ID F0S0X5_DESTD Unreviewed; 436 AA.
AC F0S0X5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Dester_0121 {ECO:0000313|EMBL:ADY72779.1};
OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Desulfurobacterium.
OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY72779.1, ECO:0000313|Proteomes:UP000007102};
RN [1] {ECO:0000313|EMBL:ADY72779.1, ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX PubMed=22675590; DOI=10.4056/sigs.2465574;
RA Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfur-reducer
RT Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT hydrothermal vent.";
RL Stand. Genomic Sci. 5:407-415(2011).
RN [2] {ECO:0000313|Proteomes:UP000007102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL Submitted (FEB-2011) 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; CP002543; ADY72779.1; -; Genomic_DNA.
DR RefSeq; WP_013637739.1; NC_015185.1.
DR AlphaFoldDB; F0S0X5; -.
DR STRING; 868864.Dester_0121; -.
DR KEGG; dte:Dester_0121; -.
DR eggNOG; COG1206; Bacteria.
DR HOGENOM; CLU_033057_1_0_0; -.
DR InParanoid; F0S0X5; -.
DR OrthoDB; 9803114at2; -.
DR Proteomes; UP000007102; 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; 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:UP000007102};
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..368
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 436 AA; 49016 MW; 31C39393DB8114F3 CRC64;
MKEIINVIGA GLAGVEAAYK VANKGHKVRL FEMRPKKTTP AHKTSLFAEL VCSNTLGGKE
VTTPRGLLKA EMELLNSLIV EAARKTEVPA GGALAVDREK FAEYITEKIE NHPNIEVVRE
EVTEIPKEGI TIVASGPLTS DKFSEYLRNY LGEKELHFYD AISPIVYADT IDYSKCFWGS
RYGKGGDDYL NCPMTEEEYE RFYTALMEAE KVPLKDFEKA CYFEGCMPIE EMAERGKQTL
LFGPLKPVGL IDPKTGKRPF AVVQLRKENK EGTLLNLVGF QTKLKYPEQK RVFRLIPGLE
NAEFARFGSI HRNTFIKSPK LLLKTLQLKK NPKVFFAGQI TGVEGYPESA ATGIIAGINA
VKLAEGKELV YPPETTMIGA LLKYITTADP KTFQPMNANF GILLPPEKKI RGKRERRKYL
AERALEDMKK WLELVY
//
