Information on EC 4.1.99.18 - cyclic pyranopterin phosphate synthase

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

EC NUMBER
COMMENTARY
4.1.99.18
-
RECOMMENDED NAME
GeneOntology No.
cyclic pyranopterin phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP = cyclic pyranopterin phosphate + diphosphate
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
molybdenum cofactor biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
GTP 8,9-lyase (cyclic pyranopterin monophosphate-forming)
The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). The enzyme MoaA from bacteria and the human enzyme MOCS1A each contain two oxygen-sensitive FeS clusters. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. In bacteria, the reaction is catalysed by MoaA and requires the action of MoaC. The latter protein is equivalent to the C-terminal domain of the eukaryotic enzyme MOCS1A which does not need further protein components to perform the reaction.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
MoaA
-
-
-
-
MoaA
-
gene name
MoaC
-
-
-
-
MoaC
Q975D5
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
MoaC
Sulfolobus tokodaii 7
Q975D5
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
MoaC
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
MOCS1A
-
-
-
-
MOCS1A
-
-
molybdenum cofactor biosynthesis protein 1
-
-
-
-
ST0472
Q975D5
-
ST0472
Sulfolobus tokodaii 7
Q975D5
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Sulfolobus tokodaii 7
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
physiological function
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
Sulfolobus tokodaii 7
-
the formation of the cyclic pyranopterin monophosphate from GTP is an early step in the biosynthesis of the molybdenum cofactor. It is catalyzed by MaoA and requires the action of MoaC
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the reaction is catalysed by MoaA and requires the action of MoaC
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the reaction is catalyzed by the S-adenosyl-L-methionine-dependent enzyme MoaA and the accessory protein MoaC. This reaction involves the radical-initiated intramolecular rearrangement of the guanine C8 atom
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
-
-
?
additional information
?
-
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
additional information
?
-
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
additional information
?
-
Sulfolobus tokodaii 7
Q975D5
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
-
-
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
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
P65388
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
GTP
cyclic pyranopterin monophosphate + diphosphate
show the reaction diagram
-
the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
Q44118
the enzyme contains iron-sulfur centres
iron-sulfur centre
-
contains two oxygen-sensitive FeS clusters, each coordinated by three cysteine residues. A redox-active [4Fe-4S]2+cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S] cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+clusters. The N-terminal [4Fe-4S]2+cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S] cluster intermediate
iron-sulfur centre
-
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
iron-sulfur centre
-
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
S-adenosyl-L-methionine
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
iron-sulfur centre
Q44118
the enzyme contains iron-sulfur centres
iron-sulfur centre
-
guanine N1 binds to [4Fe-4S] cluster II
iron-sulfur centre
-
contains two oxygen-sensitive FeS clusters, each coordinated by only three cysteine residues. A redox-active [4Fe-4S]2+,+cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S]0 cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+clusters. The N-terminal [4Fe-4S]2+cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S]0 cluster intermediate
iron-sulfur centre
-
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate
iron-sulfur centre
-
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
MoaC protein
-
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z
-
MoaC protein
-
formation cyclic pyranopterin monophosphate by MoaA requires the action of MoaC protein
-
MoaC protein
-
the reaction is catalyzed by the S-adenosylmethionine-dependent enzyme MoaA and the accessory protein MoaC
-
additional information
-
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
additional information
Q975D5, -
the formation of the cyclic pyranopterin monophosphate from GTP is catalyzed by MaoA and requires the action of MoaC
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at
PDB
SCOP
CATH
ORGANISM
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
Staphylococcus aureus (strain N315)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41000
-
-
monomer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
82000
-
-
homodimer, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da), gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 42000, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da)
hexamer
Q975D5, -
-
hexamer
Sulfolobus tokodaii 7
-
-
-
monomer
-
1 * 42000, in solution MoaA exists as a monomer (41000 Da) and dimer (82000 Da)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of wild-type MoaA, MoaA-R17A/R266A/R268A and MoaA in complex with 5'-GTP2.35 A resolution
-
crystals are grown under anaerobic conditions, hanging drop vapor diffusion technique, crystals belong to space group P2(1)2(1)2(1) with cell dimensions of a = 48.1, b = 102.4, and c = 191.2 A and contain two molecules per asymmetric unit, structures of MoaA in the apo-state (2.8 A) and in complex with S-adenosyl-L-methionine (2.2 A)
-
sitting-drop method, hanging-drop vapour-diffusion method, at room temperature
Q975D5, -
GTP-bound crystal structure
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified under anaerobic conditions
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expressed as His-tagged proteins in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C24S/C28S/C31S
-
the mutant does not contain the catalytic S-adenosyl-L-methionine-binding cluster I
N124A/N165A
-
mutation reduces binding of 5'-GTP
R17A
-
complete loss of activity
R17A/R266A/R268A
-
complete loss of activity
R192A
-
80% loss of activity
R266A
-
complete loss of activity
R268A
-
complete loss of activity
R71A
-
80% loss of activity
S126A
-
mutant enzyme with low activity
T73A
-
mutant enzyme with low activity
Y30A
-
mutant enzyme with low activity