Information on EC 6.3.3.1 - phosphoribosylformylglycinamidine cyclo-ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.3.3.1
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylformylglycinamidine cyclo-ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-N bond formation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5-aminoimidazole ribonucleotide biosynthesis I
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5-aminoimidazole ribonucleotide biosynthesis II
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Metabolic pathways
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purine metabolism
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Purine metabolism
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superpathway of 5-aminoimidazole ribonucleotide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
2-(Formamido)-N1-(5-phosphoribosyl)acetamidine cyclo-ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-53-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
overproduces a large protein with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
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Manually annotated by BRENDA team
K12
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
Pigeon
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-
-
Manually annotated by BRENDA team
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
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-
Manually annotated by BRENDA team
serovar typhimurium
SwissProt
Manually annotated by BRENDA team
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(5-phosphoribosyl)-5-aminoimidazole
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AMP
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competitive to ATP
fluorosulfonylbenzoyl adenosine
FSBA, time-dependent inactivation by covalent binding to Lys27
phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.066
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
0.012 - 1.68
ATP
0.172
ATPgammaS
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0.065 - 0.078
MgATP2-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
fluorosulfonylbenzoyl adenosine
15C, pH 7.7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.32
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0.43
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.1
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about 90% of maximal activity at pH 7.4 and 8.1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Geobacillus kaustophilus (strain HTA426)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71700
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gel filtration, sucrose density gradient ultracentrifugation
74400
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native PAGE of the plastid enzyme
75900
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native PAGE of the mitochondrial enzyme
133000
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sucrose density gradient ultracentrifugation, trifunctional enzyme: AIR synthase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
240000
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gel filtration, bifunctional enzyme with AIR synthetase activity and phosphoribosylglycinamide synthetase activity
330000
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gel filtration, trifunctional enzyme: aminoimidazole ribonucleotide synthase, glycinamide ribonucleotide synthetase, and glycineamide ribonucleotide transformylase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for many weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
copurification of AIR synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
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purification of a histidine-tagged enzyme by nickel-affinity column chromatography
purification of a histidine-tagged recombinant enzyme by affinity chromatography
purification of wild type and recombinant enzymes using C8-linked ATP affinity column
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
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using a recombinant histidine-tagged AIRS:cyanogen bromide Sepharose affinity resin
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and characterization of a 12-gene cluster encoding nine enzymes for de novo purine nucleotide synthesis. The cluster is likely an operon and is organized into three groups of overlapping genes followed by the last gene: purEKB-purC(or)QLF-purMNH(J)-purD
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expression in Escherichia coli
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expression in Escherichia coli of a histidine-tagged enzyme
expression in Escherichia coli of a histidine-tagged recombinant enzyme
expression in Saccharomyces cerevisiae
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expression of recombinant enzymes in Escherichia coli
expression of the trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity, in mutant CHO cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K27L
obtained by site-directed mutagenesis and expression in Escherichia coli
K27Q
obtained by site-directed mutagenesis and expression in Escherichia coli
K27R
obtained by site-directed mutagenesis and expression in Escherichia coli
additional information
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