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Information on EC 6.3.2.12 - dihydrofolate synthase and Organism(s) Arabidopsis thaliana and UniProt Accession F4JYE9

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IUBMB Comments
In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase , the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date . This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa .
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: F4JYE9
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Arabidopsis thaliana
Synonyms
7,8-Dihydrofolate synthetase, 7,8-Dihydropteroate:L-glutamate ligase (ADP), DHFR, DHFS, dihydrofolate reductase, dihydrofolate synthase, Dihydrofolate synthetase, dihydrofolate synthetase-folylpolyglutamate synthetase, dihydropteroate:L-glutamate ligase (ADP-forming), FHFS, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7,8-Dihydrofolate synthetase
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7,8-Dihydropteroate:L-glutamate ligase (ADP)
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Dihydrofolate synthetase
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dihydropteroate:L-glutamate ligase (ADP-forming)
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FHFS
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FHFS/FPGS
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Folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase
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Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase
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Synthetase, dihydrofolate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxamide formation
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carboxylic acid amide formation
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydropteroate:L-glutamate ligase (ADP-forming)
In some bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase [2], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date [3]. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa [3].
CAS REGISTRY NUMBER
COMMENTARY hide
37318-62-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
show the reaction diagram
Q8W041
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?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
DHFS_ARATH
530
0
56904
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
Q8W041
x * 53000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
Q8W041
x * 53000, SDS-PAGE
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
purification of a histidine-tagged recombinant enzyme using metal-affinity chromatography
Q8W041
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of a histidine-tagged recombinant enzyme in a Saccharomyces cerevisiae lacking a DHFS functional gene
Q8W041
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ravanel, S.; Cherest, H.; Jabrin, S.; Grunwald, D.; Surdin-Kerjan, Y.; Douce, R.; Rebeille, F.
Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
98
15360-15365
2001
Arabidopsis thaliana, Arabidopsis thaliana (Q8W041)
Manually annotated by BRENDA team
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