ID   QUEC_SULAC              Reviewed;         462 AA.
AC   Q4JBY3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Saci_0280;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY79696.1; -; Genomic_DNA.
DR   RefSeq; WP_011277198.1; NC_007181.1.
DR   AlphaFoldDB; Q4JBY3; -.
DR   SMR; Q4JBY3; -.
DR   STRING; 330779.Saci_0280; -.
DR   PRIDE; Q4JBY3; -.
DR   EnsemblBacteria; AAY79696; AAY79696; Saci_0280.
DR   GeneID; 3473885; -.
DR   KEGG; sai:Saci_0280; -.
DR   PATRIC; fig|330779.12.peg.277; -.
DR   eggNOG; arCOG00039; Archaea.
DR   HOGENOM; CLU_550565_0_0_2; -.
DR   OMA; NEMEFVR; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000001018; 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   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..462
FT                   /note="7-cyano-7-deazaguanine synthase"
FT                   /id="PRO_0000246989"
FT   DOMAIN          2..225
FT                   /note="Glutamine amidotransferase type-2"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         439
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  51977 MW;  82D7F8FA62F7F00C CRC64;
     MCSVTGVLIL NPHNYKEIEK KLAKILIRAE DRGRDSFGIV VIQKDGSTKS SKHVGKPSLQ
     EEKLYGILDE NSKVVIANNR AEPTTEYVRR KTENDIQPFE GERFVVTHNG IIANDMELEK
     KYKVSKLSRI DSSVLPPVLD RSWNGNLDSL SEILNSIRGS FALVIGDKKN PDRIFIAQNF
     KPVYMMYDRD LGAVFFTSLD DYFDATELDN VTKLDPYSVV MVDDKLEIRK VPLLKEKNKK
     RILVVASGGL DSTVAATYLV RQGHEVTLLH FNYHHKAEEK EREAVRKISE YLNVPFVEID
     TDLFKIVGHS TLIKGSSGEI VKDRKGEEGA EFAHEWVPAR NLIFFSVALA MAEAYGFDAI
     ASGINLEEAG AYPDNEMEFV RMFSRLVPYA VGPNKKVEVL MPVGNLVKHE IVKLGVQIDA
     PLHLTWSCYE GGNKHCGKCG PCYMRKVAFE VNGLKDPVEY EA