ID A0A1W6K1P7_9CREN Unreviewed; 308 AA. AC A0A1W6K1P7; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 19-JAN-2022, entry version 15. DE RecName: Full=Probable GTP 3',8-cyclase {ECO:0000256|HAMAP-Rule:MF_01225}; DE EC=4.1.99.22 {ECO:0000256|HAMAP-Rule:MF_01225}; DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000256|HAMAP-Rule:MF_01225}; GN Name=moaA {ECO:0000256|HAMAP-Rule:MF_01225}; GN ORFNames=B6F84_10815 {ECO:0000313|EMBL:ARM76463.1}; OS Acidianus manzaensis. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Acidianus. OX NCBI_TaxID=282676 {ECO:0000313|EMBL:ARM76463.1, ECO:0000313|Proteomes:UP000193404}; RN [1] {ECO:0000313|EMBL:ARM76463.1, ECO:0000313|Proteomes:UP000193404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YN-25 {ECO:0000313|EMBL:ARM76463.1, RC ECO:0000313|Proteomes:UP000193404}; RA Ma Y., Yang Y., Xia J.; RT "Sulfur activation and transportation mechanism of thermophilic Archaea RT Acidianus manzaensis YN-25."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate. {ECO:0000256|HAMAP-Rule:MF_01225}. 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 Evidence={ECO:0000256|ARBA:ARBA00000034, ECO:0000256|HAMAP- CC Rule:MF_01225}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01225}; 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. {ECO:0000256|HAMAP-Rule:MF_01225}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01225}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. CC {ECO:0000256|HAMAP-Rule:MF_01225}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01225}. 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; CP020477; ARM76463.1; -; Genomic_DNA. DR STRING; 282676.B6F84_10815; -. DR EnsemblBacteria; ARM76463; ARM76463; B6F84_10815. DR KEGG; aman:B6F84_10815; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000193404; Chromosome. DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01225_A; MoaA_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR013485; MoaA_arc. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR010505; Mob_synth_C. DR InterPro; IPR007197; rSAM. DR Pfam; PF06463; Mob_synth_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR02668; moaA_archaeal; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01225}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01225}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01225}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01225}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01225}; KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150, KW ECO:0000256|HAMAP-Rule:MF_01225}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01225}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01225}. FT DOMAIN 4..224 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT NP_BIND 250..252 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 20 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 24 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 27 FT /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 245 FT /note="Iron-sulfur 2 (4Fe-4S-substrate)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 248 FT /note="Iron-sulfur 2 (4Fe-4S-substrate)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT METAL 262 FT /note="Iron-sulfur 2 (4Fe-4S-substrate)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 13 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 61 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 65 FT /note="S-adenosyl-L-methionine; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 90 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 114 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" FT BINDING 151 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225" SQ SEQUENCE 308 AA; 35274 MW; AC6C7D2D2D5165FB CRC64; MKDRYGRELE DLRITLTHVC NFSCFFCHME GEGDLYVNGL TPDEIELVAE VSKEYGIKYV KLTGGEPTLR RDLTEIIYRL RNLGLEVSMT TNGYMLSKIA SKLKEAGLNR VNISLHTLDK EKFKKITGVD GMDRVIEGIK EAINVGLKPV KLNFVATKMN INEAFNVIDF AEKIGVNELH LIELHPVGMG KIAFSYHEKL NNLENVLKEK ALREGTRNKH YRPRFYLPSG LVVEIVKPYA NPIFCSGCNR IRLTVDGKLK TCLYRDDNSI EILNILRSNL DKYHKMQLLK EAFDVAIAIR EPNFKYII //