ID   D9Q026_ACIS3            Unreviewed;       347 AA.
AC   D9Q026;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   02-NOV-2016, entry version 30.
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}.
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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; 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-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   DOMAIN       69    245       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   DOMAIN      258    318       Wyosine_form. {ECO:0000259|Pfam:PF08608}.
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
//