A0A0S3RAU5 · A0A0S3RAU5_PHAAN

  • Protein
    Bifunctional dihydrofolate reductase-thymidylate synthase
  • Gene
    Vigan.02G008400
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

Catalytic activity

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site411

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functiondihydrofolate reductase activity
Molecular Functionthymidylate synthase activity
Biological ProcessdTMP biosynthetic process
Biological Processmethylation
Biological Processone-carbon metabolic process
Biological Processtetrahydrofolate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional dihydrofolate reductase-thymidylate synthase

Gene names

    • Name
      Vigan.02G008400
    • ORF names
      VIGAN_02008400

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Shumari
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Vigna

Accessions

  • Primary accession
    A0A0S3RAU5

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-22Disordered
Domain25-202DHFR

Sequence similarities

In the C-terminal section; belongs to the thymidylate synthase family.
In the N-terminal section; belongs to the dihydrofolate reductase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    529
  • Mass (Da)
    59,855
  • Last updated
    2016-02-17 v1
  • Checksum
    B7172DDEFBB9E12D
MASDFSVISNGDSNGNVNPQPNQRTYQVVVAATQDWGIGKDGKLPWRLPTDLKFFKEITEKTSDPGKKNAIVMGRKTWESIPLQYRPLSGRLNVVLTRSGSFDIATAENVVICGSINSALELLASSPYSLSIEKVFVIGGGQIFREALNAPGCEAIHLTEIQSNIECDTFMPSVDFTIFRPWYSSFPKMENNIRHSFISYVRVRSSPVVSLNQDIDPFIDNNSDSIKFEVKDFSFLPKMIFERHEENMYLKLVQDIISEGTIKGDRTGTGTLSKFGSQMRFNLRRSFPLLTTKKVFWRGVVEELLWFISGSTNAKVLQEKNIHIWDGNASREYLDGVGLTEREEGDLGPVYGFQWRHFGARYTDMHADYSGQGFDQLLDVINKIKHNPDDRRIILSAWNPADLKLMALPPCHMFAQFYVAHGELSCQMYQRSADMGLGVPFNIASYALLTCMIAHVCDLIPGEFIHVIGDTHVYRNHVRPLQEQLHNLPKPFPTLKINPKKKDIDSFVAADFKLIGYDPHQKIDMKLAV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP015035
EMBL· GenBank· DDBJ
BAT77503.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp