ID Q8TP54_METAC Unreviewed; 343 AA.
AC Q8TP54;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=MA_2064 {ECO:0000313|EMBL:AAM05466.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM05466.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM05466.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM05466.1; -; Genomic_DNA.
DR RefSeq; WP_011022056.1; NC_003552.1.
DR AlphaFoldDB; Q8TP54; -.
DR STRING; 188937.MA_2064; -.
DR EnsemblBacteria; AAM05466; AAM05466; MA_2064.
DR GeneID; 1473953; -.
DR KEGG; mac:MA_2064; -.
DR HOGENOM; CLU_022610_0_2_2; -.
DR InParanoid; Q8TP54; -.
DR OrthoDB; 8079at2157; -.
DR PhylomeDB; Q8TP54; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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 Reference proteome {ECO:0000313|Proteomes:UP000002487};
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; 38590 MW; 2A648E236378C7C0 CRC64;
MYRTIRVPPE KGEEIREKAV AGNFLDPARK IRKIQTSTGT FLEIPVTEAA GEIVGDFPVI
KQEKPEFLEK TCSLKEYLSG TLTEAEMKHI PSGWHILGDI IIVSIPETLE SKKIQIAEAL
LSMYPKCRSV VRDFGIEGKF RQPKRELLLG SGAETIHKEH GCFFKQDVTK VMYSKGNLEE
RKRMSKLGQG EIVVDMFAGI GYFSIPMAVH AHPEKIISIE INPESFAYLN ENIRLNQVED
IITPIQGDCA EAAPEGEADR VIMGYVGTTH HYLEPGIKAL KKSGGILHYH ETVPENLFRT
RPEERIKKAA RCLGKKVEVL AIRRIKKYSP GVLHVVVDAR IFE
//