ID   MNMC_ALBFT              Reviewed;         609 AA.
AC   Q21WM8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Rfer_2101;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-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; CP000267; ABD69825.1; -; Genomic_DNA.
DR   RefSeq; WP_011464393.1; NC_007908.1.
DR   AlphaFoldDB; Q21WM8; -.
DR   SMR; Q21WM8; -.
DR   STRING; 338969.Rfer_2101; -.
DR   PRIDE; Q21WM8; -.
DR   EnsemblBacteria; ABD69825; ABD69825; Rfer_2101.
DR   KEGG; rfr:Rfer_2101; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG4121; Bacteria.
DR   HOGENOM; CLU_022427_1_0_4; -.
DR   OMA; NFLCAWQ; -.
DR   OrthoDB; 912110at2; -.
DR   Proteomes; UP000008332; 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; -; 2.
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   Pfam; PF01266; DAO; 2.
DR   Pfam; PF05430; Methyltransf_30; 1.
DR   SUPFAM; SSF51905; SSF51905; 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..609
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000348019"
FT   REGION          1..229
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          237..609
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   609 AA;  65624 MW;  9CBD920B41E74D0B CRC64;
     MVELAAATCL HECGLPQAWC KQEAWRILET RFGQGLHFLT TWQAWRNDPQ RPRMLHYVAV
     TAAPPDIDEL LAGMASSPEL LLLAKELAPQ CLGLSTGFQR LTFDGGHVLL TLCVGDLTAM
     LRAQQFAADS IYLTPDPTDC PDRCAASNWR VWTAKALARC CRRGTTLVAP VDADHLYADL
     TQCGFELSTI QAGQPTGPEA APTNISLRAQ FNPRWTIKNT RNTLPARAMA VSSCAVIGAG
     LAGASVAASL ARRGWQVQVL DQAHTPAAGA SGLPVGLVVP HVSADDCVLS RLSRSGVRLM
     LQQARSLLRQ GQDWDATGVL ERRLDGPPGV PDIWHPQAAW LKPTQLVRAW LAQLGITFQG
     DAKVAALRQR GDEWELLDTD GGMLHRASRV VFANAGGAMA LLDTLQARLP ALNIRVNQFP
     VMQGVRGQVS WAMHTGLPDE TFPPFPINGA GSIVPWVPVD EDCGQNLAWF VGASYQPDSQ
     PPAPDEKNHA TNLARLHKLS PKLGQALAGK FAAGAVNAWK NTRCVTADRL PAVGPLDQVD
     HPGLWMCAGM GSRGLSFSML CAELLAARWS GEPLPIDAGL ARTLEARRGA DCHRNRLDRS
     PELPVSCAP