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Information on EC 6.3.4.3 - formate-tetrahydrofolate ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07245
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6.3.4.3 formate-tetrahydrofolate ligaseIUBMB Comments
In eukaryotes occurs as a trifunctional enzyme also having methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activity.
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Word Map
- 6.3.4.3
-
trifunctional
-
one-carbon
- 5,10-methylenetetrahydrofolate
-
acetogens
- mthfr
- 5,10-methenyltetrahydrofolate
-
homoacetogens
-
folate-dependent
-
acetogenesis
- cylindrosporum
- thermoaceticum
-
folate-mediated
-
1.5.1.5
-
dehydrogenase-cyclohydrolase
-
5,10-methenyl-thf
-
5,10-methylene-thf
-
biogas
- acetobacterium
- acidi-urici
-
syntrophic
- pharmacology
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fthfs, formyltetrahydrofolate synthetase, c1-thf synthase, mthfd, 10-formyltetrahydrofolate synthetase, c1-tetrahydrofolate synthase, 10-formyl-thf synthetase, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase, methylenetetrahydrofolate dehydrogenase 1-like, n10-formyltetrahydrofolate synthetase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10-Formyltetrahydrofolate synthetase
-
-
-
-
FHS
-
-
-
-
formate-tetrahydrofolate ligase
-
-
-
-
formate:tetrahydrofolate ligase (ADP-forming)
-
-
-
-
Formyl-THF synthetase
-
-
-
-
Formyltetrahydrofolate synthetase
FTHFS
-
-
-
-
Synthetase, formyl tetrahydrofolate
-
-
-
-
Tetrahydrofolate formylase
-
-
-
-
Tetrahydrofolic formylase
-
-
-
-
THFS
-
-
-
-
Formyltetrahydrofolate synthetase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
sequential mechanism, formyl phosphate is an intermediate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formylation
formylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
formate:tetrahydrofolate ligase (ADP-forming)
In eukaryotes occurs as a trifunctional enzyme also having methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activity.
CAS REGISTRY NUMBER
COMMENTARY
9023-66-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
ATP + formate
ADP + HCOOPO32-
-
formate kinase reaction, sequential random bi bi mechanism
-
?
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
ATP + formate + tetrahydrofolate
?
-
two different physiological roles: 1. Functions anabolically in most organisms to activate formate via the forward reaction, and brings it into the one-carbon metabolic pool as N10-formyltetrahydrofolate, 2. In purine-fermenting bacteria the enzyme probably functions catabolically in the terminal step of the purine degradative pathway. This reaction may be responsible for ATP production in these organisms
-
-
?
ATP + formate + tetrahydrofolate
?
-
the trifunctional enzyme is involved in the interconversion of one-carbon adducts of tetrahydrofolate
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
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-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
-
ATP in form of MgATP2-
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
ATP + formate + tetrahydrofolate
?
-
two different physiological roles: 1. Functions anabolically in most organisms to activate formate via the forward reaction, and brings it into the one-carbon metabolic pool as N10-formyltetrahydrofolate, 2. In purine-fermenting bacteria the enzyme probably functions catabolically in the terminal step of the purine degradative pathway. This reaction may be responsible for ATP production in these organisms
-
-
?
ATP + formate + tetrahydrofolate
?
-
the trifunctional enzyme is involved in the interconversion of one-carbon adducts of tetrahydrofolate
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paukert, J.L.; Rabinowitz, J.C.
Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): a multifunctional protein in eukaryotic folate metabolism
Methods Enzymol.
66
616-626
1980
Saccharomyces cerevisiae, Ovis aries, Sus scrofa
Buttlaire, D.H.
Purification and properties of formyltetrahydrofolate synthetase
Methods Enzymol.
66
585-599
1980
Clostridium acidi-urici, Clostridium cylindrosporum, Escherichia coli, Gallus gallus, Homo sapiens, Micrococcus aerogenes, Moorella thermoacetica, Neurospora crassa, Oryctolagus cuniculus, Ovis aries, Pigeon, Pisum sativum, Priestia megaterium, Proteus vulgaris, Saccharomyces cerevisiae, Spinacia oleracea, Veillonella parvula
Mejillano, M.R.; Jahansouz, H.; Matsunaga, T.O.; Kenyon, G.L.; Himes, R.H.
Formation and utilization of formyl phosphate by N10-formyltetrahydrofolate synthetase: evidence for formyl phosphate as an intermediate in the reaction
Biochemistry
28
5136-5145
1989
Saccharomyces cerevisiae, Clostridium cylindrosporum
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