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-NOV-2015, entry version 27. 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 RT supports a new order, Acidilobales, and suggests an important RT ecological role in terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: Component of the wyosine derivatives biosynthesis CC pathway that catalyzes the condensation of N-methylguanine with 2 CC carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine CC (imG-14) on guanosine-37 of tRNA(Phe). {ECO:0000256|HAMAP- CC Rule:MF_01921}. CC -!- CATALYTIC ACTIVITY: N(1)-methylguanine(37) in tRNA(Phe) + pyruvate CC + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + CC L-methionine + 5'-deoxyadenosine + CO(2) + H(2)O. CC {ECO:0000256|HAMAP-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 CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {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 ProteinModelPortal; D9Q026; -. 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; VKLCHWL; -. DR BioCyc; ASAC666510:GH9G-267-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-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. 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; IPR023993; TYW1_archaea. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF08608; Wyosine_form; 1. DR TIGRFAMs; TIGR03972; rSAM_TYW1; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01921}; KW Complete proteome {ECO:0000313|Proteomes:UP000000346}; 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 METAL 36 36 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01921}. FT METAL 49 49 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01921}. FT METAL 62 62 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_01921}. FT METAL 72 72 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01921}. FT METAL 76 76 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01921}. FT METAL 79 79 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {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 //