ID A0A0N0LZL7_9SPHN Unreviewed; 449 AA.
AC A0A0N0LZL7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=ADT71_14080 {ECO:0000313|EMBL:KPH63041.1}, EDF59_12229
GN {ECO:0000313|EMBL:TCM32530.1};
OS Novosphingobium sp. ST904.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH63041.1, ECO:0000313|Proteomes:UP000037878};
RN [1] {ECO:0000313|EMBL:KPH63041.1, ECO:0000313|Proteomes:UP000037878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:KPH63041.1,
RC ECO:0000313|Proteomes:UP000037878};
RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F.,
RA Vangronsveld J.;
RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol and
RT stimulates plant growth.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TCM32530.1, ECO:0000313|Proteomes:UP000295740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST904 {ECO:0000313|EMBL:TCM32530.1,
RC ECO:0000313|Proteomes:UP000295740};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (MAR-2019) 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:KPH63041.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGJH01000146; KPH63041.1; -; Genomic_DNA.
DR EMBL; SLVC01000022; TCM32530.1; -; Genomic_DNA.
DR RefSeq; WP_054437796.1; NZ_SLVC01000022.1.
DR AlphaFoldDB; A0A0N0LZL7; -.
DR STRING; 1684385.ADT71_14080; -.
DR PATRIC; fig|1684385.3.peg.2508; -.
DR OrthoDB; 9803114at2; -.
DR Proteomes; UP000037878; Unassembled WGS sequence.
DR Proteomes; UP000295740; 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; 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:UP000037878};
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 4..378
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 449 AA; 49373 MW; 504EC4828B513DA5 CRC64;
MTQDVHIIGG GLAGSEAAWQ LGRRGFRVRL SEMRGTGERS PAHQGDGLAE LVCSNSFRSD
DHEKNAVGLL HHEMRGCDSL IMSAAAKAQV PAGSALAVDR DVFSAEVEAR LSALPNVEIV
RERIDTLPET GTTIVATGPL TAESLAGSIG RATGSDSLAF FDAIAPIVYR DSIDMDVCWM
ASRWDKGETK DYINCPMDKD QYLAFHQALL NGEKTAFKEW EENTPYFDGC MPIEVMAERG
VETLRFGPMK PVGLDNPHWA TPEHPNGRWA YAVVQLRQDN KLGTIWNMVG FQTKLKHAEQ
VRLFRTIPGL ENAEFARLGG LHRNTFLNSP ILLDRQFRLK TALHVRFAGQ ITGCEGYVES
AAVGLMAGLM TAAELSGRDW QTPPRTTALG ALLSHITGDA EAETYQPMNV NFGLFPPLHD
VKKKQRKEAY TSRAKEEIAP WLEGLVPTA
//
