ID A0A1J0VBV3_9EURY Unreviewed; 233 AA. AC A0A1J0VBV3; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 07-JUN-2017, entry version 5. DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633}; DE EC=6.3.4.20 {ECO:0000256|HAMAP-Rule:MF_01633}; DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633}; DE AltName: Full=Archaeosine biosynthesis protein QueC {ECO:0000256|HAMAP-Rule:MF_01633}; DE AltName: Full=PreQ(0) synthase {ECO:0000256|HAMAP-Rule:MF_01633}; GN Name=queC {ECO:0000256|HAMAP-Rule:MF_01633}; GN ORFNames=BOX17_00080 {ECO:0000313|EMBL:APE29495.1}; OS Halolamina sediminis. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Halorubraceae. OX NCBI_TaxID=1480675 {ECO:0000313|EMBL:APE29495.1, ECO:0000313|Proteomes:UP000181985}; RN [1] {ECO:0000313|EMBL:APE29495.1, ECO:0000313|Proteomes:UP000181985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hb3 {ECO:0000313|EMBL:APE29495.1, RC ECO:0000313|Proteomes:UP000181985}; RA Koh H.-W., Rani S., Park S.-J.; RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon RT isolated from solar salt."; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). CC {ECO:0000256|HAMAP-Rule:MF_01633}. CC -!- CATALYTIC ACTIVITY: 7-carboxy-7-carbaguanine + NH(3) + ATP = 7- CC cyano-7-carbaguanine + ADP + phosphate + H(2)O. CC {ECO:0000256|HAMAP-Rule:MF_01633}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01633}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01633}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01633}. CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000256|HAMAP- CC Rule:MF_01633}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP018139; APE29495.1; -; Genomic_DNA. DR RefSeq; WP_071941477.1; NZ_CP018139.1. DR GeneID; 30418697; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000181985; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. 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 {ECO:0000256|HAMAP-Rule:MF_01633}; KW Complete proteome {ECO:0000313|Proteomes:UP000181985}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01633}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01633}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01633}; KW Reference proteome {ECO:0000313|Proteomes:UP000181985}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01633}. FT NP_BIND 13 23 ATP. {ECO:0000256|HAMAP-Rule:MF_01633}. FT METAL 190 190 Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}. FT METAL 198 198 Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}. FT METAL 201 201 Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}. FT METAL 204 204 Zinc. {ECO:0000256|HAMAP-Rule:MF_01633}. SQ SEQUENCE 233 AA; 25064 MW; 786D92F4893DB417 CRC64; MTHSPDPATV VIYSGGMDSF TVLHRALREG LDVHALSFDY GQRHRRELEV AERVCRELGV PHQVVDITAI HGLIDNSALT DASRAMPEGD YAAENLADTV VPNRNMILLS LAIAKAVNIG AGRVDYGAHG GDHVLYPDCR PEFVQAMNDV AGIANFEPLT IHAPYLRASK AEILAEGLAM GLDYADTWTC YRGEALACGR CGSCRERLAA FAANGATDPL GYSERPDLDE GAP //