A0AA50DKY6 · A0AA50DKY6_9GAMM

  • Protein
    Bifunctional aspartokinase/homoserine dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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 Functionmetal ion binding
Molecular FunctionNADP binding
Biological Processhomoserine biosynthetic process
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processmethionine biosynthetic process
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

    • ORF names
      Q3V30_20540

Organism names

  • Taxonomic identifier
  • Organism
    Erwinia pyri
  • Strain
    • DE2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Erwinia

Accessions

  • Primary accession
    A0AA50DKY6

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-283Aspartate/glutamate/uridylate kinase
Domain464-599Aspartate/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)
    89,075
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    13A918CFD5834749E1206C501A03D177
MSQSAVAAGSRQLHKFGGSSLADAKCYQRVAGIMAEYSRPGDIMVVSAAGSTTNQLISWLKLSQSDRLSAHQVQQALRRYQSELIGSLLPADQADGLIGQFIHDLEKLAALLDGKITEAVYAEVVGHGEIWSARLMAAVLSLRDIEASWLDARDFLCAERAAQPEVDEGKSWPLLQQLMIQHPGRRLVVTGFISRNEAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHTRTLQPVSGSDIDLQLRCSYQPEQGSTRIERVLASGTGARIVTSHDDVCLIEFQVPPQHDFASLHKEIDHLLKRAQLRPLATGVHPDRNLLQLCYTSEVVSSALNLLQDAGIPGRIQLREGMAMVAMVGAGVCRNPLHSHRFWQQLKDQPVEFIWQSEESISLVAVLRVGPTESLIRGLHQSLFRAEKRIGLILFGKGNIGSRWLELFGREQKTLSARTGFEFLLAGVVDSRRSLLSYEGVDASRAMAFFEEEAVEQDEESLFLWMRAHPFDDLVVLDITASDTLADQYLDFASHGFHVISANKIAGASSGNRYRQIRDAFAKTGRQWLYNATVGAGLPINHTVRDLRESGDSILAISGIFSGTLSWLFLQYDGTVPFTELVDQAWQQGLTEPDPRVDLSGQDVMRKLVILAREAGYEIEPGQVRVESLVPKSCEGESVDHFFENGEALNEQMQQRFEAAQEMGLVLRYVARFDANGKARVGVEAVRNDHPLASLLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDLNRLAQLL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP132353
EMBL· GenBank· DDBJ
WLS78778.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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