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
6.3.3.1
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylformylglycinamidine cyclo-ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
enzyme catalyzes transfer of the oxygen of the formyl group to phosphate; sequential mechanism in which ATP binds first to the enzyme and ADP is released last
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-N bond formation
-
-
PATHWAY
KEGG Link
MetaCyc Link
5-aminoimidazole ribonucleotide biosynthesis I
-
5-aminoimidazole ribonucleotide biosynthesis II
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Purine metabolism
-
superpathway of 5-aminoimidazole ribonucleotide biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
2-(Formamido)-N1-(5-phosphoribosyl)acetamidine cyclo-ligase (ADP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5'-Aminoimidazole ribonucleotide synthetase
-
-
-
-
5'-Phosphoribosyl-5-aminoimidazole synthetase
-
-
-
-
AIR synthase
-
-
-
-
AIR synthetase
-
-
-
-
AIRS
-
-
-
-
aminoimidazole ribonucleotide synthetase
-
-
aminoimidazole ribonucleotide synthetase
P74883
-
aminoimidazole ribonucleotide synthetase
-
-
phosphoribosyl aminoimidazole synthetase
-
-
Phosphoribosyl-aminoimidazole synthetase
-
-
-
-
Phosphoribosylaminoimidazole synthetase
-
-
-
-
Synthetase, phosphoribosylaminoimidazole
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-53-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
overproduces a large protein with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
Manually annotated by BRENDA team
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
-
Manually annotated by BRENDA team
serovar typhimurium
SwissProt
Manually annotated by BRENDA team
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
-
Manually annotated by BRENDA team
cowpea
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
P08178
-
-
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
Pigeon
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
P74883, -
-
-
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
P52424, -
-
-
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
ir
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
Escherichia coli K12
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
fifth step in de novo purine biosynthesis
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
Pigeon
-
enzyme of purine biosynthetic pathway
-
-
-
ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
show the reaction diagram
-
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
fifth step in de novo purine biosynthesis
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
-
enzyme of purine biosynthetic pathway
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
show the reaction diagram
Pigeon
-
enzyme of purine biosynthetic pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
absolutely required; Km: 96 mM
K+
-
absolutely required; optimal concentration: 150 mM
K+
-
absolutely required
Mg2+
-
absolutely required; Km: 0.3 mM
Mg2+
-
absolutely required; optimal concentration: 20 mM
Mg2+
-
absolutely required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(5-phosphoribosyl)-5-aminoimidazole
-
-
AMP
-
competitive to ATP
fluorosulfonylbenzoyl adenosine
P08178
FSBA, time-dependent inactivation by covalent binding to Lys27
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.009
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
-
0.027
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
-
0.049
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
P74883, -
37C, pH 7.7, wild type enzyme
0.066
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
P74883, -
37C, pH 7.7, R35C/E57G mutant enzyme
0.012
-
ATP
P08178
pH 7.7, K27R mutant
0.046
-
ATP
P08178
pH 7.7, K27L mutant
0.058
-
ATP
P08178
pH 7.7, K27Q mutant
0.073
-
ATP
P08178
pH 7.7, wild type enzyme
0.126
-
ATP
P74883, -
37C, pH 7.7, wild type enzyme
1.68
-
ATP
P74883, -
37C, pH 7.7, R35C/E57G mutant enzyme
0.172
-
ATPgammaS
-
-
0.065
-
MgATP2-
-
-
0.078
-
MgATP2-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
fluorosulfonylbenzoyl adenosine
P08178
15C, pH 7.7
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.32
-
-
-
0.43
-
-
-
3.35
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
8.1
-
about 90% of maximal activity at pH 7.4 and 8.1
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pigeon
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
71700
-
-
gel filtration, sucrose density gradient ultracentrifugation
74400
-
-
native PAGE of the plastid enzyme
75900
-
-
native PAGE of the mitochondrial enzyme
133000
-
-
sucrose density gradient ultracentrifugation, trifunctional enzyme: AIR synthase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
240000
-
-
gel filtration, bifunctional enzyme with AIR synthetase activity and phosphoribosylglycinamide synthetase activity
330000
-
-
gel filtration, trifunctional enzyme: aminoimidazole ribonucleotide synthase, glycinamide ribonucleotide synthetase, and glycineamide ribonucleotide transformylase
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37057, calculation from nucleotide sequence
?
-
x * 36726, calculation from nucleotide sequence
?
-
4-6 * 40000, SDS-PAGE, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity. Phosphoribosyl-glycinamide synthetase activity is associated with both the monomeric and multimeric forms, but AIR synthetase is only associated with the multimer
?
P52424, -
x * 35500, SDS-PAGE
?
Escherichia coli K12
-
x * 36726, calculation from nucleotide sequence
-
dimer
-
2 * 38500, SDS-PAGE
dimer
-
2 * 87000, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
dimer
-
2 * 36400, SDS-PAGE of the plastid enzyme, 2 * 36900, SDS-PAGE of the mitochondrial enzyme
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for many weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification of wild type and recombinant enzymes using C8-linked ATP affinity column
P08178
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
copurification of AIR synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
-
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
purification of a histidine-tagged enzyme by nickel-affinity column chromatography
P74883, -
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
purification of a histidine-tagged recombinant enzyme by affinity chromatography
P52424, -
using a recombinant histidine-tagged AIRS:cyanogen bromide Sepharose affinity resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
expression in Escherichia coli
-
expression of recombinant enzymes in Escherichia coli
P08178
expression of the trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity, in mutant CHO cells
-
expression in Saccharomyces cerevisiae
-
expression in Escherichia coli of a histidine-tagged enzyme
P74883, -
expression in Escherichia coli of a histidine-tagged recombinant enzyme
P52424, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K27L
P08178
obtained by site-directed mutagenesis and expression in Escherichia coli
K27Q
P08178
obtained by site-directed mutagenesis and expression in Escherichia coli
K27R
P08178
obtained by site-directed mutagenesis and expression in Escherichia coli
additional information
P74883, -
double mutant R35C/E57G obtained by site-directed mutagenesis; triple mutant R35C/E57G/R198W obtained by site-directed mutagenesis