A0A158JZV0 · A0A158JZV0_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
      AWB66_05004

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LMG 22936
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia

Accessions

  • Primary accession
    A0A158JZV0

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain47-269Mur ligase central
Domain295-421Mur ligase C-terminal

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    436
  • Mass (Da)
    47,103
  • Last updated
    2017-09-27 v1
  • Checksum
    16BB7C392D7700DB
MTTFPTLDAWLAHLEAAHPVGIDMGLTRIGRVKDALGLSFDCPVITVGGTNGKGSTCAILETILLRAGYRVGCHTSPHLLAFNERARIDGADATDAELLEHFEAVEAARASLSEPVSLTYFEFTTLAILRLFASRKLDAVILEVGLGGRLDAVNIVDTDCAIVTSIDIDHTDYLGDTREKIGFEKAGIFRAGKPAVCGDPSPPQTLIDHAEAVGADLWLVGRDFRYEAQPGNERQQWSYIGRSQRRSALAYPALRGANQLINTSAALAALESLRERIPVSAQDIRLGLANVELAGRFQVLPGKPQIILDVAHNPHAAAVLAQNLGNMGFFPYTYAVFGAMGDKDVEGIVKQLKGEIDHWNVTSLPTPRAASTEALEAALREAGVEDGPDSSVTRFETPVEAFQDAIKRASENDRILVFGSFYTVAGVMAYRKSQHH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FCNZ02000024
EMBL· GenBank· DDBJ
SAL74454.1
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