QUEC_XANOR
ID QUEC_XANOR Reviewed; 224 AA.
AC Q5H288;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633};
GN Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=XOO1679;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC {ECO:0000255|HAMAP-Rule:MF_01633}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-
CC deazaguanine + ADP + H(+) + H2O + phosphate; Xref=Rhea:RHEA:27982,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:45075,
CC ChEBI:CHEBI:61036, ChEBI:CHEBI:456216; EC=6.3.4.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01633};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01633}.
CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP-
CC Rule:MF_01633}.
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DR EMBL; AE013598; AAW74933.1; -; Genomic_DNA.
DR RefSeq; WP_008578058.1; NC_006834.1.
DR AlphaFoldDB; Q5H288; -.
DR SMR; Q5H288; -.
DR STRING; 291331.XOO1679; -.
DR EnsemblBacteria; AAW74933; AAW74933; XOO1679.
DR KEGG; xoo:XOO1679; -.
DR HOGENOM; CLU_081854_1_1_6; -.
DR OMA; QDPIKYV; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000006735; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01995; ExsB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01633; QueC; 1.
DR InterPro; IPR018317; QueC.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR42914; PTHR42914; 1.
DR Pfam; PF06508; QueC; 1.
DR PIRSF; PIRSF006293; ExsB; 1.
DR TIGRFAMs; TIGR00364; TIGR00364; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..224
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_0000246965"
FT BINDING 8..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ SEQUENCE 224 AA; 23263 MW; FA47886C12B6F253 CRC64;
MKKAVVLLSG GMDSAAVIAL AQEQGFAVYA LSVRYGQRHT SELDAAARVA AAQGVVAHKV
VDVDLRSIGG SALTDDIDVP DAGGDGIPVT YVPARNTIML SLALGWAEVV GANDLFCGVN
AVDYSGYPDC RPEFVRAFEV LANLATKAGV EGAGLRVHAP LQFLSKADIV REGVRLGVDF
GLTVSCYRAD ADGRACGHCD ACRLRAAGFA DAGVPDPTHY AILS
