AC MF_01225; DC Protein; auto c? TR HAMAP; MF_01225_B; -; 1; level=0 c? TR HAMAP; MF_01225_A; -; 1; level=0 XX Names: MoaA XX ID MOAA case DE RecName: Full=GTP 3',8-cyclase; DE EC=4.1.99.22; DE AltName: Full=Molybdenum cofactor biosynthesis protein A; end case case DE RecName: Full=Probable GTP 3',8-cyclase; DE EC=4.1.99.22; DE AltName: Full=Molybdenum cofactor biosynthesis protein A; end case GN Name=moaA; XX CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L- CC methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:131766; EC=4.1.99.22; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 CC [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived CC substrate.; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. case CC -!- SUBUNIT: Monomer and homodimer. end case CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. XX DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1; trigger=no DR Pfam; PF06463; Mob_synth_C; 1; trigger=no DR Pfam; PF04055; Radical_SAM; 1; trigger=no DR NCBIfam; TIGR02666; MoaA; 1; trigger=no DR NCBIfam; TIGR02668; moaA_archaeal; 1; trigger=no XX KW 4Fe-4S KW GTP-binding KW Iron KW Iron-sulfur KW Lyase KW Metal-binding KW Molybdenum cofactor biosynthesis KW Nucleotide-binding KW S-adenosyl-L-methionine XX GO GO:0005525; F:GTP binding GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0061798; F:GTP 3',8'-cyclase activity GO GO:1904047; F:S-adenosyl-L-methionine binding GO GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process XX FT From: MOAA_STAA8 (P69848) case FT BINDING 266..268 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [RK]-x-R FT BINDING 24 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 28 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 31 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 261 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 264 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 278 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 30 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 102 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [TS] FT BINDING 126 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 163 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: K FT BINDING 197 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: M end case FT From: MOAA_PYRAB (Q9V2G2) case FT BINDING 255..257 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R-x-R FT BINDING 21 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 25 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 28 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT Condition: C FT BINDING 250 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 253 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 267 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT Condition: C FT BINDING 14 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 27 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: Y FT BINDING 61 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [KR] FT BINDING 65 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 90 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: T FT BINDING 114 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 150 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: K FT BINDING 189 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Optional; Condition: M end case XX case Size: 318-378; end case case Size: 296-357; end case Related: None; Template: P69848; Q44118; P30745; Q9X5W3; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in MYCTU, PSEAE Plasmid: in ARTNI Comments: None XX # Revision 1.35 2023/06/01 //