ID I0K102_METFB Unreviewed; 445 AA.
AC I0K102;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:CCG93171.1};
GN ORFNames=MFUM_940046 {ECO:0000313|EMBL:CCG93171.1};
OS Methylacidiphilum fumariolicum (strain SolV).
OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG93171.1, ECO:0000313|Proteomes:UP000004837};
RN [1] {ECO:0000313|EMBL:CCG93171.1, ECO:0000313|Proteomes:UP000004837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolV {ECO:0000313|EMBL:CCG93171.1,
RC ECO:0000313|Proteomes:UP000004837};
RX PubMed=22740660; DOI=10.1128/JB.00501-12;
RA Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R.,
RA Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J.,
RA Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A.,
RA Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.;
RT "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic
RT Methanotroph Methylacidiphilum fumariolicum Strain SolV.";
RL J. Bacteriol. 194:3729-3730(2012).
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:CCG93171.1}.
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DR EMBL; CAHT01000104; CCG93171.1; -; Genomic_DNA.
DR RefSeq; WP_009061685.1; NZ_CAHT01000104.1.
DR AlphaFoldDB; I0K102; -.
DR STRING; 1156937.GCA_000953475_00418; -.
DR eggNOG; COG1206; Bacteria.
DR InParanoid; I0K102; -.
DR OrthoDB; 9803114at2; -.
DR Proteomes; UP000004837; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000004837};
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..374
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 445 AA; 49463 MW; A2D5D9262785A404 CRC64;
MKFCSAKGIV VIGGGLAGSE AAWQIAQRGI PVFLYEMRPF IPTGAHSGSN LAEIVCSNSF
GSNLLSNASG LLLQELRILD SLLISIADSC SVPAGKSLAV DRERFSQMVT QNILKEPNIT
LIREEVVDLV FDSICIIATG PLTSPRLAAR LEALTQSNSL YFYDALCPIV DASSIDFSSA
FKASRYMDPA NSGDYVNCPL TKEQYLELSR ELANAERINL HDFEKELYFE GCLPIEIMAK
RGEDTLRFGP LRPTGLIDPK TNKRPYAVVQ LRQDNLAASL YNMVGFQTNL TYKEQDRIFR
MIPALKNAEF IRYGQLHRNT FINAPKLLLP TLQFKDNPLL FFAGQLAGFE GYAANIASGL
VAGINASRLF QGKEPIIFPR QTMIGELLWY ICHADPLHFQ PMKANFGLFD LTLEKNLPRD
KAARNLFLSQ RSLSNIEAFV RTILA
//
