKLNKDIPMADIEDLLANDNPWAELVPNRKEETLARLTPAAVSGTLKTPVGRVRKMKMGPQYLSAFTCGDQLLWGAAEPLRRMLRILRERA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PPFX01000047
EMBL· GenBank· DDBJ
PNU18889.1
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