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Information on EC 6.3.4.23 - formate-phosphoribosylaminoimidazolecarboxamide ligase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57600

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IUBMB Comments
This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyses a step in the synthesis of purine nucleotides. It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. cf. EC 2.1.2.3, phosphoribosylaminoimidazolecarboxamide formyltransferase.
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Methanocaldococcus jannaschii
UNIPROT: Q57600
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
5-formaminoimidazole-4-carboxamide ribonucleotide synthetase, 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase, PurP, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-formaminoimidazole-4-carboxamide ribonucleotide synthetase
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5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase
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SYSTEMATIC NAME
IUBMB Comments
formate:5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide ligase (ADP-forming)
This archaeal enzyme, characterized from the methanogen Methanocaldococcus jannaschii, catalyses a step in the synthesis of purine nucleotides. It differs from the orthologous bacterial/eukaryotic enzymes, which utilize 10-formyltetrahydrofolate rather than formate and ATP. cf. EC 2.1.2.3, phosphoribosylaminoimidazolecarboxamide formyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
formylphosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + ?
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
catalyses a step in the synthesis of purine nucleotides
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Mg2+ is the best divalent metal in supporting the reaction, with Mn2+ being 87% as active as Mg2+
Mn2+
Mg2+ is the best divalent metal in supporting the reaction, with Mn2+ being 87% as active as Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
pH 5.0: about 60% of maximal activity, pH 8.0: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 18°C, X-ray crystal structures of FAICAR synthetase complexed with various ligands, including the tertiary substrate complex and product complex
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
the enzyme maintains 100% of activity when heated for 15 min at temperatures up to 100°C, but it loses all activity when heated above 100°C for 15 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Y.; White, R.H.; Ealick, S.E.
Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii
Biochemistry
47
205-217
2008
Methanocaldococcus jannaschii (Q57600), Methanocaldococcus jannaschii
Manually annotated by BRENDA team
Ownby, K., Xu, H. and White, R.H.
A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate synthetase. A new enzyme in purine biosynthesis
J. Biol. Chem.
280
10881-10887
2005
Methanocaldococcus jannaschii (Q57600), Methanocaldococcus jannaschii
Manually annotated by BRENDA team