AC MF_00917; DC Protein; auto TR HAMAP; MF_00917; -; 1; level=0 XX Names: QueE XX ID QUEE case DE RecName: Full=7-carboxy-7-deazaguanine synthase; DE Short=CDG synthase; DE EC=4.3.99.3; DE AltName: Full=Queuosine biosynthesis protein QueE; else case DE RecName: Full=7-carboxy-7-deazaguanine synthase; DE Short=CDG synthase; DE EC=4.3.99.3; DE AltName: Full=Archaeosine biosynthesis protein QueE; end case GN Name=queE; XX CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- CC deazaguanine (CDG), a step common to the biosynthetic pathways of all CC 7-deazapurine-containing compounds. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7- CC deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Note=Binds 1 S-adenosyl-L-methionine per subunit.; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- CC deazaguanine synthase family. XX DR Pfam; PF04055; Radical_SAM; 1; trigger=no DR NCBIfam; TIGR04508; queE_Cx14CxxC; 1; trigger=no DR NCBIfam; TIGR03365; Bsubt_queE; 1; trigger=no DR NCBIfam; TIGR04322; rSAM_QueE_Ecoli; 1; trigger=no DR NCBIfam; TIGR03963; rSAM_QueE_Clost; 1; trigger=no DR PIRSF; PIRSF000370; QueE; 1; trigger=no XX KW 4Fe-4S KW Iron KW Iron-sulfur KW Lyase KW Magnesium KW Metal-binding case KW Queuosine biosynthesis end case KW S-adenosyl-L-methionine XX GO GO:0000287; F:magnesium ion binding GO GO:0016840; F:carbon-nitrogen lyase activity GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:1904047; F:S-adenosyl-L-methionine binding case GO GO:0008616; P:queuosine biosynthetic process end case XX FT From: QUEE_BURM1 (A0A0H3KB22) FT BINDING 12..14 FT /ligand="substrate" FT Condition: x-x-G FT BINDING 48..50 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FYW]-x-D FT BINDING 133..135 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: S-x-K FT BINDING 173..176 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: Q-x-x-D FT BINDING 31 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 46 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 49 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 51 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Optional; Condition: [TS] FT BINDING 27 FT /ligand="substrate" FT Condition: R FT BINDING 90 FT /ligand="substrate" FT Condition: [TS] FT BINDING 92 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING Cter FT /ligand="substrate" FT Optional; Condition: P XX Size: 180-290; Related: None; Template: O31677; A0A0H3KB22; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: in HALS3, HALSA Comments: None XX # Revision 1.12 2023/06/01 //