MNMC_VIBVY
ID MNMC_VIBVY Reviewed; 672 AA.
AC Q7MIT5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000255|HAMAP-Rule:MF_01102};
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=2.1.1.61 {ECO:0000255|HAMAP-Rule:MF_01102};
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01102};
DE EC=1.5.-.- {ECO:0000255|HAMAP-Rule:MF_01102};
GN Name=mnmC {ECO:0000255|HAMAP-Rule:MF_01102}; OrderedLocusNames=VV2430;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
CC -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position
CC (U34) in tRNA. Catalyzes the FAD-dependent demodification of
CC cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl
CC group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC mnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569, Rhea:RHEA-
CC COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454,
CC ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01102};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01102}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000255|HAMAP-Rule:MF_01102}.
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DR EMBL; BA000037; BAC95194.1; -; Genomic_DNA.
DR RefSeq; WP_011150886.1; NC_005139.1.
DR AlphaFoldDB; Q7MIT5; -.
DR SMR; Q7MIT5; -.
DR STRING; 672.VV93_v1c21330; -.
DR PRIDE; Q7MIT5; -.
DR EnsemblBacteria; BAC95194; BAC95194; BAC95194.
DR KEGG; vvy:VV2430; -.
DR PATRIC; fig|196600.6.peg.2436; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_2_1_6; -.
DR OMA; NFLCAWQ; -.
DR OrthoDB; 912110at2; -.
DR Proteomes; UP000002675; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_01102; MnmC; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008471; MnmC-like_methylTransf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05430; Methyltransf_30; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme;
KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..672
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000095032"
FT REGION 1..243
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 269..672
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 672 AA; 74969 MW; 5B8264A8FC23556D CRC64;
MTSITHAELG WNEVGTPVSD QFDDVYFSNV NGLEETRYVF LKQNLIPERW QEFDRRRFVI
GETGFGTGLN FLAVWQAFND FRRANPDATL KELHFISFEK FPLSKQDLIK AHQAWPELAE
LAEKLHRHYP PAVPECHRIV LDNGAVTLDL WLGDIKDCLP SVPYGEEGII DTWFLDGFAP
SKNPEMWNQD LFNGMAKLAR SECRVATFTS AGFVRRGLIE AGFAMKKVKG FGTKREMIAG
CMETRQPQSR HAPYFNRTSA SHLDSIAIIG GGIASAALAK ALVQRGQKVT LYCKHAQAAE
GASGNRQGAV YPLLNGSHDG VSRVFAPAFL FTRQFVEQAA QALTFDHDWC GVTQLMWDEK
STNKLDKMLS GNFAPELIQK LSAEETAAKI GLPIDMASVH YPLGGWLCPA ELTQALFAQL
DTLDNFTAKF EQSVEQLIWD ERSQQWQVHT QGQHDTYSAV VIANGHEFQT FSQTADIPLG
QVKGQVSHAP ATETLSKLKS VLCYDGYMTP VNPNNQHLCI GASYDRRHLD TEFDVNAQQE
NAEKLTQCVP NQAWAKEVDT SGNLSRQGIR CVSRDHLPFV GNVGDFSAIK RQYADLPHTQ
AEEIEVISQF PNLFCLLGLG SRGLSSAPLM AELLASQICN DPLPLPVDVL EELHPSRMWV
RKLRKGKAIT EL