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Database: UniProt
Entry: V6YZ38_STRAG
LinkDB: V6YZ38_STRAG
Original site: V6YZ38_STRAG 
ID   V6YZ38_STRAG            Unreviewed;       447 AA.
AC   V6YZ38;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=gid {ECO:0000313|EMBL:ESV53892.1};
GN   Synonyms=trmFO {ECO:0000256|HAMAP-Rule:MF_01037};
GN   ORFNames=SAG0136_01160 {ECO:0000313|EMBL:ESV53892.1};
OS   Streptococcus agalactiae LMG 14747.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV53892.1, ECO:0000313|Proteomes:UP000018482};
RN   [1] {ECO:0000313|EMBL:ESV53892.1, ECO:0000313|Proteomes:UP000018482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV53892.1,
RC   ECO:0000313|Proteomes:UP000018482};
RA   Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., Stanhope M.J.,
RA   Town C.D., Venter J.C.;
RL   Submitted (MAY-2013) 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:ESV53892.1}.
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DR   EMBL; ANQC01000018; ESV53892.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6YZ38; -.
DR   eggNOG; COG1206; Bacteria.
DR   Proteomes; UP000018482; 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; 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   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          9..379
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ   SEQUENCE   447 AA;  49697 MW;  681938E5BB89BDA7 CRC64;
     MSQSIAKHIN VIGAGLAGSE AAYQIAKRGI PVKLYEMRGV KPTPQHKTAN FAELVCSNSF
     RGDSLTNAVG LLKEEMRRLD SIIMRNGENH RVPAGGAMAV DREGYAEAVT AELENHPLIE
     IIRGEITEIP DDTITVIATG PLTSDALAEK IHALNGGDGF YFYDAAAPII DKSTIDMDKV
     YLKSRYDKGE AAYLNCPMTK EEFMAFHEAL TTAEEAPLNS FEKEKYFEGC MPIEVMAKRG
     IKTMLYGPMK PVGLEYPDDY TGPRDGDFKT PYAVVQLRQD NAAGSLYNIV GFQTHLKWGE
     QKRVFQMIPG LENAEFVRYG VMHRNSYMDS PNLLTQTFAT RQNPNLFFAG QMTGVEGYVE
     SAASGLVAGI NAVRRFKDEE PVVFPHTTAI GALPYYVTHT ESKHFQPMNV NFGIIKELDG
     PRIRDKKERY EAIAERALTD LEAYLGY
//
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