ID   MNMC_PASMU              Reviewed;         672 AA.
AC   Q9CNT7;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=PM0338;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02422.1; -; Genomic_DNA.
DR   RefSeq; WP_010906597.1; NC_002663.1.
DR   AlphaFoldDB; Q9CNT7; -.
DR   SMR; Q9CNT7; -.
DR   STRING; 747.DR93_1112; -.
DR   EnsemblBacteria; AAK02422; AAK02422; PM0338.
DR   KEGG; pmu:PM0338; -.
DR   PATRIC; fig|272843.6.peg.351; -.
DR   HOGENOM; CLU_022427_2_1_6; -.
DR   OMA; NFLCAWQ; -.
DR   Proteomes; UP000000809; 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; 3.40.50.150; -; 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_0000095019"
FT   REGION          1..241
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;  75945 MW;  C92927D963ED4D21 CRC64;
     MHKVQFADVH FNAENTPVSA QFDDVYFSNQ DGLAESHYIF QEGNQLWQRW QQTSEAHFVI
     AETGFGTGLN FFAVTQRFRE FRLTYPDAPL KRLFFISFEK YPLPLAQLKR AHQAYPEFQS
     LAQQLQQSWL EPIVGCYRFH FAETTLDLWF GDMAENLPQL GDYMCNKIDA WFLDGFAPSK
     NPQMWQDTLY QHMYRYTKTQ GTFSTFTAAS AVRKGLIHAG FTVTKRKGYG KKRECLQGVK
     AQQQPADIHA PWALVQPAEL TENADIALIG GGIASVFSAL SLLERGAKVT VYCEDNSLAA
     NASGNKQGAF YPQLSDDDLR YIRFYIHAFA YGKQRFNWAI EQGITFEHDF CGVALCAYDA
     KSAVKLAKIS ALQLPPSLYQ PLSQQALSEQ VGLPLPCDGG FIAQGAWLSP QQFVQNTFDF
     LATRGVIIKT QQKITALERQ TTHWLLTTEQ GDSFKHQVVV LANGHKLTQF RQTEHLPVYP
     VRGQVSEIAT STELSKLKAV ICYDGYLTPK AASQTHCLGA SHLRDNAERA FSLQEQQENQ
     QKIQTNLASV DWVNEVDTRN NQARIGIRCS VRDRIPMLGN VPDFEQQLSD YHNLYNLRRR
     KHAIKHAALH PNLFLIGALG SRGLTSAPLL AETLASLIYH EPLPLSEDIL HQLNANRSWI
     RKLLKGSQVK QG