TRMA_ECOBR
ID TRMA_ECOBR Reviewed; 366 AA.
AC C6UJK3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011};
DE EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011};
DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
GN Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011}; OrderedLocusNames=ECB_03850;
OS Escherichia coli (strain B / REL606).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=413997;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / REL606;
RX PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL J. Mol. Biol. 394:644-652(2009).
CC -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the
CC formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and
CC that of position 341 (m5U341) in tmRNA (transfer-mRNA).
CC {ECO:0000255|HAMAP-Rule:MF_01011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(341) in tmRNA = 5-
CC methyluridine(341) in tmRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43612, Rhea:RHEA-COMP:10630, Rhea:RHEA-COMP:10631,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01011};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01011}.
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DR EMBL; CP000819; ACT41487.1; -; Genomic_DNA.
DR RefSeq; WP_000187022.1; NC_012967.1.
DR AlphaFoldDB; C6UJK3; -.
DR SMR; C6UJK3; -.
DR GeneID; 66672123; -.
DR KEGG; ebr:ECB_03850; -.
DR HOGENOM; CLU_043022_0_0_6; -.
DR OMA; DHMESGV; -.
DR BioCyc; ECOL413997:GCQD-4099-MON; -.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011869; TrmA_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR47790; PTHR47790; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02143; trmA_only; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..366
FT /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT /id="PRO_0000388556"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ SEQUENCE 366 AA; 41967 MW; A7A65FD98380D27D CRC64;
MTPEHLPTEQ YEAQLAEKVV RLQSMMAPFS DLVPEVFRSP VSHYRMRAEF RIWHDGDDLY
HIIFDQQTKS RIRVDSFPAA SELINQLMTA MIAGVRNNPV LRHKLFQIDY LTTLSNQAVV
SLLYHKKLDD EWRQEAEALR DALRAQNLNV HLIGRATKTK IELDQDYIDE RLPVAGKEMI
YRQVENSFTQ PNAAMNIQML EWALDVTKGS KGDLLELYCG NGNFSLALAR NFDRVLATEI
AKPSVAAAQY NIAANHIDNV QIIRMAAEEF TQAMNGVREF NRLQGIDLKS YQCETIFVDP
PRSGLDSETE KMVQAYPRIL YISCNPETLC KNLETLSQTH KVERLALFDQ FPYTHHMECG
VLLTAK
