ID MOAA_METTM Reviewed; 305 AA. AC Q50746; D9PU47; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 29-MAY-2024, entry version 119. DE RecName: Full=Probable GTP 3',8-cyclase {ECO:0000255|HAMAP-Rule:MF_01225}; DE EC=4.1.99.22 {ECO:0000255|HAMAP-Rule:MF_01225}; DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01225}; GN Name=moaA {ECO:0000255|HAMAP-Rule:MF_01225}; GN OrderedLocusNames=MTBMA_c01360; OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium OS thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=20802048; DOI=10.1128/jb.00844-10; RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., RA Gottschalk G., Thauer R.K.; RT "Complete genome sequence of Methanothermobacter marburgensis, a RT methanoarchaeon model organism."; RL J. Bacteriol. 192:5850-5851(2010). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=8575452; DOI=10.1111/j.1432-1033.1995.910_a.x; RA Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.; RT "The tungsten formylmethanofuran dehydrogenase from Methanobacterium RT thermoautotrophicum contains sequence motifs characteristic for enzymes RT containing molybdopterin dinucleotide."; RL Eur. J. Biochem. 234:910-920(1995). CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- CC dihydroguanosine 5'-triphosphate. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01225}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01225}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. CC {ECO:0000255|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; X87968; CAA61207.1; -; Genomic_DNA. DR EMBL; CP001710; ADL57745.1; -; Genomic_DNA. DR RefSeq; WP_013294974.1; NC_014408.1. DR AlphaFoldDB; Q50746; -. DR SMR; Q50746; -. DR STRING; 79929.MTBMA_c01360; -. DR PaxDb; 79929-MTBMA_c01360; -. DR GeneID; 9703841; -. DR KEGG; mmg:MTBMA_c01360; -. DR PATRIC; fig|79929.8.peg.132; -. DR HOGENOM; CLU_009273_0_1_2; -. DR OrthoDB; 6925at2157; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000345; 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:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:TreeGrafter. 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 CDD; cd01335; Radical_SAM; 1. DR CDD; cd21117; Twitch_MoaA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01225_A; MoaA_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR013485; MoaA_arc. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR010505; MoaA_twitch. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR02668; moaA_archaeal; 1. DR PANTHER; PTHR22960:SF0; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1; 1. DR PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1. DR Pfam; PF13353; Fer4_12; 1. DR Pfam; PF06463; Mob_synth_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1. DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding; KW Molybdenum cofactor biosynthesis; Nucleotide-binding; KW S-adenosyl-L-methionine. FT CHAIN 1..305 FT /note="Probable GTP 3',8-cyclase" FT /id="PRO_0000153021" FT DOMAIN 6..228 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 22 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 26 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 28 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 29 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 62 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 66 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 92 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 116 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 153 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 249 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 252 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 254..256 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 266 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" SQ SEQUENCE 305 AA; 34831 MW; 36B65CED21C1D260 CRC64; MQVHDNHRRP LVSLRISVTG RCNVSCIYCH RDGILRSDEE MSPEDIENIC RVASDLGVKK IRLSGGEPLI RDDIVEIVEK INSIGFRDIS ITTNGTLLED LSVPLRDAGL DRVNVSFDTL KPETYRFITR KDYLERVKAG IEGAVMAGLD PVKINMVILR GVNHHEIWDM FEFCRQQGAV LQIIELLKTD SCPDNGVERY HCDITPIEAE LAEMADRIMT RKFMQDRKKY FIGDGEVEVV RPMDNTRFCA NCTRLRVTPD GKLKPCLLRN DNLVDTKEAL SSGDLEGLRE LFLEAIRRRS PYYQS //