ID A0A1H8EF11_9FIRM Unreviewed; 218 AA.
AC A0A1H8EF11;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tRNA 5-hydroxyuridine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02217};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02217};
DE AltName: Full=ho5U methyltransferase {ECO:0000256|HAMAP-Rule:MF_02217};
GN Name=trmR {ECO:0000256|HAMAP-Rule:MF_02217};
GN ORFNames=SAMN05216454_10176 {ECO:0000313|EMBL:SEN17338.1};
OS Peptostreptococcus russellii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN17338.1, ECO:0000313|Proteomes:UP000199512};
RN [1] {ECO:0000313|EMBL:SEN17338.1, ECO:0000313|Proteomes:UP000199512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Calf135 {ECO:0000313|EMBL:SEN17338.1,
RC ECO:0000313|Proteomes:UP000199512};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form
CC 5-methoxyuridine (mo5U) at position 34 in tRNAs. {ECO:0000256|HAMAP-
CC Rule:MF_02217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-
CC methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60524, Rhea:RHEA-COMP:13381, Rhea:RHEA-COMP:15591,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:136877, ChEBI:CHEBI:143860; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02217};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02217}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_02217}.
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DR EMBL; FODF01000001; SEN17338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8EF11; -.
DR STRING; 215200.SAMN05216454_10176; -.
DR OrthoDB; 9799672at2; -.
DR Proteomes; UP000199512; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0016300; F:tRNA (uridine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02217; TrmR_methyltr; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR InterPro; IPR043675; TrmR_methyltr.
DR PANTHER; PTHR10509:SF14; CATECHOL O-METHYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR10509; O-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02217};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02217};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02217}; Reference proteome {ECO:0000313|Proteomes:UP000199512};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02217}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_02217}.
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 115..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
SQ SEQUENCE 218 AA; 24891 MW; 5ABBF478201C3574 CRC64;
MSNIVYDVVE DYIRETLEQN TGQIREMELY AEENSVPIIH KEVAELLKVI LKIHRPKRIL
EIGCAIGYSS ILFSSILDND VEIITTERNP VMLEKAVENI KKAGLEDKIK ILVGDAQETL
KDIDGEFDMI FIDAAKGQYK MFFDMVIDKL KVDGLVISDN ILYKGMIASD DLVVRRKKTI
VKRMRDYLDY ICQSDYLDTS IIPIGDGLAI SYKKSESK
//
