ID   MNMC_SHELP              Reviewed;         686 AA.
AC   A3QFM9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Shew_2411;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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. {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; CP000606; ABO24277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3QFM9; -.
DR   SMR; A3QFM9; -.
DR   STRING; 323850.Shew_2411; -.
DR   EnsemblBacteria; ABO24277; ABO24277; Shew_2411.
DR   KEGG; slo:Shew_2411; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_022427_2_1_6; -.
DR   OMA; MGCAPDF; -.
DR   Proteomes; UP000001558; 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: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; 3.50.50.60; -; 1.
DR   HAMAP; MF_01102; MnmC; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR   InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR   Pfam; PF01266; DAO; 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..686
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000348029"
FT   REGION          1..258
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          276..686
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   686 AA;  75269 MW;  8CF2E7CAAADA46DB CRC64;
     MPNIPLRVNS LATEHPNNAQ NSDKMPTFDA IFSHLSAIAS HNSHQIIALL PSSDANWPAA
     LIAERLTQAG SKQHLQKQHL HLHLFAQHQA SWLKALAESE TLASPAKEQI KAICDARVSG
     SHRLKLVNAR LIIDIHLGDP LTQLKDLVSP SLASQAIQGW LANTQATDEA LIWQMARLSQ
     DNAEFLLLEN NDVNLDKTSN NANTNLLTQL IIKAGFTCYR LNLSLKDDQL VTLAEKPSLA
     SLEIAMVERR ALRRQQLDKF AFNPLTQGRE GETAIIGGGV ASANLALSLA ERGKKVSFFC
     MDKAPGEQAS GNKQGAIYPL LTPEHGSLSH YFLLGYLFSR QRIKQLLESG HEIPHDFCGV
     LQTGHDERSH KRLTKIINAQ PWAESIARPV DALQATALAG VTIEHQGIYY PLAGWVSPQA
     FTRAAISQAE RLGKQTSHYQ CQITAIRFEN QQWYLSAIQD GQKVEFGPYA NLVLANGRHL
     TDFAQTDHLP ISGFRGQVSH IPERAPLKDL KTVLCAHGYL TPAHDKLHCT GASYVKDASN
     LDYSAVEQVE NLDKIRTSYG GEWTKAVDIT GHSARVGVRM VTRDHAPMMG CAPDFEAISA
     TYISHQQTKK STKESAKCWQ TTSAPVHQGL FILGGLGSRG LTSGPLAAEI LAAQLCGELL
     PATQDILALL NPNRMWMRKL IKGKAL