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TRMFO_MYXXD
ID   TRMFO_MYXXD             Reviewed;         457 AA.
AC   Q9S449; Q1D807; Q84F98;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000255|HAMAP-Rule:MF_01037};
DE            EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
DE   AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
GN   Name=trmFO {ECO:0000255|HAMAP-Rule:MF_01037}; Synonyms=gid, gidA;
GN   OrderedLocusNames=MXAN_3007;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10844655; DOI=10.1046/j.1365-2958.2000.01887.x;
RA   White D.J., Hartzell P.L.;
RT   "AglU, a protein required for gliding motility and spore maturation in
RT   Myxococcus xanthus, is related to WD-repeat proteins.";
RL   Mol. Microbiol. 36:662-678(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12828649; DOI=10.1046/j.1365-2958.2003.03582.x;
RA   Youderian P.A., Burke N., White D.J., Hartzell P.L.;
RT   "Identification of genes required for adventurous gliding motility in
RT   Myxococcus xanthus with the transposable element mariner.";
RL   Mol. Microbiol. 49:555-570(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN   [4]
RP   FAD-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=11703671; DOI=10.1046/j.1365-2958.2001.02659.x;
RA   White D.J., Merod R., Thomasson B., Hartzell P.L.;
RT   "GidA is an FAD-binding protein involved in development of Myxococcus
RT   xanthus.";
RL   Mol. Microbiol. 42:503-517(2001).
CC   -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine
CC       at position 54 (M-5-U54) in all tRNAs. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01037};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01037,
CC         ECO:0000269|PubMed:11703671};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037,
CC       ECO:0000269|PubMed:11703671}.
CC   -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01037}.
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DR   EMBL; AF162663; AAD46374.1; -; Genomic_DNA.
DR   EMBL; AY204472; AAO22919.1; -; Genomic_DNA.
DR   EMBL; CP000113; ABF92331.1; -; Genomic_DNA.
DR   RefSeq; WP_011553063.1; NC_008095.1.
DR   AlphaFoldDB; Q9S449; -.
DR   SMR; Q9S449; -.
DR   STRING; 246197.MXAN_3007; -.
DR   EnsemblBacteria; ABF92331; ABF92331; MXAN_3007.
DR   GeneID; 41360368; -.
DR   KEGG; mxa:MXAN_3007; -.
DR   eggNOG; COG1206; Bacteria.
DR   HOGENOM; CLU_033057_1_0_7; -.
DR   OMA; MHRNTFL; -.
DR   OrthoDB; 516534at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 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   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF2; PTHR11806:SF2; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00137; gid_trmFO; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; Methyltransferase; NAD; NADP;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..457
FT                   /note="Methylenetetrahydrofolate--tRNA-(uracil-5-)-
FT                   methyltransferase TrmFO"
FT                   /id="PRO_0000117253"
FT   BINDING         12..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01037"
FT   CONFLICT        126..127
FT                   /note="EQ -> DE (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="Y -> S (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="D -> N (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="Q -> H (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="R -> L (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="I -> M (in Ref. 1; AAD46374)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  49764 MW;  BE51C4E247353970 CRC64;
     MADQKQRVTV IGGGLAGTEC AYQLSRRGVP VVLREMKPQK RSPAHKSDTL AELVCSNSLR
     SDNPESAIGL LHAELRALGS LVLSAADANR VPAGDALAVE RERFSAAITE SLLRQPGVEL
     VAGEVEQLPE DGPVVIATGP LTSDALTREL ERHVGTRLYF YDSIAPILSA DSIDMNVAFR
     QSRYGKGGGD DYLNLPMTKD EYYRFIAEVK AGQKVVPHAF EEPKYFEGCL PIEVMAERGD
     DTLAYGPMKP VGLRDPRTGQ EPYAVVQLRM EDVGGTSWNM VGFQTRLTWG EQKRIFSSFI
     PGLQQAEFLR MGQIHRNTFI DSPRLLAKDL SLKTEPRLYF AGQISGVEGY VESAACGYLV
     ALALHARLTG TEFVPPPATT AMGALLRHVT GEAHPPDYPH QPSNISFGIF SPLTGRMKKA
     EKRAAYSARA KQDLAAWLPH AGVPAAGAPE HVDQRSA
 
 
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