ID MOAA_HELPJ Reviewed; 321 AA. AC Q9ZL75; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=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=jhp_0705; OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J99 / ATCC 700824; RX PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D., RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human gastric RT pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). 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 -!- SUBUNIT: Monomer and homodimer. {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; AE001439; AAD06280.1; -; Genomic_DNA. DR PIR; A71900; A71900. DR RefSeq; WP_010882557.1; NZ_CP011330.1. DR AlphaFoldDB; Q9ZL75; -. DR SMR; Q9ZL75; -. DR KEGG; hpj:jhp_0705; -. DR PATRIC; fig|85963.30.peg.272; -. DR eggNOG; COG2896; Bacteria. DR UniPathway; UPA00344; -. DR Proteomes; UP000000804; 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 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_B; MoaA_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR013483; MoaA. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR010505; MoaA_twitch. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR02666; moaA; 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; SFLDS00029; Radical_SAM; 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..321 FT /note="GTP 3',8-cyclase" FT /id="PRO_0000152968" FT DOMAIN 5..233 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 14 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" 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 /evidence="ECO:0000255|HAMAP-Rule:MF_01225" 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 /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 27 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" 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 /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 64 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 68 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 95 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 119 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 155 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225" FT BINDING 189 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" 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 321 AA; 36455 MW; B7802F6FCC6D2197 CRC64; MLVDSFNRVI DYIRVSVTKQ CNFRCQYCMP TTPLDFFDDE ELLPLDNVLE FLKIAIDEGV KKIRITGGEP LLRKGLDEFI AKLHAYNKEV ALVLSTNGFS LKKMAKGLKD AGLSRVNVSL DSLKSDRVLK ISQKDALKNT LEGIEESLKV GLKLKLNTVV MKGVNDDEIL ELLEYAKNRS IQIRYIEFME NTHAKSLVKG LKEKEILDLI AQKYKIMGME KPKQGSSKIY TLENGYQFGI IAPHSDDFCQ SCNRIRLASD GKICPCLYYQ DAIDAKEAII NKDTKMMKRL LKQSIINKPE KNMWNDKNGG TPTRAFYYTG G //