TRMA_GLAP5
ID TRMA_GLAP5 Reviewed; 369 AA.
AC B8F7Z1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=HAPS_1963;
OS Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Glaesserella.
OX NCBI_TaxID=557723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH0165;
RX PubMed=19074396; DOI=10.1128/jb.01682-08;
RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA Jin M., Jin Q., Chen H.;
RT "Complete genome sequence of Haemophilus parasuis SH0165.";
RL J. Bacteriol. 191:1359-1360(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; CP001321; ACL33443.1; -; Genomic_DNA.
DR RefSeq; WP_015940003.1; NC_011852.1.
DR AlphaFoldDB; B8F7Z1; -.
DR SMR; B8F7Z1; -.
DR STRING; 557723.HAPS_1963; -.
DR EnsemblBacteria; ACL33443; ACL33443; HAPS_1963.
DR KEGG; hap:HAPS_1963; -.
DR PATRIC; fig|557723.8.peg.1951; -.
DR HOGENOM; CLU_043022_0_0_6; -.
DR OMA; DHMESGV; -.
DR Proteomes; UP000006743; Chromosome.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..369
FT /note="tRNA/tmRNA (uracil-C(5))-methyltransferase"
FT /id="PRO_1000148888"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
FT BINDING 296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01011"
SQ SEQUENCE 369 AA; 42368 MW; 2AE54E6027F9A0E9 CRC64;
MTLPIHQYPA LLAKKAENLT ALLAPFNAPE LDVFASDTSH FRLRAEFRVW HDNGDLYHIM
FDQATKQRYR VDQFPIASQL INRMMTVLLA EIKGNELLTR KLFQIDYLST LSGQIAVSML
YHKSLTEEWI EQAKLLKQRL IGYGFDVQLI GRATKQKIAL DCDYVEEALN VDGQIYRYRQ
VENSFTQPNG KMNIKMLEWA RACTANSKGD LLELYCGNGN FSIALANQFR KVLATEISKS
SVESAQYNIA VNGVDNLQII RMSAEEFTEA MNGVRVFYRL RGIDLKQYDC NTIFVDPPRV
GLDQATLEMV QGYEKILYIS CNPHTLADNL KQLTQTHRIE RCALFDQFPY TEHIESGVWL
IRNNQVGEK
