Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.4.20 - 7-cyano-7-deazaguanine synthase and Organism(s) Bacillus subtilis and UniProt Accession O31675

for references in articles please use BRENDA:EC6.3.4.20
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.20 7-cyano-7-deazaguanine synthase
IUBMB Comments
Binds Zn2+. The reaction is part of the biosynthesis pathway of queuosine.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: O31675
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
7-cyano-7-deazaguanine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7-cyano-7-carbaguanine synthase
-
-
-
-
preQ0 synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
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 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-carboxy-7-carbaguanine + NH3 + ATP
7-cyano-7-carbaguanine + ADP + phosphate + H2O
show the reaction diagram
-
-
-
-
?
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
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the products of four genes, queC, queD, queE, and queF, are involved in preQ1 biosynthesis with GTP as the starting material. preQ1 is transformed to Q in tRNA
metabolism
-
the metabolic pathway includes the conversion of the biosynthetic intermediate, 6-carboxy-5,6,7,8-tetrahydropterin, to intermediate, 7-carboxy-7-deazaguanine, CDG, by an unusual transformation catalyzed by QueE, a member of the radical SAM enzyme superfamily. The carboxylate moiety on CDG is converted subsequently to a nitrile to yield preQ0 by QueC in an ATP-dependent reaction, in which ammonia serves as the nitrogen source. CDG may be the central precursor to all deazapurines, biosynthesis of deazapurine containing compounds in nature incorporates H2NTP, CPH4 and CDG as common intermediates
SUBUNIT
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
in vitro preparation of the deazapurine nucleoside, preQ0, by the successive action of the four involved enzymes, i.e. Escherichia coli QueD, Bacillus subtilis QueE and QueC, and Streptomyces rimosus ToyM, cloning and expression in Escherichia coli strain BL21(DE3), overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
recombinant His-tagged QueC from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3)
cloning of His-tagged QueC and expression in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McCarty, R.M.; Somogyi, A.; Lin, G.; Jacobsen, N.E.; Bandarian, V.
The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of PreQ(0) from guanosine 5-triphosphate in four steps
Biochemistry
48
3847-3852
2009
Bacillus subtilis
Manually annotated by BRENDA team
Cicmil, N.; Huang, R.
Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis
Proteins
72
1084-1088
2008
Bacillus subtilis (O31675)
Manually annotated by BRENDA team