(data stored in SCRATCH zone)

SWISSPROT: D5E8N3_METMS

ID   D5E8N3_METMS            Unreviewed;       310 AA.
AC   D5E8N3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 45.
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=Mmah_0004 {ECO:0000313|EMBL:ADE35542.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35542.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35542.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001994; ADE35542.1; -; Genomic_DNA.
DR   RefSeq; WP_013036485.1; NC_014002.1.
DR   EnsemblBacteria; ADE35542; ADE35542; Mmah_0004.
DR   GeneID; 8982135; -.
DR   KEGG; mmh:Mmah_0004; -.
DR   eggNOG; arCOG04174; Archaea.
DR   eggNOG; COG0731; LUCA.
DR   HOGENOM; HOG000224906; -.
DR   KO; K15449; -.
DR   OMA; HRCLQMT; -.
DR   OrthoDB; 36053at2157; -.
DR   BioCyc; MMAH547558:G1GHT-4-MONOMER; -.
DR   Proteomes; UP000001059; 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   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR03972; rSAM_TYW1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E8N3.
DR   SWISS-2DPAGE; D5E8N3.
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:UP000001059};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01921};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01921}.
FT   DOMAIN          59..236
FT                   /note="Radical_SAM"
FT                   /evidence="ECO:0000259|Pfam:PF04055"
FT   DOMAIN          238..297
FT                   /note="Wyosine_form"
FT                   /evidence="ECO:0000259|Pfam:PF08608"
FT   METAL           30
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   METAL           43
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   METAL           56
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   METAL           65
FT                   /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   METAL           69
FT                   /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)"
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"
SQ   SEQUENCE   310 AA;  35099 MW;  3ADEF13B3F175AA1 CRC64;
     MASDLLPDIG TLIKKQGYRL AGSHSAVKTC LWMRRAVREE GECYKARFYG ISSHRCLQMT
     PTLCCNQRCL HCWRPVELDV PTPQKWDSPV EIMGSSIECQ RNLISGFGGS ASRELWQQAN
     EPAHVAISLS GEPTLYPYLD ELIEEFRSRG VSTFVVTNGT VPETIKRIKP SQLYMSLDAP
     ERQTYMEVCS PKDPCLWDNI NESLSILKNK ECRTAIRITL IKGVNMFDVK GYADLIRKAQ
     PDIIEVKAYM HLGFSRNRLE RDAMPGHEEV LDFANQLGCE LGYEVGDQVE ISRVVMLFRD
     GKFVASKLPV
//

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