ID   MNMC_SHEHH              Reviewed;         636 AA.
AC   B0TL07;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Shal_2655;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ77209.1; -; Genomic_DNA.
DR   RefSeq; WP_012277737.1; NC_010334.1.
DR   AlphaFoldDB; B0TL07; -.
DR   SMR; B0TL07; -.
DR   STRING; 458817.Shal_2655; -.
DR   EnsemblBacteria; ABZ77209; ABZ77209; Shal_2655.
DR   KEGG; shl:Shal_2655; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_022427_2_1_6; -.
DR   OMA; NFLCAWQ; -.
DR   OrthoDB; 912110at2; -.
DR   Proteomes; UP000001317; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..636
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000348028"
FT   REGION          1..202
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          227..636
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   636 AA;  69857 MW;  39073EF072D155D4 CRC64;
     MTVSKILKQV INRKTTRQIV IAQLGLGSLA SLKQLIIEQL QLISDHRVTL KIFSQIEPNL
     HTFISDTELA ELFSSKPNTS LSLAAIEGCQ RIIVNDGKLK IDFHLGSYAQ QLQQLPIVSS
     GFIDGWNMAD NLAQEQLDSA LFWQMAKLAH NDCLFCLEPT LTPEAQQQSL LLAEQVGLYS
     ELPLKNDDTL FQERAALRAQ SHQQQAPFPI CPAALTPVEN DIGIAIIGGG VASACLALSL
     AERDQRVTLF CEDDALAQAA SGNKQGAIYP LLTPDNNTLS QYFQQAYLFS LQRLKTLAAR
     GHKIDFDLCG VVHTGHDERS RKRVAKITHG HNWEPNIALA IAAEQASNIA GVKLDDGGLF
     YPQGGWVSPQ DFTRAAFNQA QAISDASLKL NTQITGIHSK DNVWYLSSKT ERFGPFKALI
     VANGKSITQY PQTQYLQATG FRGQVSHVPS RAKLSKLSAV LCAHGYMTPS NNDLHCLGAS
     YVKNAADTRY SPSEQVENLH KIQHSYIGQD WIEDIDVSGH SARVDVRMVT RDHAPMMGPV
     PNLDAILALY QQHQLTPESR QFWQTHAAPT HKNLYVLGGL GSRGLCSGPL AAEALAAQIC
     GEPMPISLDF VSLLNPNRMW MRKLLKGKAL EMSGKS