ID A0A1W6K1P7_9CREN Unreviewed; 308 AA. AC A0A1W6K1P7; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 30-AUG-2017, entry version 2. 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 RT Archaea 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- CC Rule:MF_01225}. CC -!- CATALYTIC ACTIVITY: GTP + S-adenosyl-L-methionine + reduced CC electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'- CC triphosphate + 5'-deoxyadenosine + L-methionine + oxidized CC electron acceptor. {ECO:0000256|HAMAP-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 CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and CC the GTP-derived substrate. {ECO:0000256|HAMAP-Rule:MF_01225}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {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 CC of 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 UniPathway; UPA00344; -. DR Proteomes; UP000193404; Chromosome. 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; IPR034481; Main_SPASM_domain-containing. DR InterPro; IPR013483; MoaA. 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 SFLD; SFLDG01383; cyclic_pyranopterin_phosphate_; 1. DR SFLD; SFLDG01386; main_SPASM_domain-containing; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR02668; moaA_archaeal; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225}; KW Complete proteome {ECO:0000313|Proteomes:UP000193404}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01225}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01225}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225}; KW Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225}. FT DOMAIN 10 214 Elp3. {ECO:0000259|SMART:SM00729}. FT NP_BIND 250 252 GTP. {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 20 20 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 24 24 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 27 27 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 245 245 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 248 248 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT METAL 262 262 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT BINDING 13 13 GTP. {ECO:0000256|HAMAP-Rule:MF_01225}. FT BINDING 61 61 GTP. {ECO:0000256|HAMAP-Rule:MF_01225}. FT BINDING 65 65 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_01225}. FT BINDING 90 90 GTP. {ECO:0000256|HAMAP-Rule:MF_01225}. FT BINDING 114 114 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_01225}. FT BINDING 151 151 GTP. {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 //