Information on EC 4.3.99.3 - 7-carboxy-7-deazaguanine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.3.99.3
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RECOMMENDED NAME
GeneOntology No.
7-carboxy-7-deazaguanine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-carboxy-5,6,7,8-tetrahydropterin = 7-carboxy-7-carbaguanine + NH3
show the reaction diagram
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
6-carboxy-5,6,7,8-tetrahydropterin ammonia-lyase
Requires Mg2+. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The S-adenosyl-L-methionine is catalytic as it is regenerated at the end of the reaction. The reaction is part of the biosynthesis pathway of queuosine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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A9AC61
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
show the reaction diagram
6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-deazaguanine + NH3
show the reaction diagram
additional information
?
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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
6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-carbaguanine + NH3
show the reaction diagram
6-carboxy-5,6,7,8-tetrahydropterin
7-carboxy-7-deazaguanine + NH3
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
6-carboxy-5,6,7,8-tetrahydropterin
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pH 7,4, temperature not specified in the publication, recombinant enzyme
additional information
additional information
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steady-state kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
6-carboxy-5,6,7,8-tetrahydropterin
Bacillus subtilis
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pH 7,4, temperature not specified in the publication, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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2 * 29000, recombinant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified His6-tagged enzyme in complex with substrate 6-carboxy-5,6,7,8-tetrahydropterin and cofactor S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2-2.6 A resolution
A9AC61
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged QueE from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene queE, expression of His-tagged QueE in Escherichia coli strain BL21(DE3) from plasmid pRM78
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recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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