ID B7JYL8_RIPO1 Unreviewed; 459 AA. AC B7JYL8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 89. 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=PCC8801_0806 {ECO:0000313|EMBL:ACK64888.1}; OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC OS 8801)). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis. OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK64888.1, ECO:0000313|Proteomes:UP000008204}; RN [1] {ECO:0000313|Proteomes:UP000008204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204}; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., RA Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of RT unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). 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, ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP001287; ACK64888.1; -; Genomic_DNA. DR RefSeq; WP_012594164.1; NC_011726.1. DR AlphaFoldDB; B7JYL8; -. DR STRING; 41431.PCC8801_0806; -. DR KEGG; cyp:PCC8801_0806; -. DR eggNOG; COG1206; Bacteria. DR HOGENOM; CLU_033057_1_0_3; -. DR OrthoDB; 9803114at2; -. DR Proteomes; UP000008204; 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:UP000008204}; 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..380 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 459 AA; 50805 MW; 072BE7030E92E378 CRC64; MNDRSTTTIQ VIGGGLAGTE AAWQIAQAGV PVILYEMRPL RTSPAHHSEE LAELVCSNSF GAMSSDRAAG LLHEELRRLG SIIIQTADQH SVPAGGALAV DRGVFSHALT QTLDNHPLIT LKRAAIGQIP SEGIVVLTTG PLTTPDLAED LQRFTGMDYL SFFDAASPII VGDSINRDIA FLASRYDKGE AAYLNCPLTK EQYLHFREEL CQAEQAELKD FERETAQFFE GCLPIEELAK RGEDTMRYGP LKPVGLFDSR LGDFRDPENK GKRPYGVVQL RQEDKNGQLW NMVGFQTNLK WGEQKRIFRL IPGLETAEFV RMGVMHRNTF INSPQLLEAT LQFKSRPTLL AAGQLIGTEG YSAAAAGGWL AGTNAARLAL RLDPLKMPET TMMGALFEFI SSASPKHFQP MPPNFGIIPE LSHKIGNKRE RYGKYRDRAL ADLETWNNQS VNKRSLCVQ //