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A0A379ASZ4 · A0A379ASZ4_AVIAV

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 Processphosphorylation
Biological Processthreonine biosynthetic process

Keywords

Enzyme and pathway databases

    • UPA00034UER00015
    • UPA00050UER00063
    • UPA00051UER00462

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
      thrA
    • ORF names
      NCTC11297_01773

Organism names

Accessions

  • Primary accession
    A0A379ASZ4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain320-401ACT

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
    815
  • Mass (Da)
    88,266
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    D3789DFC22DC3BD7832BF360684CDABF
MRVLKFGGTSLANPERFSQAARLIEKAHLEEQAAGVLSAPAKITNYLVALSEKASQNLPTDTDFNQALEIFYTIINGLYAESENFDLAGCKAVIDAEFAQIAELLAEIRAKGVLDDAIKATIDCRGEKLSIAMMKAWFETRGYQVTVINPVEKLLAQGGYLESSVDIEESTKRIDVASIPKNNVVLMAGFTAGNDKGELVLLGRNGSDYSAACLAACLNASVCEIWTDVDGVFTCDPRLVPDARLLPSLSYREAMELSYFGAKVIHPRTIGPLAQANIPCLIKNTGNPDAKGSIIDSNAQSEQLQVKGITNLDNLAMFNVSGPGMQGMVGMAARVFSTMSKAGVSVILITQSSSEYSISFCVPVKAAEVAKNALEVEFAQELKNQDLEEIEVIKDLSIISVVGEGMRQAKGIAAHFFSALAQANISIVAIAQGSSERSISAVVPQNKAIEAVKATHQALFNNKKVVDIFLVGVGGVGSELIEQVKNQRDYLAKKDIEIRVCAIANSNKMLLDANGLNLDHWQEDLENATQPSDFDVLLSFIKLHHVVNPVFVDCTSAESVAGLYARALSEGFHVVTPNKKANTRELEYYNLLRENARKSQHKFLYETNVGAGLPVIENLQNLLAAGDELIRFSGILSGSLSFIFGKLEEGLSLSEVTALAREKGFTEPDPRDDLSGQDVARKLLILAREAGLQLELSDVEVEGVLPKGFAEGKSVNEFMAMLPQLDAEFKARVEKAKAEGKVLRYVGQIENGKCKVSIVEVGQDDPLYKVKNGENALAFYTRYYQPIPLLLRGYGAGNAVTAAGIFADILRTLHN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UGSP01000001
EMBL· GenBank· DDBJ
SUB24719.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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