A0A158GT09 · A0A158GT09_9BURK

  • Protein
    Dihydrofolate synthase/folylpolyglutamate synthase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.

Catalytic activity

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functiondihydrofolate synthase activity
Molecular Functionmetal ion binding
Molecular Functiontetrahydrofolylpolyglutamate synthase activity
Biological Processfolic acid biosynthetic process
Biological Processtetrahydrofolate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrofolate synthase/folylpolyglutamate synthase
  • EC number
  • Alternative names
    • Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase
    • Folylpolyglutamate synthetase
    • Tetrahydrofolylpolyglutamate synthase

Gene names

    • ORF names
      AWB69_03280

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LMG 27134
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia

Accessions

  • Primary accession
    A0A158GT09

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain55-277Mur ligase central
Domain303-429Mur ligase C-terminal

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    444
  • Mass (Da)
    48,108
  • Last updated
    2016-11-02 v1
  • Checksum
    9AF63F1E22B569CF
MATSSTSSSFTFPTLDAWLTHLESAHPVGIDMGLTRISKVRDALGLKFTCPVITVGGTNGKGSTCAIIETILVRAGYRVGCHTSPHLLDFNERARLNGVDATDDELLEHFEAVEQARVSLAEPVTLTYFEFTTLAIMRLFATRDLDAVILEVGLGGRLDAVNIIDTDCAIVTSIDIDHTEYLGDTREKIGFEKAGIFRPDTPAICGDPSPPQSLIDHAKAIGADLWLVGRDFRYEAQSGNERQQWSYIGRTQRRSALAYPALRGANQLINTSAALAALEALRERIPVSAQDIRLGLANVELPGRFQVVPGKPQVILDVAHNPHAAAVLAQNLGNMGFFPYTYAVFGAMGDKDIAGVVEHLKGEIDHWNVTALPTPRAASSAMLESVLRNAGVNDSSDSSVTQFNNPADAFQDALKRASENDRILVFGSFHTVAGVMAYRKSQHH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FCOK02000019
EMBL· GenBank· DDBJ
SAL35182.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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