ID A0A0B0KIN5_9GAMM Unreviewed; 361 AA.
AC A0A0B0KIN5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=PJ15_2318 {ECO:0000313|EMBL:KHF76109.1};
OS Acinetobacter sp. neg1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1561068 {ECO:0000313|EMBL:KHF76109.1, ECO:0000313|Proteomes:UP000030886};
RN [1] {ECO:0000313|EMBL:KHF76109.1, ECO:0000313|Proteomes:UP000030886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=neg1 {ECO:0000313|Proteomes:UP000030886};
RA Chiara M., Horner D.S., Pesole G., Mule' G., Logrieco A., Fanelli F.;
RT "Genome Sequencing of an Acinetobacter spp capable to degrade OTA.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF76109.1}.
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DR EMBL; JSZD01000020; KHF76109.1; -; Genomic_DNA.
DR RefSeq; WP_047432811.1; NZ_JSZD01000020.1.
DR AlphaFoldDB; A0A0B0KIN5; -.
DR PATRIC; fig|1561068.3.peg.3318; -.
DR Proteomes; UP000030886; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01011};
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 361 AA; 41942 MW; E7BD9A794784809D CRC64;
MTVSYQQQLQ EKVERITAQF APFNPPALEV FQSPEQHFRM RAEFRIWHTE DDMFYAMFER
AEDGKQKDVV RVDEFPIADQ SINDLMPRLL EELKAVPVLS QRIFEADFLA TLSGEMLVTL
IYHRKLDEEW ETAAKALAEK LNIKIMGRSR GQKVIIGEDY VVEQLNVHDR TFKYKQIESS
FTQPNAQVCQ HMLEWACDAA QGSQKDLLEL YCGNGNFTLP LSLKFKRVLA TELAKSSVYA
AQWNIEQNQI ENIQVARLSA EEFTQAYQGE REFRRLQEAN IDIQSYDFDT VFVDPPRAGI
DDETLKLLQG FERILYISCN PDTLHDNLNT LTQTHRIVKF AMFDQFPFTH HVESGVLLEK
I
//
