A0A0F5PBZ3 · A0A0F5PBZ3_9SPHN

  • Protein
    Dihydrofolate synthase/folylpolyglutamate synthase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
Molecular FunctionATP binding
Molecular Functiondihydrofolate synthase activity
Molecular Functionmetal ion binding
Molecular Functiontetrahydrofolylpolyglutamate synthase activity
Biological Processcell division
Biological Processcell wall organization
Biological Processfolic acid biosynthetic process
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape
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
      WP12_11380

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SRS2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    A0A0F5PBZ3

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain46-190Mur ligase central
Domain307-422Mur ligase C-terminal

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    438
  • Mass (Da)
    47,285
  • Last updated
    2015-06-24 v1
  • Checksum
    5EF2E7F8ACE63F7C
MVRMDAFLTRLLTLHPKRIDLSLDRMWRILDRLGHPERRLPPVIHVAGTNGKGSTVAFLRAIVEAAGRAVHVYTSPHLVRFNERIRLARPGGGALVEDDELADAFATCERLNAGDPITFFEITTAAAFLLFARHPADVLLLEVGLGGRLDATNVIERLLASVITPISLDHQDFLGNTIELIAAEKAGILKPNVLAVTAPQSREALTVIERQAARMRAPLRIAGKHWVVTPERGRMAYRDEHGLIDLPAPCLSGRHQFDNAGTAIATLRSIPALQIPHAAFKQGVAKVEWPARMQRLPHGRLVELAPQGSELWLDGGHNPDCGRAVVGALADLEKRGPRPLILIVGMLASKDCEGFLMNFAVLVCRVIAVPIQQDTALPSEEIAQVARCVGIPAETRDSVGDALATISALGLDPAPRILITGSLYLAGEVLAANGTLPI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LARW01000086
EMBL· GenBank· DDBJ
KKC25935.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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