P0AC19 · FOLX_ECOLI

Function

function

Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP) (PubMed:9182560, PubMed:9651328).
Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli (PubMed:19897652).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
13 μM7,8-dihydroneopterin triphosphate
149 μM7,8-dihydroneopterin
66 μM7,8-dihydromonapterin
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
480 μmol/h/mgfor the epimerization of 7,8-dihydroneopterin triphosphate
0.95 μmol/h/mgfor the epimerization of 7,8-dihydroneopterin
0.67 μmol/h/mgfor the epimerization of 7,8-dihydromonapterin

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Molecular Functiondihydroneopterin aldolase activity
Molecular Functiondihydroneopterin triphosphate 2'-epimerase activity
Molecular Functionidentical protein binding
Biological Processfolic acid-containing compound metabolic process
Biological Processpteridine-containing compound biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydroneopterin triphosphate 2'-epimerase
  • EC number
  • Alternative names
    • D-erythro-7,8-dihydroneopterin triphosphate epimerase

Gene names

    • Name
      folX
    • Ordered locus names
      b2303, JW2300

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / RR28
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
    • DSM 613
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AC19
  • Secondary accessions
    • P77796
    • P80449

Proteomes

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene show no detectable growth defect on complete and minimal medium (PubMed:9651328).
The folX deletion selectively eliminates monapterin production and secretion, but has no effect on the intra- and extracellular folate profiles (PubMed:19897652).

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001682952-120Dihydroneopterin triphosphate 2'-epimerase

Proteomic databases

Interaction

Subunit

Homooctamer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the DHNA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    120
  • Mass (Da)
    14,082
  • Last updated
    2007-01-23 v2
  • Checksum
    5DDFF76540827ED6
MAQPAAIIRIKNLRLRTFIGIKEEEINNRQDIVINVTIHYPADKARTSEDINDALNYRTVTKNIIQHVENNRFSLLEKLTQDVLDIAREHHWVTYAEVEIDKLHALRYADSVSMTLSWQR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict27-30in Ref. 2; AAB47972
Sequence conflict48-49in Ref. 2; AAB47972
Sequence conflict55in Ref. 2; AAB47972
Sequence conflict107in Ref. 2; AAB47972

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X96709
EMBL· GenBank· DDBJ
CAA65471.1
EMBL· GenBank· DDBJ
Genomic DNA
U47639
EMBL· GenBank· DDBJ
AAB47972.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16140.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC75363.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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