ID A0A1B2M157_9GAMM Unreviewed; 363 AA.
AC A0A1B2M157;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE EC=2.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
DE Short=RUMT {ECO:0000256|HAMAP-Rule:MF_01011};
DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01011};
GN Name=trmA {ECO:0000256|HAMAP-Rule:MF_01011};
GN ORFNames=BFG52_10600 {ECO:0000313|EMBL:AOA58753.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA58753.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA58753.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA58753.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_01011};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. TrmA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01011}.
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DR EMBL; CP016895; AOA58753.1; -; Genomic_DNA.
DR RefSeq; WP_067555807.1; NZ_CP016895.1.
DR AlphaFoldDB; A0A1B2M157; -.
DR STRING; 1789224.BFG52_10600; -.
DR KEGG; ala:BFG52_10600; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000093391; Chromosome.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:UniProtKB-UniRule.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR02143; trmA_only; 1.
DR PANTHER; PTHR47790; TRNA/TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR47790:SF2; TRNA_TMRNA (URACIL-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01011}; Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01011};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01011}.
FT ACT_SITE 319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01011,
FT ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 363 AA; 42092 MW; 462F994AFD12677E CRC64;
MTSAYQQQLA EKVERIQQQF QVFQAPPLQV FPSAEQNFRM RAEFRIWHQE DDLFYAMFER
SPDQKQKIVQ RIEQFPIAHQ SINQLMPILL TEIKNNLHLS KRLFEIHFLC TLHGDMLVSL
IYHRQLDADW HSAAATLAQQ LNINLIGRCR GEKYVFGEQF VLEQLTVSAR DYCYKQYENS
FTQPNAVVCQ SMLQWAVDAI AGDNQDLLEL YCGNGNFTLP LSTQFNKVLA TELAKSSVQA
AQWNIARNHI ENIKVARLSA EEFSQAFRGE RQFRRLQEAD IALADYQFDT IFVDPPRAGI
DADTLALMQQ FPKILYISCN PDTLYDNLQQ LCKTHKIVQF ALFDQFPYTH HVESGVLLEK
VTT
//
