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 05-DEC-2018, entry version 100. 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., RA Seedorf H., 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 RT enzymes 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- CC Rule:MF_01225}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo- CC 7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + CC H(+) + L-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 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: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 ProteinModelPortal; Q50746; -. DR SMR; Q50746; -. DR STRING; 79929.MTBMA_c01360; -. DR EnsemblBacteria; ADL57745; ADL57745; MTBMA_c01360. DR GeneID; 9703841; -. DR KEGG; mmg:MTBMA_c01360; -. DR PATRIC; fig|79929.8.peg.132; -. DR eggNOG; arCOG00930; Archaea. DR eggNOG; COG2896; LUCA. DR HOGENOM; HOG000228680; -. DR KO; K03639; -. DR OMA; IEFMPIG; -. DR OrthoDB; POG093Z04PY; -. DR BioCyc; MMAR79929:G1GML-133-MONOMER; -. 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: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. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase; KW Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding; KW S-adenosyl-L-methionine. FT CHAIN 1 305 Probable GTP 3',8-cyclase. FT /FTId=PRO_0000153021. FT NP_BIND 254 256 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 26 26 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 29 29 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 249 249 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 252 252 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 266 266 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 15 15 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 28 28 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 62 62 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 66 66 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01225}. FT BINDING 92 92 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 116 116 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 153 153 GTP. {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 //