A0A7Y5MX82 · A0A7Y5MX82_BACUN

  • 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

Enzyme and pathway databases

    • UPA00034UER00015
    • UPA00050UER00063
    • UPA00051UER00462

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
      HUV07_00720

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A23
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A7Y5MX82

Proteomes

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain395-468ACT

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
    810
  • Mass (Da)
    88,559
  • Last updated
    2021-06-02 v1
  • Checksum
    5E3F1D2A9FC7FFE1
MKVMKFGGTSVGSVNSILSVKRIVEAVDEPVIVVVSALGGITDKLINTSRMAVAGDASYENEFREIVYRHVEMIKEVIPAGEAQVALQRQIGELLNELKDIFQGIYLIKDLSQKTSDTIVSYGERLSSIIVAQLTGAEWFDSRKFIKTEKKHSKHVLDTELTNSLVRETFSSLPKRVLVPGFISTDKMTGEVTNLGRGGSDYTAAIIAAALDADSLEIWTDVDGFMTADPRVISRAYTINELSYVEATELCNFGAKVVYPPTIYPVCHKNIPILVKNTFNPEGVGTVIKREVSDPQSKAIKGISSINDTSLITVQGLGMVGVIGVNYRIFKALAKNGISVFLVSQASSENSTSIGVRNADADLACEVLNEEFAKEIEMGEISPIQAEKNLATVAIVGENMKHTPGIAGKLFGTLGRNGINVIACAQGASETNISFVVDSKSLRKSLNVIHDSFFLSEYQVLNLFICGIGTVGGSLIEQIHSQRQKLMQENGLQLNVVGIADANKAMFSREGFDLGRFREELQEKGKDSSLETLRNEIIGMNIFNSVFVDCTASAGVASLYKDLLLHNVSVVAANKIAASSEYENYRELKQIARQRGVKYLFETNVGAGLPIINTINDLIHSGDKILKIEAVLSGTLNYIFNKISADIPFSKTIKMAQEERYSEPDPRIDLSGKDVIRKLVILAREAGYCLEQSDVEKNLFVPDDFFEGSLDDFWKKVPSLDADFEARRKVLEAENKHWRFVAKLENGKASVGLQEVGANHPFYGLEGSNNIILLTTARYKEYPMMIQGYGAGAGVTAAGVFADIMSIANV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABWDF010000002
EMBL· GenBank· DDBJ
NUO10701.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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