ID   QUEC_SACS2              Reviewed;         464 AA.
AC   Q981C9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=7-cyano-7-deazaguanine synthase;
DE            EC=6.3.4.20;
DE   AltName: Full=7-cyano-7-carbaguanine synthase;
DE   AltName: Full=Archaeosine biosynthesis protein QueC;
DE   AltName: Full=PreQ(0) synthase;
GN   Name=queC; OrderedLocusNames=SSO0016;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC       deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC   -!- SIMILARITY: Belongs to the QueC family. {ECO:0000305}.
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DR   EMBL; AE006641; AAK40383.1; -; Genomic_DNA.
DR   PIR; H90140; H90140.
DR   RefSeq; WP_009989631.1; NC_002754.1.
DR   AlphaFoldDB; Q981C9; -.
DR   SMR; Q981C9; -.
DR   STRING; 273057.SSO0016; -.
DR   PRIDE; Q981C9; -.
DR   DNASU; 1455274; -.
DR   EnsemblBacteria; AAK40383; AAK40383; SSO0016.
DR   GeneID; 44128978; -.
DR   KEGG; sso:SSO0016; -.
DR   PATRIC; fig|273057.12.peg.17; -.
DR   eggNOG; arCOG00039; Archaea.
DR   HOGENOM; CLU_550565_0_0_2; -.
DR   OMA; NEMEFVR; -.
DR   BRENDA; 2.6.1.97; 6163.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000001974; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR   CDD; cd01995; ExsB; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_01633; QueC; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR018317; QueC.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR42914; PTHR42914; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   Pfam; PF06508; QueC; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR00364; TIGR00364; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..464
FT                   /note="7-cyano-7-deazaguanine synthase"
FT                   /id="PRO_0000246990"
FT   DOMAIN          2..227
FT                   /note="Glutamine amidotransferase type-2"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  52383 MW;  1B1EA2A9FA494ED4 CRC64;
     MCSVSGVLIL NPKNFEKVEL KLASILKKAE DRGRDSFGIV VIQKDGTVKV RKSIGKPSEK
     EELLYGILDE DSRVVIANNR AEPTTEYVRQ KTEDDIQPFI GDRYIVTHNG IIANDLELEK
     KYELKRKTKI DSAILPLLLD KTWDGNLEAL KGILEQIKGS FALVIGDKKN PDRIFLAQNF
     KPLYMAYDHS LESLFFTSLD EYFDAKPFDP VNITKLEPYS VVMVTSNKLI TTLPIMEKRK
     KYRVLVVASG GLDSTVAATK LLREGHEVTL IHFNYHHKAE EKEREAVRKI AEYLQIPLLE
     INTDLFKIIG HATLIKGGGE IVKDRKGEEG AEFAHEWVPA RNLIFFSVSL AIAEAYGYDA
     IASGINLEEA GAYPDNEMEF IRMLNKLSPY ATGPNKRIEI LMPVGNLVKH EIVKLGYEIG
     APLHLTWSCY EGGQKHCGKC GPCYMRKMAF RINGLKDPVE YDEE