A0AA37G7W8 · A0AA37G7W8_AERCA

Function

function

Bifunctional aspartate kinase and homoserine dehydrogenase that catalyzes the first and the third steps toward the synthesis of lysine, methionine and threonine from aspartate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

a metal cation (UniProtKB | Rhea| CHEBI:25213 )

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.

GO annotations

AspectTerm
Molecular Functionaspartate kinase activity
Molecular FunctionATP binding
Molecular Functionhomoserine dehydrogenase activity
Molecular FunctionNADP binding
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processthreonine biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional aspartokinase/homoserine dehydrogenase

Including 2 domains:

  • Recommended name
    Aspartokinase
  • EC number
  • Recommended name
    Homoserine dehydrogenase
  • EC number

Gene names

    • Name
      metL
    • ORF names
      KAM379_30090

Organism names

Accessions

  • Primary accession
    A0AA37G7W8

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-280Aspartate/glutamate/uridylate kinase
Domain466-598Aspartate/homoserine dehydrogenase NAD-binding
Domain607-802Homoserine dehydrogenase catalytic

Sequence similarities

In the C-terminal section; belongs to the homoserine dehydrogenase family.
In the N-terminal section; belongs to the aspartokinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    809
  • Mass (Da)
    89,154
  • Last updated
    2024-01-24 v1
  • Checksum
    09BD89ACD2673065
MVATEAVFKRRHVHKFGGSSLADPVCYRRVASIVEQQVGGSELVVVSAAGKTTNRLIQLVELAEAGDEAAGEAITALHAYQQSLIDGLLEGDLHLDLSQQLTDDMQLIAKTLEGQFDRFERNGLLAFGEVWSARLLAALLTSRGEAAAWLDARSFLRAEDGALIKVDTALSSELLKARLAEHAGRIVVTGFIAADMEGRSLLLGRNGSDYSASLLAALADGESTTIWSDVAGVYSADPRRVKEARLLERLSLAEANELARLGSSVLHSRTLQPVADSRQRLTLRCSYNPDEGCTHILRRAPRSGGARIVSSVDQIALIELKVLPQTDFEQTVAAIEAHLARHRLHPLTLQRQPDRRVLRLAYTLEVAQGAFEVLRDFQLQGNFTGLIQKEGFSLVALVGAGVTDNAEQCHRFYQLLADQPLEFVQVAKDGLSLVAVLRQIVLEPLLIALHSALFSRPTRVGLVVFGKGNIGGHWLGLYAREKARLEHELNLALTLYGVFDSKGGLLDEEGLDPLKVQDNFHPKPLIWPELLSQLEQHSFDSLIALDMTASETVSRYYPDFAQLGIHIIAANKFAGAADSEFYQRIKQTCRDHQVQWRYNATVGAGLPIQSSIQMLRQSGDRIQGVSGIFSGTLSWLFQQYDGTRPFSELVDEAWQHGLTEPDPREDLSGQDVRRKLLILAREAGFELDSADIELENLVPVALRKVSADQFMDRLKELDDPIQTAFEGARRVGKVLRYVARFEHDGKARVGLEALEPHHPFANLLPCDNVFAIESDSYRTNPLVIQGPGAGREVTAAAIQYDLWQICASL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BPOM01000026
EMBL· GenBank· DDBJ
GJB73951.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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