ID   D9Q026_ACIS3            Unreviewed;       347 AA.
AC   D9Q026;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   19-JAN-2022, entry version 47.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000664, 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}.
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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   HOGENOM; CLU_007952_3_0_2; -.
DR   OMA; HRCLQMT; -.
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   PANTHER; PTHR13930; PTHR13930; 1.
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.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01921};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01921};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01921}; Reference proteome {ECO:0000313|Proteomes:UP000000346};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01921};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01921}.
FT   DOMAIN          55..312
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
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
//