ID Q8RGI1_FUSNN Unreviewed; 215 AA.
AC Q8RGI1;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 97.
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 OrderedLocusNames=FN0314 {ECO:0000313|EMBL:AAL94520.1};
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL94520.1, ECO:0000313|Proteomes:UP000002521};
RN [1] {ECO:0000313|EMBL:AAL94520.1, ECO:0000313|Proteomes:UP000002521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 /
RC KCTC 2640 / LMG 13131 / VPI 4355 {ECO:0000313|Proteomes:UP000002521};
RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N., Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2] {ECO:0007829|PDB:8K1F}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RA He S.R., Bai X.;
RT "Crystal Structure of TrmR from Fusobacterium nucleatum.";
RL Submitted (JUL-2023) to the PDB data bank.
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; AE009951; AAL94520.1; -; Genomic_DNA.
DR RefSeq; NP_603221.1; NC_003454.1.
DR RefSeq; WP_011016305.1; NZ_CP028101.1.
DR PDB; 8K1F; X-ray; 2.40 A; A/B/C=1-215.
DR AlphaFoldDB; Q8RGI1; -.
DR SMR; Q8RGI1; -.
DR STRING; 190304.FN0314; -.
DR PaxDb; 190304-FN0314; -.
DR EnsemblBacteria; AAL94520; AAL94520; FN0314.
DR GeneID; 79783323; -.
DR KEGG; fnu:FN0314; -.
DR PATRIC; fig|190304.8.peg.894; -.
DR eggNOG; COG4122; Bacteria.
DR HOGENOM; CLU_067676_4_0_0; -.
DR InParanoid; Q8RGI1; -.
DR BioCyc; FNUC190304:G1FZS-911-MONOMER; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:8K1F};
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:UP000002521};
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 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02217"
SQ SEQUENCE 215 AA; 25037 MW; 8929806CDA41A8BB CRC64;
MLEELKEANE YISSKIDKYK SPNLELIKEI EKDAEINNVP IISKEIREYL KFIIRTNKNI
KNILEIGTAT GYSGIIMSEE IQGRNGTLTT IEIDEDRFKI AQSNFEKSNL KGIEQILGDA
TEEIEKLNKN FDFIFIDAAK GQYKKFFEDS YKLLNECGIV FVDNILFRGY LYKESPKRFK
TIVKRLDEFV NYLYENFDFV LLPISDGVGI IHKPF
//
