TYW2_METJA
ID TYW2_METJA Reviewed; 249 AA.
AC Q58952;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000255|HAMAP-Rule:MF_01922};
DE EC=2.5.1.114 {ECO:0000255|HAMAP-Rule:MF_01922};
DE AltName: Full=MjTYW2;
DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw2 {ECO:0000255|HAMAP-Rule:MF_01922};
GN Name=taw2 {ECO:0000255|HAMAP-Rule:MF_01922}; OrderedLocusNames=MJ1557;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP GENE NAME.
RX PubMed=20382657; DOI=10.1093/molbev/msq096;
RA de Crecy-Lagard V., Brochier-Armanet C., Urbonavicius J., Fernandez B.,
RA Phillips G., Lyons B., Noma A., Alvarez S., Droogmans L., Armengaud J.,
RA Grosjean H.;
RT "Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse
RT pathway in Archaea.";
RL Mol. Biol. Evol. 27:2062-2077(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19717466; DOI=10.1073/pnas.0905270106;
RA Umitsu M., Nishimasu H., Noma A., Suzuki T., Ishitani R., Nureki O.;
RT "Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction
RT catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15616-15621(2009).
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:0000255|HAMAP-Rule:MF_01922,
CC ECO:0000269|PubMed:19717466}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01922, ECO:0000269|PubMed:19717466};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01922}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000255|HAMAP-Rule:MF_01922}.
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DR EMBL; L77117; AAB99577.1; -; Genomic_DNA.
DR PIR; D64494; D64494.
DR PDB; 3A27; X-ray; 2.00 A; A=1-249.
DR PDBsum; 3A27; -.
DR AlphaFoldDB; Q58952; -.
DR SMR; Q58952; -.
DR STRING; 243232.MJ_1557; -.
DR EnsemblBacteria; AAB99577; AAB99577; MJ_1557.
DR KEGG; mja:MJ_1557; -.
DR eggNOG; arCOG10124; Archaea.
DR HOGENOM; CLU_022610_0_2_2; -.
DR InParanoid; Q58952; -.
DR OMA; IHYHETV; -.
DR PhylomeDB; Q58952; -.
DR BRENDA; 2.5.1.114; 3260.
DR EvolutionaryTrace; Q58952; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
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 GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01922; TYW2_archaea; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR030867; TYW2_archaea.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..249
FT /note="tRNA(Phe) (4-demethylwyosine(37)-C(7))
FT aminocarboxypropyltransferase"
FT /id="PRO_0000107411"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01922,
FT ECO:0000269|PubMed:19717466"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01922"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01922,
FT ECO:0000269|PubMed:19717466"
FT BINDING 154..155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3A27"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3A27"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 186..199
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3A27"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3A27"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 220..234
FT /evidence="ECO:0007829|PDB:3A27"
FT STRAND 237..248
FT /evidence="ECO:0007829|PDB:3A27"
SQ SEQUENCE 249 AA; 29302 MW; A4D1EB10B63CA51C CRC64;
MGIKYQKIGD VVIVKKELSE DEIREIVKRT KCKAILLYTT QITGEFRTPH VKILYGKETE
TIHKEYGCLF KLDVAKIMWS QGNIEERKRM AFISNENEVV VDMFAGIGYF TIPLAKYSKP
KLVYAIEKNP TAYHYLCENI KLNKLNNVIP ILADNRDVEL KDVADRVIMG YVHKTHKFLD
KTFEFLKDRG VIHYHETVAE KIMYERPIER LKFYAEKNGY KLIDYEVRKI KKYAPGVWHV
VVDAKFERI
