A0A349FDM9 · A0A349FDM9_VIBSX

  • Protein
    Bifunctional aspartokinase/homoserine dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • 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 FunctionATP binding
Molecular Functionhomoserine dehydrogenase activity
Molecular FunctionNADP binding
Biological Processlysine biosynthetic process via diaminopimelate
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
      DCS35_10110

Organism names

  • Taxonomic identifier
  • Organism
    Vibrio sp
  • Strain
    • UBA8383
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio

Accessions

  • Primary accession
    A0A349FDM9

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain320-395ACT

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
    819
  • Mass (Da)
    88,345
  • Last updated
    2018-11-07 v1
  • Checksum
    FDE2451D355DCB03
MRVLKFGGSSLSDADRFLRAADIIANNAQQEEVAVVLSAPGKTTNKLVAVIEAALKGSDAELQIAEIEDLFRDLFEEIKQVLPNIDGNGYNHQVKASLSQLRQFVNGISLLGMCPDNVNARIISKGERVSIELMKAVLEAKGQPASLIDPVKYLLAQGDYLEAMVDVELSTENFRAQPLPQGHVNIMPGFTAGNAKGELVTLGRNGSDYSAAVLAACLRAECCEIWTDVDGVYNCDPRLVDDARLLKSLSYQEAMELSYFGASVLHPKTIAPIAQFHIPCLIKNSFNPQGAGTLIGQDTGEDKLAIKGITTLSDLTMVNVSGPGMKGMVGMASRVFGAMSSAGVSIVLITQSSSEYSISFCIEAQDKALAEQALKEAFELELKDGLLEPVEYINDVAIVTLVGDGMRTSRGVASQFFLSLAEVNVNIVAIAQGSSERAISAVIPEDKISEAIKACHENLFNSKHFLDVFVVGVGGVGGELIDQIQRQQPKLAEKGIVLRVCGLANSKGVLLDGAGLPLEHWRDRLNGISEKFSLATLTSLVQRNHIINPVLVDCTSSEEVANQYADFLAAGFHVVTPNKKANTASMAYYHQLRNVARSSRRKLMYETTVGAGLPVIENLQNLISAGDELERFTGILSGSLSYIFGKLDEGMTLSQATNIAKDNGFTEPDPRDDLSGMDVARKLLILAREAGMALELEDVIVDQALPPGFDDSGSIEEFMQRLPEADAYFQDLAAQAREEGKVLRFVGEIADGQCRVSIAAVDENDPMFKIKDGENALAFYSRYYNPIPLVLRGYGAGTEVTAAGVFADVMRTLGWKLGV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DMWE01000323
EMBL· GenBank· DDBJ
HAS62892.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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