ID Q469W6_METBF Unreviewed; 343 AA.
AC Q469W6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|HAMAP-Rule:MF_01922};
DE EC=2.5.1.114 {ECO:0000256|HAMAP-Rule:MF_01922};
DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN Name=taw2 {ECO:0000256|HAMAP-Rule:MF_01922};
GN OrderedLocusNames=Mbar_A2406 {ECO:0000313|EMBL:AAZ71326.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ71326.1};
RN [1] {ECO:0000313|EMBL:AAZ71326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ71326.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC component of the wyosine derivatives biosynthesis pathway. Catalyzes
CC the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-
CC aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of
CC tRNA(Phe). {ECO:0000256|HAMAP-Rule:MF_01922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC ChEBI:CHEBI:73550; EC=2.5.1.114;
CC Evidence={ECO:0000256|ARBA:ARBA00036405, ECO:0000256|HAMAP-
CC Rule:MF_01922};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000256|HAMAP-Rule:MF_01922}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01922}.
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DR EMBL; CP000099; AAZ71326.1; -; Genomic_DNA.
DR AlphaFoldDB; Q469W6; -.
DR STRING; 269797.Mbar_A2406; -.
DR PaxDb; 269797-Mbar_A2406; -.
DR KEGG; mba:Mbar_A2406; -.
DR eggNOG; arCOG10124; Archaea.
DR HOGENOM; CLU_022610_0_2_2; -.
DR OrthoDB; 8079at2157; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.70.2580; -; 1.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01922; TYW2_archaea; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR040601; Trm5_N.
DR InterPro; IPR030867; TYW2_archaea.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245:SF25; TRNA WYBUTOSINE-SYNTHESIZING PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF02475; Met_10; 1.
DR Pfam; PF18093; Trm5_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01922};
KW Methyltransferase {ECO:0000313|EMBL:AAZ71326.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01922}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01922}.
FT DOMAIN 94..343
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01922"
SQ SEQUENCE 343 AA; 39045 MW; B7830AFE83E2ACCB CRC64;
MYRMIRIAPK KGEELRKKAI QGGFLDTSRK IRKVRTEEGN FLEIPVTESA YNSVDGFLVL
EQENPEFLEK PNSFKDSLKG FLSETELASV PSGWQILGDI IIVFIPEILE DKKKRIAEAL
LSMYPRCRTV VRDFGIEGQF RQPKRELLLG SETETIHREH GCFFKQDVTK VMYSKGNLEE
RKRMSRLGEG EVIVDMFAGI GYFSIPMAVH SRPKKIIGIE INPESFAYLK ENIRLNKVED
IFVPICGDCS RVAPEGTADR VLMGYVGTTH HYLEPAIKAL KKNGGILHYH ETVPESLARI
RPKERIEKAA CALGKKVEIL ETHRIKKYSP GVLHVVVDAR IFE
//
