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Database: UniProt
Entry: A0A0P0A7S1_9RHOB
LinkDB: A0A0P0A7S1_9RHOB
Original site: A0A0P0A7S1_9RHOB 
ID   A0A0P0A7S1_9RHOB        Unreviewed;       448 AA.
AC   A0A0P0A7S1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=IMCC12053_489 {ECO:0000313|EMBL:ALI54438.1};
OS   Celeribacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI54438.1, ECO:0000313|Proteomes:UP000064920};
RN   [1] {ECO:0000313|EMBL:ALI54438.1, ECO:0000313|Proteomes:UP000064920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI54438.1,
RC   ECO:0000313|Proteomes:UP000064920};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-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}.
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DR   EMBL; CP012023; ALI54438.1; -; Genomic_DNA.
DR   RefSeq; WP_062215394.1; NZ_FOSM01000008.1.
DR   AlphaFoldDB; A0A0P0A7S1; -.
DR   STRING; 1397108.IMCC12053_489; -.
DR   KEGG; cmar:IMCC12053_489; -.
DR   PATRIC; fig|1397108.4.peg.505; -.
DR   OrthoDB; 9803114at2; -.
DR   Proteomes; UP000064920; Chromosome.
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; IPR020595; MnmG-rel_CS.
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.
DR   PROSITE; PS01281; GIDA_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000064920};
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          6..375
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   448 AA;  48636 MW;  1EEDDB8B743EC88B CRC64;
     MTDKTLHIVG GGMAGSEAAW QAANLGINVV LHEMRPKVET FAHQTGNFGE MVCSNSFRSD
     DDEQNAVGLL HWEMRAAGGL VMASADANKL PAGGALAVDR EAFAEHITAK INAHPLISVE
     FGEVSELPTD GTWLFATGPL TSPALGAAIA AETGTDRLAF FDAIAPIVYA DSVNMDIAWL
     QSRYDKGETE EEQKAYLNCP MTKDQYEAFI DALAAADKTE FHEGETAGYF DGCLPIEVMA
     ERGRETLRFG PMKPVGLTNA NGPENKPYAV VQLRRDNKLG TLYNIVGFQT KMKYGAQTEV
     FKMIPGLEDA SFARLGGIHR NTFLNSPTLL DDQMRLKSRP NIRFAGQVTG VEGYVESAAM
     GLLAGRMAAA ELLGRDLPPP PFTTAMGALI NHITGGAEAK TFQPMNVNFG LFPPLDGMRG
     GRKGRKERYK GYTDRAKDDY NQWLDGQI
//
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