QUEC_HALS3
ID QUEC_HALS3 Reviewed; 229 AA.
AC B0R9W5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=OE_5195R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774418; CAP15546.1; -; Genomic_DNA.
DR RefSeq; WP_010904151.1; NC_010368.1.
DR AlphaFoldDB; B0R9W5; -.
DR SMR; B0R9W5; -.
DR EnsemblBacteria; CAP15546; CAP15546; OE_5195R.
DR GeneID; 5954768; -.
DR GeneID; 62888206; -.
DR KEGG; hsl:OE_5195R; -.
DR HOGENOM; CLU_081854_1_0_2; -.
DR OMA; CESCMRR; -.
DR PhylomeDB; B0R9W5; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000001321; Plasmid PHS3.
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 CDD; cd01995; ExsB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01633; QueC; 1.
DR InterPro; IPR018317; QueC.
DR InterPro; IPR001763; Rhodanese-like_dom.
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; Plasmid; Zinc.
FT CHAIN 1..229
FT /note="7-cyano-7-deazaguanine synthase"
FT /id="PRO_0000408955"
FT BINDING 10..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 229 AA; 24660 MW; 0491707BF1D84E44 CRC64;
MSAKRAVVLA SGGMDSATAA AVAHNAGYEV YMLHTSYGQQ TEHKEHECAT AQAAALGAAD
FLHLTTDHLS KIGASSLTDD EMAVADADME SDEIPTSYVP FRNANLLAMA TSYAEANDCE
AVFIGAHSED FSGYPDCQPA FFEAFQQTVA AGTKPDTEIS INAPFVDWSK TDIAERGLEL
GVPYEHTWSC YRAEAPACGT CDACAFRLQA FQNLGERDPI EYAERPSYT
