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Information on EC 1.7.1.13 - preQ1 synthase and Organism(s) Bacillus subtilis and UniProt Accession O31678

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IUBMB Comments
The reaction occurs in the reverse direction. This enzyme catalyses one of the early steps in the synthesis of queuosine (Q-tRNA), and is followed by the action of EC 2.4.2.29, tRNA-guanosine34 transglycosylase. Queuosine is found in the wobble position of tRNAGUN in Eukarya and Bacteria and is thought to be involved in translational modulation. The enzyme is not a GTP cyclohydrolase, as was thought previously based on sequence-homology studies.
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Bacillus subtilis
UNIPROT: O31678
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
nitrile reductase, 7-cyano-7-deazaguanine reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase
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7-cyano-7-deazaguanine reductase
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preQ0 reductase
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preQ0oxidoreductase
-
queuine synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase
The reaction occurs in the reverse direction. This enzyme catalyses one of the early steps in the synthesis of queuosine (Q-tRNA), and is followed by the action of EC 2.4.2.29, tRNA-guanosine34 transglycosylase. Queuosine is found in the wobble position of tRNAGUN in Eukarya and Bacteria [2] and is thought to be involved in translational modulation. The enzyme is not a GTP cyclohydrolase, as was thought previously based on sequence-homology studies.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
peroxide
peroxide-induced inactivation of the wild-type enzyme is reversible with thioredoxin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method, space group: P3(1)21. Unit-cell parameters: a = b = 93.52 A, c = 193.76 A
structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C99A
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
C99S
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Swairjo, M.A.; Reddy, R.R.; Lee, B.; Van Lanen, S.G.; Brown, S.; de Crecy-Lagard, V.; Iwata-Reuyl, D.; Schimmel, P.
Crystallization and preliminary x-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme
Acta Crystallogr. Sect. F
F61
945-948
2005
Bacillus subtilis (O31678), Bacillus subtilis
Manually annotated by BRENDA team
van Lanen, S.G.; Reader, J.S.; Swairjo, M.A.; de Crecy-Lagard, V.; Lee, B.; Iwata-Reuyl, D.
From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold
Proc. Natl. Acad. Sci. USA
102
4264-4269
2005
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Mohammad, A.; Bon Ramos, A.; Lee, B.W.; Cohen, S.W.; Kiani, M.K.; Iwata-Reuyl, D.; Stec, B.; Swairjo, M.A.
Protection of the queuosine biosynthesis enzyme QueF from irreversible oxidation by a conserved intramolecular disulfide
Biomolecules
7
E30
2017
Bacillus subtilis (O31678), Bacillus subtilis 168 (O31678)
Manually annotated by BRENDA team