TRML_ECOLI
ID TRML_ECOLI Reviewed; 157 AA.
AC P0AGJ7; P33899; Q2M7S0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=tRNA (cytidine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01885};
DE EC=2.1.1.207 {ECO:0000255|HAMAP-Rule:MF_01885};
DE AltName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmL {ECO:0000255|HAMAP-Rule:MF_01885};
GN Name=trmL {ECO:0000255|HAMAP-Rule:MF_01885}; Synonyms=yibK;
GN OrderedLocusNames=b3606, JW3581;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8407843; DOI=10.1128/jb.175.20.6671-6678.1993;
RA Dong J.M., Taylor J.S., Latour D.J., Iuchi S., Lin E.C.C.;
RT "Three overlapping lct genes involved in L-lactate utilization by
RT Escherichia coli.";
RL J. Bacteriol. 175:6671-6678(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-157.
RC STRAIN=K12;
RX PubMed=2108679; DOI=10.1016/0006-291x(90)90615-t;
RA Tei H., Murata K., Kimura A.;
RT "Structure and expression of cysX, the second gene in the Escherichia coli
RT K-12 cysE locus.";
RL Biochem. Biophys. Res. Commun. 167:948-955(1990).
RN [6]
RP IDENTIFICATION.
RX PubMed=8265370; DOI=10.1093/nar/21.23.5519;
RA Koonin E.V., Rudd K.E.;
RT "SpoU protein of Escherichia coli belongs to a new family of putative rRNA
RT methylases.";
RL Nucleic Acids Res. 21:5519-5519(1993).
RN [7]
RP FUNCTION AS A METHYLTRANSFERASE, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20855540; DOI=10.1261/rna.2245910;
RA Benitez-Paez A., Villarroya M., Douthwaite S., Gabaldon T., Armengod M.E.;
RT "YibK is the 2'-O-methyltransferase TrmL that modifies the wobble
RT nucleotide in Escherichia coli tRNALeu isoacceptors.";
RL RNA 16:2131-2143(2010).
CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in
CC the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA).
CC Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH
CC of the wobble nucleotide. Recognition of the target requires a pyridine
CC at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position
CC 37. {ECO:0000255|HAMAP-Rule:MF_01885, ECO:0000269|PubMed:20855540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01885,
CC ECO:0000269|PubMed:20855540};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-
CC adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-
CC methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43088, Rhea:RHEA-COMP:10333, Rhea:RHEA-COMP:10334,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74508, ChEBI:CHEBI:74511; EC=2.1.1.207;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01885,
CC ECO:0000269|PubMed:20855540};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01885,
CC ECO:0000269|PubMed:20855540}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01885}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01885}.
CC -!- CAUTION: Possibly identical to GltE. {ECO:0000305}.
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DR EMBL; L13970; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U00039; AAB18583.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76630.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77686.1; -; Genomic_DNA.
DR EMBL; M34333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S47827; S47827.
DR RefSeq; NP_418063.1; NC_000913.3.
DR RefSeq; WP_000932347.1; NZ_SSZK01000022.1.
DR PDB; 4JAK; X-ray; 2.00 A; A/B=2-157.
DR PDB; 4JAL; X-ray; 2.00 A; A/B=2-157.
DR PDBsum; 4JAK; -.
DR PDBsum; 4JAL; -.
DR AlphaFoldDB; P0AGJ7; -.
DR SMR; P0AGJ7; -.
DR BioGRID; 4262552; 53.
DR IntAct; P0AGJ7; 7.
DR STRING; 511145.b3606; -.
DR jPOST; P0AGJ7; -.
DR PaxDb; P0AGJ7; -.
DR PRIDE; P0AGJ7; -.
DR EnsemblBacteria; AAC76630; AAC76630; b3606.
DR EnsemblBacteria; BAE77686; BAE77686; BAE77686.
DR GeneID; 948119; -.
DR KEGG; ecj:JW3581; -.
DR KEGG; eco:b3606; -.
DR PATRIC; fig|1411691.4.peg.3100; -.
DR EchoBASE; EB1834; -.
DR eggNOG; COG0219; Bacteria.
DR HOGENOM; CLU_110125_1_0_6; -.
DR InParanoid; P0AGJ7; -.
DR OMA; AGLDYWH; -.
DR PhylomeDB; P0AGJ7; -.
DR BioCyc; EcoCyc:EG11888-MON; -.
DR BioCyc; MetaCyc:EG11888-MON; -.
DR BRENDA; 2.1.1.207; 2026.
DR PRO; PR:P0AGJ7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0002131; P:wobble position cytosine ribose methylation; IMP:EcoCyc.
DR GO; GO:0002132; P:wobble position uridine ribose methylation; IMP:EcoCyc.
DR CDD; cd18094; SpoU-like_TrmL; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_01885; tRNA_methyltr_TrmL; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR016914; tRNA_cyt/urid_MeTfrase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42971; PTHR42971; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF029256; SpoU_TrmH_prd; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00185; tRNA_yibK_trmL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..157
FT /note="tRNA (cytidine(34)-2'-O)-methyltransferase"
FT /id="PRO_0000159817"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01885"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4JAK"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4JAK"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4JAL"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4JAK"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4JAK"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:4JAK"
SQ SEQUENCE 157 AA; 17726 MW; BF065D29B86C341B CRC64;
MLNIVLYEPE IPPNTGNIIR LCANTGFRLH IIEPMGFAWD DKRLRRAGLD YHEFTAVTRH
HDYRAFLEAE NPQRLFALTT KGTPAHSAVS YQDGDYLMFG PETRGLPASI LDALPAEQKI
RIPMVPDSRS MNLSNAVSVV VYEAWRQLGY PGAVLRD
