A0A8T4HCU9 · A0A8T4HCU9_9SPHI

  • Protein
    Bifunctional aspartate kinase/homoserine dehydrogenase I
  • Gene
    thrA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • 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.

Caution

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 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
Cellular Componentcytosol
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

Names & Taxonomy

Protein names

  • Submitted names
    • Bifunctional aspartate kinase/homoserine dehydrogenase I
      (EC:1.1.1.3
      , EC:2.7.2.4
      )

Gene names

    • Name
      thrA
    • ORF names
      J5U18_03210

Organism names

  • Taxonomic identifier
  • Strain
    • WQ 2009
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Rhinopithecimicrobium

Accessions

  • Primary accession
    A0A8T4HCU9

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain400-478ACT

Sequence similarities

Belongs to the aspartokinase family.
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)
    88,886
  • Last updated
    2022-10-12 v1
  • Checksum
    E933DBB0FE6CEA62
MKILKFGGTSVGDAPSISAVLAIVKKSYAAGERPLVVLSAMAGVTNLLTKMAEDAAAGQSFQADLKRVEERHFAIVKELMAVKYQNPVYTKLKLFFNEIEDLLQGIYALRELSPQSKDLIVSFGERCSNFMVSKIAAQDIPEALYIDASHYVKTDSNFGQAHVNESLTDQLITALAHAHADNLLFVTGFIGSNEKGRITTLGRGGSDYTAAIFGSVLNAEAIEIWTDVNGMLTADPRIVKKAFSLPVLSYTEAMELSYFGAKVIYPPTMIPAFLKKIPIVIRNTFDPHFPGTIIQFDAGKTTLPIKGISSIAESSVINLAGSGMIGKSGFSGRLFTLLAREQINVVLITQSSSEHSITFAVNPDDALKAVKLIEMEFELELQANKLVQPTVEDNLSVLAIVGENMKKTPGMSGRLFYALGRNGINVRAIAQGSSEYNISVIINKVDLAKALNAVHDAFFAELKKTLYVFNLGTGNIGSTLFKQLEKQHEFLSEQNDVEIKVVGVSNSRKMYFDVDGINLSSWEGTLEGAGEVADLGTFIEKMKALNLPNCVFVDNTASKLPATYYEDIFKANISIVTCNKIANSGTFEQYKKLRDTARKHGVDFFYETNVGAGLPIVRVLKDLMLSGDQIIRIEAILSGTISYIFNNFKGDASFYDVVKKAQELGYTEPDPRDDLGGIDFMRKMLILARDAGHEIESEDVDLGAILPASCLAATSVEAFYAELLRENKFFEDLKERAASANKVIRYIGKLEHGKVAIALELVDENHPFYALSGSDNIISFTTERYKDRPLVVKGPGAGAEVTAAGVFADLVNVGA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGKSB010000003
EMBL· GenBank· DDBJ
MBP3942581.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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