ID   QUEC_SALPA              Reviewed;         231 AA.
AC   Q5PFP1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SPA2267;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78152.1; -; Genomic_DNA.
DR   RefSeq; WP_000817205.1; NC_006511.1.
DR   AlphaFoldDB; Q5PFP1; -.
DR   SMR; Q5PFP1; -.
DR   EnsemblBacteria; AAV78152; AAV78152; SPA2267.
DR   KEGG; spt:SPA2267; -.
DR   HOGENOM; CLU_081854_0_0_6; -.
DR   OMA; CESCMRR; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000008185; 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_0000246918"
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;  25499 MW;  EA2CA1238D00EAF8 CRC64;
     MKRAVVVFSG GQDSTTCLAQ ARHQYDEVHC VTFDYGQRHR AEIDVARALA LKLGARAHKV
     LDVTLLNELA VSSLTRDSIP VPDYEPNADG IPNTFVPGRN ILFLTLVAIY AYQVKAEAVI
     TGVCETDFSG YPDCRDEFVK ALNHAVNLGM AKDIRFETPL MWIDKAETWA LADYWGQLDL
     VREETLTCYN GIKGDGCGHC AACNLRANGL NHYLSNKSAV MAAMKQKTGL R