ID   MNMC_VEREI              Reviewed;         623 AA.
AC   A1WH84;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC;
DE            Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein;
DE   Includes:
DE     RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase;
DE              EC=2.1.1.61;
DE   Includes:
DE     RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase;
DE              EC=1.5.-.-;
GN   Name=mnmC; OrderedLocusNames=Veis_1221;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC       superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC       {ECO:0000305}.
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DR   EMBL; CP000542; ABM56991.1; -; Genomic_DNA.
DR   RefSeq; WP_011809002.1; NC_008786.1.
DR   AlphaFoldDB; A1WH84; -.
DR   SMR; A1WH84; -.
DR   STRING; 391735.Veis_1221; -.
DR   EnsemblBacteria; ABM56991; ABM56991; Veis_1221.
DR   KEGG; vei:Veis_1221; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG4121; Bacteria.
DR   HOGENOM; CLU_022427_1_0_4; -.
DR   OMA; NFLCAWQ; -.
DR   OrthoDB; 912110at2; -.
DR   Proteomes; UP000000374; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 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..623
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000348045"
FT   REGION          1..209
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          232..623
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   623 AA;  66034 MW;  E52428DFC9A687C6 CRC64;
     MTQRGEVPDF LHGCGLPAAW AGLPQWRILE TGFGFGLNFL ATWAAWRADP HRPVLLHFVA
     TEAQPVSAAD LLRAGSARPG LAPLAQELSR QWWGLLPGLH RLRFDDGHVL LTLCLGDWQA
     QLRQQRQQLT VDSVYLHDLP QDWRPQRHPA PAGLPGLPGL KAVAACCRRG TRLASRCSTV
     RDALVQCGFT LHPAPGSDAQ RDMLHAVYQP HWQPRTMRPA AAPATPGECM VIGGGIAGAA
     TAASLARRGW QLRVLDQAAA PAAGASGLPA GIFAPHVSAD DNLLSRLSRS GVRSTLEQAR
     WRLREGLDWS HCGVLEHRAD ASPGLPARWS DGPGADGRQS AAHAALGALA QSGLPANASV
     CWHPQAGWIR PARLVAALLA QPGIRWQGAC RVARLRRVQA PGAGPTAWQA LDAQGRVLAQ
     APTVVIAAGA GSLELLEHRW PLQPVRGQVS WGLHGDPAAP LLPFPVNGHG HLVPRFPLGD
     DAQGPCAWVM GATFERGVEQ MPPAPADVQA AHASHWARLQ TLLPRMAPPL ESAFAAARAD
     AGLAASARAA QSWAAVRCTA PDRLPIVGPV DAAALPGLWV CSAMGARGLT LALLCGELLA
     ARLQGEPLPI EHRLAKALDS GRM