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Database: UniProt
Entry: A0A0S6UT05_9BRAD
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Original site: A0A0S6UT05_9BRAD 
ID   A0A0S6UT05_9BRAD        Unreviewed;       475 AA.
AC   A0A0S6UT05;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=BDOA9_0146850 {ECO:0000313|EMBL:GAJ35479.1};
OS   Bradyrhizobium sp. DOA9.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ35479.1};
RN   [1] {ECO:0000313|EMBL:GAJ35479.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOA9 {ECO:0000313|EMBL:GAJ35479.1};
RX   PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA   Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA   Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA   Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT   "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT   Plasmid.";
RL   PLoS ONE 10:e0117392-e0117392(2015).
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; DF820425; GAJ35479.1; -; Genomic_DNA.
DR   RefSeq; WP_025036447.1; NZ_DF820425.1.
DR   AlphaFoldDB; A0A0S6UT05; -.
DR   STRING; 1126627.BDOA9_0146850; -.
DR   eggNOG; COG1206; Bacteria.
DR   OrthoDB; 9803114at2; -.
DR   Proteomes; UP000066441; 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..381
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   475 AA;  51010 MW;  95FF64EEA1550FB3 CRC64;
     MTGPQSNIVH VIGAGLAGSE AAWQVAKSGV PVVLHEMRPT RMTEAHRTDG LAELVCSNSF
     RSDDAANNAV GLLHAEMRRL DSLIMRAADA NQVPAGGALA VDRDGFSAAV TKALNDHPLI
     EIARGEIAGL PPADWSNVIV ATGPLTSAPL ADAIRELTDE NALAFFDAIA PIVHRESIDM
     SVAWFQSRYD KVGPGGNGAD YINCPMTKEQ YDSFVAALIA GEKTEFKEWE TNTPYFDGCL
     PIEVMAERGP ETLRHGPMKP VGLTNPHDPT TKAYAIVQLR QDNKLGTLYN IVGFQTKLKY
     GEQQRIFRTI PGLENAEFAR LGGLHRNTFL NSPKLLDAQL RLRAQPRLRF AGQMTGCEGY
     VESASVGLIA GLYAAADARG EALVSPPGTT ALGSLLGHIT GGHIETIEPG TRSFQPMNIN
     FGLFPPLASV PTKKPDGTRL RGNEKTVAKK QALSARALAD LDRWIADHLR IAAAA
//
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