4.1.99.18: cyclic pyranopterin phosphate synthase
This is an abbreviated version!
For detailed information about cyclic pyranopterin phosphate synthase, go to the full flat file.
Word Map on EC 4.1.99.18
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4.1.99.18
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guanosine
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bicistronic
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molybdopterin
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kingdoms
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s-adenosyl-l-methionine
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s-adenosylmethionine
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adomet
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hexamer
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mocs2a
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5'-triphosphate
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gephyrin
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butirosin
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monoclinic
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thermus
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thermophilus
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barrel
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ansme
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embodying
- 4.1.99.18
- guanosine
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bicistronic
- molybdopterin
-
kingdoms
- s-adenosyl-l-methionine
- s-adenosylmethionine
- adomet
-
hexamer
-
mocs2a
- 5'-triphosphate
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gephyrin
- butirosin
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monoclinic
-
thermus
- thermophilus
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barrel
-
ansme
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embodying
transferred to EC 4.1.99.22 and EC 4.6.1.17
Synonyms
Synonyms
MoaA, MoaC, MOCS1A, molybdenum cofactor biosynthesis protein 1
ECTree
4.1.99.18 cyclic pyranopterin phosphate synthaseAdvanced search results
results (
results (| Results | in table |
|---|---|
| 136 | AA Sequence |
| 2 | Expression |
| 24 | General Information |
| 4 | Synonyms |
General Information
General Information on EC 4.1.99.18 - cyclic pyranopterin phosphate synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
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MoaA belongs to the S-adenosyl-L-methionine-dependent radical enzyme superfamily, members of which catalyse the formation of protein or substrate radicals by reductive cleavage of SAM by a [4Fe-4S] cluster
evolution
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MoaA is a member of the radical-SAM superfamily of proteins and harbors two [4Fe-4S]2+1+ clusters
evolution
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MoaA is a member of the S-adenosylmethionine (SAM)-dependent radical enzyme superfamily
evolution
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MoaA belongs to the S-adenosyl-L-methionine-dependent radical enzyme superfamily, members of which catalyse the formation of protein or substrate radicals by reductive cleavage of SAM by a [4Fe-4S] cluster
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metabolism
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MoaA and MoaC catalyze the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphtate is inserted between the C2' and the C3' carbons of the ribose
metabolism
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MoaA and MoaC together catalyze the first step in molybdopterin biosynthesis, converting GTP to cyclic pyranopterin monophosphate
metabolism
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the enzyme catalyzes teh first step of molybdenum cofactor biosynthesis, the formation of cyclic pyranopterin monophosphate, cPMP
metabolism
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the enzymes is involved in the molybdenum cofactor (Moco) biosynthesis pathway. Together with MoaA, MoaC is involved in the conversion of guanosine triphosphate (GTP) to precursor Z, the first step in Moco synthesis
metabolism
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the formation of precursor Z from guanosine triphosphate in the Molybdenum cofactor (Moco) biosynthesis pathway is catalysed by two enzymes, MoaA and MoaC
metabolism
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the enzymes is involved in the molybdenum cofactor (Moco) biosynthesis pathway. Together with MoaA, MoaC is involved in the conversion of guanosine triphosphate (GTP) to precursor Z, the first step in Moco synthesis
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metabolism
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the formation of precursor Z from guanosine triphosphate in the Molybdenum cofactor (Moco) biosynthesis pathway is catalysed by two enzymes, MoaA and MoaC
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physiological function
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the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
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the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
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the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
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the enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor
physiological function
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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
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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
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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
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physiological function
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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
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additional information
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detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview
additional information
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detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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detailed structure analysis, docking, and molecular-dynamics simulations, active site structure and structure comparisons, overview
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