ID   QUEC2_SULTO             Reviewed;         460 AA.
AC   Q96Y49; F9VPD6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=7-cyano-7-deazaguanine synthase 2;
DE            EC=6.3.4.20;
DE   AltName: Full=7-cyano-7-carbaguanine synthase 2;
DE   AltName: Full=Archaeosine biosynthesis protein QueC 2;
DE   AltName: Full=PreQ(0) synthase 2;
GN   Name=queC2; OrderedLocusNames=STK_23180;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(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; BA000023; BAK54783.1; -; Genomic_DNA.
DR   RefSeq; WP_010980403.1; NC_003106.2.
DR   AlphaFoldDB; Q96Y49; -.
DR   SMR; Q96Y49; -.
DR   STRING; 273063.STK_23180; -.
DR   EnsemblBacteria; BAK54783; BAK54783; STK_23180.
DR   GeneID; 1460401; -.
DR   KEGG; sto:STK_23180; -.
DR   PATRIC; fig|273063.9.peg.2622; -.
DR   eggNOG; arCOG00039; Archaea.
DR   OMA; NEMEFVR; -.
DR   OrthoDB; 90765at2157; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000001015; 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..460
FT                   /note="7-cyano-7-deazaguanine synthase 2"
FT                   /id="PRO_0000246992"
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         245..255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
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"
SQ   SEQUENCE   460 AA;  52194 MW;  F4BCD089C16E032A CRC64;
     MCSVTGVLII KPENYEKIEK KLIQILKRAE DRGRDSFGVI VIEKDGSVRK VKALGRPSTQ
     EEKLYGILDE NSKVIIANNR AEPTTEYVRQ KTEEDIQPFE GERYIVTHNG IIANDLELEK
     KYNVIRRTKI DSAVVPPILD KYWNGEIEQL KKILNDIKGS FAFIIGDKKR PNRIYIAQNF
     KPVYMMYDRE LGAIFFTSLD DYFDASAFDS VTKLDPYSIV EVNDNLEIRK IQLLDKKIKK
     VLVIASGGLD STVAATYLLR QGYEITLLHF NYHHKAEERE REAVKKIAEY LQVPLIEIDT
     DLFKIIGHTT LLKGGGEIVK DRLGEEGAEF AHEWVPARNL IFYSVALALA EAYGYDAIAS
     GINLEEAGAY PDNEMEFVRL FAKLSPYATG PNKKVEVMMP VGNLVKHEIV KLGVEIGAPL
     HLTWSCYEGG QKHCGKCGPC YMRKMAFRIN GLNDPVEYEN