A0A4D6YG36 · A0A4D6YG36_9GAMM

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 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

    • ORF names
      D9V81_00720

Organism names

Accessions

  • Primary accession
    A0A4D6YG36

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-284Aspartate/glutamate/uridylate kinase
Domain472-606Aspartate/homoserine dehydrogenase NAD-binding
Domain614-811Homoserine 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    815
  • Mass (Da)
    93,278
  • Last updated
    2019-07-31 v1
  • Checksum
    91A0BC36181FD008
MRILKFGGTSLSNSKKFLEVSKIIEKKFKNDNIAIVLSAPAKITNYLEQINKNITFNKNSKNIFQKIETIFYELSNGINKQQNNFPNNNINKYITNTFDDLKNKIKKIKLLNDNSKKLFSEIISKGEIISIKIMQQLLISKNYLTFYIDPIKNIVTNNDYFESDVNISKTKKNIQKIKIPNKHIILMPGFIAGNKNHELVTLGRNGSDYSAAILAVCLNAKVCEIWTDVDGIYTSDPKIIPTAKLLKSISYQEAIELSSFGAKILHPKTILPLFKSNIKCIIKNTYFPEKTGTIIQNIFEEQSTNIKGITYLNNIVNIVIKINIFKNINFIIEKIFSIFLNFDIQILFHVTSYLENKIYFYIIQKYKDQIKNILKKKLQKELIYDIINIINIDQTLKLINIVGNNINNNINVQKKIFLSLKNTNLNIISTNTTFSKNSFIIITNNNNIHENIKIIHNKLFYKINIIEIFLIGIGGVAKALLKQIQKQSQILKNKNIIFKICSISNSKKMLINLDGINLITWKEQFHTTHKKFCIKKIIKYAKNISLFNPVIIDCTASQEIANFYYDILKNNINIVTPNKKANTNTWKEYANIRNIAIKKNKKFFYETNVSAGLPIIKTLKNLFDSGDELISFEGILSGSLSFIFGKLEEGLSISEATIMAKKLGFTEPNPKDDLSGLDVARKLLILARESGYKLELEDIKIIPILPKYMLKIKDKNTFISELSKLNEYFYNKIKLAKKYKKVLRFIGTIKKGGLCKVELTEVDKKNPLYNVKNGENALIIYSKYYQPIPLVLKGYGAGNNVTAAGIFSDLLQLLP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP032996
EMBL· GenBank· DDBJ
QCI27143.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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