ID A0A2L0F036_SORCE Unreviewed; 472 AA.
AC A0A2L0F036;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:AUX44839.1};
GN Synonyms=trmFO {ECO:0000256|HAMAP-Rule:MF_01037};
GN ORFNames=SOCE26_063080 {ECO:0000313|EMBL:AUX44839.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX44839.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX44839.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX44839.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-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; CP012673; AUX44839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0F036; -.
DR OrthoDB; 9803114at2; -.
DR Proteomes; UP000238348; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
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 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 PRINTS; PR00411; PNDRDTASEI.
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 9..396
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT REGION 192..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01037"
SQ SEQUENCE 472 AA; 51173 MW; 0B9151E5D57CA9F5 CRC64;
MNGAETPSDV TVVGGGLAGC EAAYQLAQRG LHVRLIEMKP HKRTPAQTSD RMAELVCSNS
LRGAALSNAV GLLKEELRRV GSLALRCADE TAVPAGGALA VDRERFAEAM TRMIEAHPRI
VVERREVTEI PGARPVILAT GPLTSDALAA SLAAAVGAEH LAYYDAIAPI VSADSIDWSR
VWKQSRYGKG VVARGERPAP EEEAAERRDE AEAGDEAYVN CPFDEAQYKA FVRALVESEK
VEARAFEEVR YFEGCLPCEV MAARGEQTLA FGPMKPVGLT DPRTGRRPYA VLQLRPEDEA
ATAYNLVGFQ TRMKYAEQLR VFRMVPGLEE AEFLRMGSVH RNTFVNAPVL LGPAMELHAL
PGVHLAGQIS GVEGYVESAA AGFVCAVLLS QRLRGEPLRP PPPTTALGGI LTHLGRPQPS
YQPSNITWAH IAPLDPAHGK LRKRARYEAM AERALRDLDA WWAEAEGRGV SS
//
