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Information on EC 3.5.4.25 - GTP cyclohydrolase II and Organism(s) Pseudomonas aeruginosa

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EC Tree
IUBMB Comments
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.
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Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
gtp cyclohydrolase ii, riba2, 3,4-dihydroxy-2-butanone 4-phosphate synthase, gchii, gch ii, gtp cyclohydrolase 2, nbriba, gch-ii, guanosine triphosphate cyclohydrolase ii, gtpch-ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GTP 7,8-8,9-dihydrolase (diphosphate-forming)
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GTP-8-formylhydrolase
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guanosine triphosphate cyclohydrolase II
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ribA
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RIBIV
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bonds
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hydrolysis of phosphoesters
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SYSTEMATIC NAME
IUBMB Comments
GTP 7,8-8,9-dihydrolase (formate-releasing, phosphate-releasing)
The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.
CAS REGISTRY NUMBER
COMMENTARY hide
56214-35-8
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A4Y7V8V1_PSEAI
205
0
22113
TrEMBL
-
A0A6A9JXX4_PSEAI
205
0
22085
TrEMBL
-
A0A7L5F4U0_PSEAI
205
0
22157
TrEMBL
-
A0A367H3G6_PSEAI
205
0
22141
TrEMBL
-
A0A8G7D5Y0_PSEAI
205
0
22157
TrEMBL
-
A0A8G4ZRS1_PSEAI
205
0
22127
TrEMBL
-
A0A072ZE00_PSEAI
205
0
22099
TrEMBL
-
A0A8F9V791_PSEAI
205
0
22157
TrEMBL
-
A0A2R3INM5_PSEAI
205
0
22099
TrEMBL
-