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Database: UniProt
Entry: A0A0T5NZC8_9RHOB
LinkDB: A0A0T5NZC8_9RHOB
Original site: A0A0T5NZC8_9RHOB 
ID   A0A0T5NZC8_9RHOB        Unreviewed;       454 AA.
AC   A0A0T5NZC8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000256|HAMAP-Rule:MF_01037};
DE            EC=2.1.1.74 {ECO:0000256|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01037};
GN   Name=trmFO {ECO:0000256|HAMAP-Rule:MF_01037};
GN   ORFNames=XM53_00455 {ECO:0000313|EMBL:KRS14247.1};
OS   Roseovarius atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS14247.1, ECO:0000313|Proteomes:UP000051295};
RN   [1] {ECO:0000313|EMBL:KRS14247.1, ECO:0000313|Proteomes:UP000051295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R12B {ECO:0000313|EMBL:KRS14247.1,
RC   ECO:0000313|Proteomes:UP000051295};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius sp.R12b.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine
CC       at position 54 (M-5-U54) in all tRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_01037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH +
CC         uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         methyluridine(54) in tRNA + NAD(+); Xref=Rhea:RHEA:16873, Rhea:RHEA-
CC         COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01037};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH +
CC         uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         methyluridine(54) in tRNA + NADP(+); Xref=Rhea:RHEA:62372, Rhea:RHEA-
CC         COMP:10167, Rhea:RHEA-COMP:10193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.74;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01037};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_01037};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01037}.
CC   -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01037}.
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:KRS14247.1}.
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DR   EMBL; LAXJ01000002; KRS14247.1; -; Genomic_DNA.
DR   RefSeq; WP_057789213.1; NZ_LAXJ01000002.1.
DR   AlphaFoldDB; A0A0T5NZC8; -.
DR   STRING; 1641875.XM53_00455; -.
DR   PATRIC; fig|1641875.4.peg.1172; -.
DR   OrthoDB; 9803114at2; -.
DR   Proteomes; UP000051295; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047151; F:tRNA (uracil(54)-C5)-methyltransferase activity, 5,10-methylenetetrahydrofolate-dependent; IEA:UniProtKB-EC.
DR   GO; GO:0030488; P:tRNA methylation; IEA:GOC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   HAMAP; MF_01037; TrmFO; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR040131; MnmG_N.
DR   InterPro; IPR004417; TrmFO.
DR   NCBIfam; TIGR00137; gid_trmFO; 1.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF2; METHYLENETETRAHYDROFOLATE--TRNA-(URACIL-5-)-METHYLTRANSFERASE TRMFO; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01037};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01037};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01037};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01037};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01037};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01037};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01037};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01037}.
FT   DOMAIN          5..374
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   454 AA;  49427 MW;  06226C74595273E3 CRC64;
     MTETLHIVGG GMAGSEAAWQ AANMGVRVVI HEMRPKVGTF AHQTGDLAEM VCSNSFRSDD
     DEQNAVGLLH WEMRAAGGLI MEMAETHRLP AGGALAVDRE AFSQGVTARL SDHPNVSIEK
     GEVTALPDDG RWIFATGPLT SQGLGAAIAA ETGTDRLAFF DAIAPIVYHD TIDMSQAWMQ
     SRYDKGATEE ERTAYLNCPM TKDQYEAFID ALLAADKTEF HEGETATYFD GCLPIEVMAE
     RGRETLRHGP MKPVGLTNPH QPDVKPWAVV QLRRDNALGT LYNIVGFQTK MKYGAQTDVF
     KMIPGLENAS FARLGGIHRN TFLNSPTLLD DQMRLRGKPH IRFAGQITGV EGYVESAAMG
     LLAGRLAASE ILGRPLPAPP QDTAMGALIH HITGGAEAKT FQPMNVNFGL FRPVDGLKGG
     RRGRRDRYKA YTDRAKAAWT GWLAETEVDA AETV
//
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