TRMH_THET8
ID TRMH_THET8 Reviewed; 194 AA.
AC Q5SM16; Q9FAC4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000305};
DE EC=2.1.1.34 {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000269|PubMed:11918670, ECO:0000269|PubMed:15062082, ECO:0000269|PubMed:20053984, ECO:0000269|PubMed:23867454};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000305};
GN Name=trmH {ECO:0000255|HAMAP-Rule:MF_02060, ECO:0000303|PubMed:11918670};
GN OrderedLocusNames=TTHA0127 {ECO:0000312|EMBL:BAD69950.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=11918670; DOI=10.1046/j.1365-2443.2002.00520.x;
RA Hori H., Suzuki T., Sugawara K., Inoue Y., Shibata T., Kuramitsu S.,
RA Yokoyama S., Oshima T., Watanabe K.;
RT "Identification and characterization of tRNA (Gm18) methyltransferase from
RT Thermus thermophilus HB8: domain structure and conserved amino acid
RT sequence motifs.";
RL Genes Cells 7:259-272(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRNA-BINDING.
RX PubMed=20053984; DOI=10.1074/jbc.m109.065698;
RA Ochi A., Makabe K., Kuwajima K., Hori H.;
RT "Flexible recognition of the tRNA G18 methylation target site by TrmH
RT methyltransferase through first binding and induced fit processes.";
RL J. Biol. Chem. 285:9018-9029(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND TRNA-BINDING.
RX PubMed=23867454; DOI=10.1074/jbc.m113.485128;
RA Ochi A., Makabe K., Yamagami R., Hirata A., Sakaguchi R., Hou Y.M.,
RA Watanabe K., Nureki O., Kuwajima K., Hori H.;
RT "The catalytic domain of topological knot tRNA methyltransferase (TrmH)
RT discriminates between substrate tRNA and nonsubstrate tRNA via an induced-
RT fit process.";
RL J. Biol. Chem. 288:25562-25574(2013).
RN [5] {ECO:0007744|PDB:1V2X}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ARG-41; THR-99; LEU-101; GLU-124;
RP VAL-128; ILE-142; MET-144; SER-150; LEU-151 AND ASN-152.
RX PubMed=15062082; DOI=10.1016/j.str.2004.03.003;
RA Nureki O., Watanabe K., Fukai S., Ishii R., Endo Y., Hori H., Yokoyama S.;
RT "Deep knot structure for construction of active site and cofactor binding
RT site of tRNA modification enzyme.";
RL Structure 12:593-602(2004).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. Type I methylase, which methylates all tRNAs.
CC {ECO:0000269|PubMed:11918670, ECO:0000269|PubMed:15062082,
CC ECO:0000269|PubMed:20053984, ECO:0000269|PubMed:23867454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02060,
CC ECO:0000269|PubMed:11918670, ECO:0000269|PubMed:15062082,
CC ECO:0000269|PubMed:20053984, ECO:0000269|PubMed:23867454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15062082};
CC Vmax=10 umol/h/mg enzyme {ECO:0000269|PubMed:15062082};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15062082}.
CC -!- DOMAIN: Both N- and C-terminal regions function in tRNA binding, but
CC the substrate tRNA is determined by the catalytic domain.
CC {ECO:0000269|PubMed:23867454}.
CC -!- MISCELLANEOUS: Binding of TrmH to tRNA is composed of at least three
CC steps: the first is bi-molecular binding and the subsequent two are
CC uni-molecular induced-fit processes. {ECO:0000269|PubMed:20053984}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000255|HAMAP-
CC Rule:MF_02060, ECO:0000305}.
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DR EMBL; AB045130; BAB17605.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69950.1; -; Genomic_DNA.
DR RefSeq; WP_011174221.1; NC_006461.1.
DR RefSeq; YP_143393.1; NC_006461.1.
DR PDB; 1V2X; X-ray; 1.50 A; A=1-194.
DR PDBsum; 1V2X; -.
DR AlphaFoldDB; Q5SM16; -.
DR SMR; Q5SM16; -.
DR STRING; 300852.55771509; -.
DR PRIDE; Q5SM16; -.
DR EnsemblBacteria; BAD69950; BAD69950; BAD69950.
DR GeneID; 3168939; -.
DR KEGG; ttj:TTHA0127; -.
DR PATRIC; fig|300852.9.peg.125; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_0; -.
DR OMA; KIPMVGF; -.
DR PhylomeDB; Q5SM16; -.
DR BRENDA; 2.1.1.34; 2305.
DR SABIO-RK; Q5SM16; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002938; P:tRNA guanine ribose methylation; IDA:UniProtKB.
DR CDD; cd18092; SpoU-like_TrmH; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_02060; tRNA_methyltr_TrmH; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR022724; rRNA_MeTrfase_SpoU_C.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR033671; TrmH.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR43453; PTHR43453; 1.
DR Pfam; PF12105; SpoU_methylas_C; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..194
FT /note="tRNA (guanosine(18)-2'-O)-methyltransferase"
FT /id="PRO_0000436160"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060,
FT ECO:0000269|PubMed:15062082, ECO:0007744|PDB:1V2X"
FT BINDING 122..126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060,
FT ECO:0000269|PubMed:15062082, ECO:0007744|PDB:1V2X"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060,
FT ECO:0000269|PubMed:15062082, ECO:0007744|PDB:1V2X"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02060,
FT ECO:0000269|PubMed:15062082, ECO:0007744|PDB:1V2X"
FT MUTAGEN 41
FT /note="R->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 41
FT /note="R->K: 30-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 99
FT /note="T->A: Small increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 101
FT /note="L->A: 13-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 124
FT /note="E->A: 2800-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 128
FT /note="V->A: Small increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 142
FT /note="I->A: No change in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 144
FT /note="M->A: 15-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 150
FT /note="S->A: 170-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 151
FT /note="L->A: Small increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT MUTAGEN 152
FT /note="N->A: 80-fold increase in Km for AdoMet."
FT /evidence="ECO:0000269|PubMed:15062082"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1V2X"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1V2X"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1V2X"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1V2X"
SQ SEQUENCE 194 AA; 22084 MW; F499BB7E9AC1F5BF CRC64;
MRERTEARRR RIEEVLRRRQ PDLTVLLENV HKPHNLSAIL RTCDAVGVLE AHAVNPTGGV
PTFNETSGGS HKWVYLRVHP DLHEAFRFLK ERGFTVYATA LREDARDFRE VDYTKPTAVL
FGAEKWGVSE EALALADGAI KIPMLGMVQS LNVSVAAAVI LFEAQRQRLK AGLYDRPRLD
PELYQKVLAD WLRK
