QUEC_SHIF8
ID QUEC_SHIF8 Reviewed; 231 AA.
AC Q0T7D9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SFV_0418;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF02687.1; -; Genomic_DNA.
DR RefSeq; WP_000817216.1; NC_008258.1.
DR AlphaFoldDB; Q0T7D9; -.
DR SMR; Q0T7D9; -.
DR EnsemblBacteria; ABF02687; ABF02687; SFV_0418.
DR KEGG; sfv:SFV_0418; -.
DR HOGENOM; CLU_081854_0_0_6; -.
DR OMA; CESCMRR; -.
DR BioCyc; SFLE373384:SFV_RS02330-MON; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000659; 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; Zinc.
FT CHAIN 1..231
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_1000069802"
FT BINDING 8..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ SEQUENCE 231 AA; 25452 MW; 66DFD00122A023ED CRC64;
MKRAVVVFSG GQDSTTCLVQ ALQQYDEVHC VTFDYGQQHR AEIDVARELA LKLGARAHKV
LDVTLLNELA VSSLTRDSIP VPDYEPEADG IPNTFVPGRN ILFLTLAAIY AYQVKAEAVI
TGVCETDFSG YPDCRDEFVK ALNHAVSLGM AKDIRFETPL MWIDKAETWA LADYYGKLDL
VRNETLTCYN GIKGDGCGHC AACNLRANGL NHYLADKPTV MAAMKQKTGL R
