Information on EC 6.3.4.20 - 7-cyano-7-deazaguanine synthase

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

EC NUMBER
COMMENTARY hide
6.3.4.20
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RECOMMENDED NAME
GeneOntology No.
7-cyano-7-deazaguanine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7-carboxy-7-carbaguanine + NH3 + ATP = 7-cyano-7-carbaguanine + ADP + phosphate + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
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Metabolic pathways
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preQ0 biosynthesis
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tetrahydrofolate metabolism
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SYSTEMATIC NAME
IUBMB Comments
7-carboxy-7-carbaguanine:ammonia ligase (ADP-forming)
Binds Zn2+. The reaction is part of the biosynthesis pathway of queuosine.
CAS REGISTRY NUMBER
COMMENTARY hide
1256460-80-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
gene queC, renamed from ybaX
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to GAT-QueC, a two-domain family with an N-terminal glutamine amidotransferase class-II domain fused to a domain homologous to QueC, the enzyme that produces preQ0. Phylogenetic distribution of aTGT, ArcS, GAT-QueC, and QueF-like in the two archaeal phyla, overview. Most crenarchaeal genomes encode a fused GAT-QueC protein or a QueF-like protein
malfunction
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the expression of QueC from a plasmid-borne copy confers a Q+ phenotype to enzyme-deficient mutant strain Escherichia coli B105
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-carboxy-7-carbaguanine + NH3 + ATP
7-cyano-7-carbaguanine + ADP + phosphate + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7-carboxy-7-carbaguanine + NH3 + ATP
7-cyano-7-carbaguanine + ADP + phosphate + H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
coordination of a zinc ion by the conserved C(x)8CxxCxxC motif in QueC, binding structure, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer or tetramer
the biologically relevant unit is likely to be a QueC homodimer, crystal structure. Monomer structure, overview. The Rossmann fold of the N-terminal part of QueC, in combination with the C-terminal zinc-binding motif, forms a cavity in QueC of substantial size, which is likely to be the location of substrate binding
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified QueC, vapor diffusion method, 10 mg/ml protein is mixed with crystallization solution containing 25% PEG 6000, 100 mM NaCl, 10 mM 1,6 hexanediol, and 100 mM MES, pH 5.5, 1 week, X-ray diffraction structure determination and analysis at 2.95 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged QueC from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant QueC from Escherichia coli strain BL21(DE3) by anion exchange chromatography, hydrophobic interaction chromatography, and another different step of anion exchange chromatography, followed by gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of His-tagged QueC and expression in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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