ID D9Q026_ACIS3 Unreviewed; 347 AA. AC D9Q026; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 11-DEC-2019, entry version 40. DE RecName: Full=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase {ECO:0000256|HAMAP-Rule:MF_01921}; DE EC=4.1.3.44 {ECO:0000256|HAMAP-Rule:MF_01921}; DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw1 {ECO:0000256|HAMAP-Rule:MF_01921}; GN Name=taw1 {ECO:0000256|HAMAP-Rule:MF_01921}; GN OrderedLocusNames=ASAC_0257 {ECO:0000313|EMBL:ADL18664.1}; OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / OS 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18664.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL18664.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; RX PubMed=20581186; DOI=10.1128/AEM.00599-10; RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports RT a new order, Acidilobales, and suggests an important ecological role in RT terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: Component of the wyosine derivatives biosynthesis pathway CC that catalyzes the condensation of N-methylguanine with 2 carbon atoms CC from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on CC guanosine-37 of tRNA(Phe). {ECO:0000256|HAMAP-Rule:MF_01921}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl- CC L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine CC + CO2 + H2O + L-methionine; Xref=Rhea:RHEA:36347, Rhea:RHEA- CC COMP:10164, Rhea:RHEA-COMP:10165, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315, CC ChEBI:CHEBI:73542; EC=4.1.3.44; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01921}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01921}; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01921}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01921}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01921}. CC -!- SIMILARITY: Belongs to the TYW1 family. {ECO:0000256|HAMAP- CC Rule:MF_01921}. 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; CP001742; ADL18664.1; -; Genomic_DNA. DR STRING; 666510.ASAC_0257; -. DR EnsemblBacteria; ADL18664; ADL18664; ASAC_0257. DR KEGG; asc:ASAC_0257; -. DR eggNOG; arCOG04174; Archaea. DR eggNOG; COG0731; LUCA. DR HOGENOM; HOG000224906; -. DR KO; K15449; -. DR OMA; HRCLQMT; -. DR BioCyc; ASAC666510:G1GMD-272-MONOMER; -. DR Proteomes; UP000000346; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102521; F:tRNA-4-demethylwyosine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01921; TYW1_archaea; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR013917; tRNA_wybutosine-synth. DR InterPro; IPR034556; tRNA_wybutosine-synthase. DR InterPro; IPR023993; TYW1_archaea. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF08608; Wyosine_form; 1. DR SFLD; SFLDF00284; tRNA_wybutosine-synthesizing; 1. DR TIGRFAMs; TIGR03972; rSAM_TYW1; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01921}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01921}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01921}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01921}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01921}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01921}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01921}. FT DOMAIN 69..245 FT /note="Radical_SAM" FT /evidence="ECO:0000259|Pfam:PF04055" FT DOMAIN 258..318 FT /note="Wyosine_form" FT /evidence="ECO:0000259|Pfam:PF08608" FT METAL 36 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" FT METAL 49 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" FT METAL 62 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" FT METAL 72 FT /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" FT METAL 76 FT /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" FT METAL 79 FT /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01921" SQ SEQUENCE 347 AA; 40289 MW; 1DE13A5AFF735A2A CRC64; MEERQVEEKE IYNMLNQKLV KQGYHIIGNH SSVKKCYWNH AALVEGRFCY KGKFYGIESH RCIQLSVTNH WCWNACLHCW RLRPQDVGIE WNETRMPFAD DPKEIVEKAI QEYRRIISGY KGRPGVSPQM YKEATMPKHV AISLTGEATL YPRLGELIRE FHRRGISTFL VTRGVRPDVL ANLEEEPNQI YISLESWDKE SYNYFNRPLV PRAWELTLET LEMLPSFSST TVYRITIVKG YNDNETALKG FARLVDIGRP DYIEVKAYMY VGASRGRLRL DNMPRHWEVK EVAKKLSELT GYPIVSESMP SRVVLLSKLE KPVRYGNAPV DWNSPDISAP GEYEDTA //