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QUEC_HELPY
ID   QUEC_HELPY              Reviewed;         226 AA.
AC   O25356;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=HP_0639;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07701.1; -; Genomic_DNA.
DR   PIR; G64599; G64599.
DR   RefSeq; NP_207433.1; NC_000915.1.
DR   RefSeq; WP_000435648.1; NC_018939.1.
DR   AlphaFoldDB; O25356; -.
DR   SMR; O25356; -.
DR   DIP; DIP-3566N; -.
DR   IntAct; O25356; 2.
DR   MINT; O25356; -.
DR   STRING; 85962.C694_03305; -.
DR   PaxDb; O25356; -.
DR   DNASU; 898760; -.
DR   EnsemblBacteria; AAD07701; AAD07701; HP_0639.
DR   KEGG; hpy:HP_0639; -.
DR   PATRIC; fig|85962.47.peg.689; -.
DR   eggNOG; COG0603; Bacteria.
DR   OMA; CESCMRR; -.
DR   PhylomeDB; O25356; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000000429; 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; IBA:GO_Central.
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..226
FT                   /note="7-cyano-7-deazaguanine synthase"
FT                   /id="PRO_0000246852"
FT   BINDING         10..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ   SEQUENCE   226 AA;  25278 MW;  A34256A8BE1EC325 CRC64;
     MEQKICVIGF SGGQDSTTLA VWAKKRFKKV CLVGFDYAQK HSVELECAQK IASLLQLPYE
     IIPLDFLENI TRSALFKNSN DLIGHSHAQN KDLPNSFVPN RNAIFITLLH SYAQKLGASN
     IALGVSQADF SGYPDCKEDF IKSIEHALNL GSNTAIKILT PLMFLNKAQE FQMAKDLGVL
     DLVIKETHTC YQGERKILHA YGYGCDKCPA CQLRKKGFEE FQANKK
 
 
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