A0A933X3G0 · A0A933X3G0_UNCPL

  • 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

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 Functionhomoserine dehydrogenase activity
Molecular Functionmetal ion binding
Molecular FunctionNADP binding
Biological Processhomoserine biosynthetic process
Biological Processlysine biosynthetic process
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
      HZA53_17675

Organism names

Accessions

  • Primary accession
    A0A933X3G0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region175-208Disordered
Compositional bias177-199Polar residues
Domain347-416ACT

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
    845
  • Mass (Da)
    89,832
  • Last updated
    2023-02-22 v1
  • Checksum
    3DE583D197590AB0
MKFGGTSVGDAARMRRVIDLVQEALREERVCLVASAVTGVTNQLLEASRKAREGEAPGPFVERFRALHAKIVADVASELAYDARVELETALDGIAREYERLLQGVQLLREAPPLVVAKLSSLGERASCAILARLARARGLAPRELDPVQFVLASGDCLEAAPDLAKIHARWSELRAPSDQRTPSDQRAPSDQRAPSDQRAPSGPSERGERLLILPGFFAGDGEGRTVLLGRGGSDWSAAIAAHALDARLCDVWTDVDGIYSADPRLVPEAFSLPEVSFEEAMELSFFGAKVLHPKTIQPAREKGIPVAVRNSFAPEKPGTIVRASAAPSPFGVRGLTLLADVALVNLTGSGMAGIPGVASRAFAALAEAGISVILISQASSECAISLCVTGKDGARAVAALERAFEPERRLSRIDPVERRDGLSILSVVGDGMRTRMGAAGTFFRALAEVAVNVVAIAQSASERSISAVILGGDGERAIRHAHHRFFHTPETIDLFVFGAGSVGARLLAQVGAQRERLLQRGVRLRITGIANSKALVLDETGIEPAQAAARLASERAPSELARVLAFVAERRPVCPVLVDCTASGELATRYAAALEGGLHVVTANKVANASAQAYWRELRAIARKKQRRFLYATNVGAGLPVIDTLQSLVASGDRVKRIEGVLSGSMSYLLGRIEDGARLSDALREAREQGFTEPDPREDLSGRDVARKVLILAREIGIELEPDDVQVEGVLPKRFDASGTVDAFLDRVPALDAEFAARAAELAKRGAALRFAGRIEEGRAVVSLVEAGPEHPLRGVKGGENALAFLTEHYSPRPMVIRGYGAGADVTAAGVLSDILSLATWSPA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias177-199Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACRIO010000305
EMBL· GenBank· DDBJ
MBI5365012.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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