ID   MNMC_VIBCH              Reviewed;         674 AA.
AC   Q9KQ91; O87021;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=VC_2110;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-320.
RC   STRAIN=Classical Inaba Z17561 / Serotype O1;
RA   Fallarino A.;
RL   Submitted (JUL-1998) 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; AE003852; AAF95255.1; -; Genomic_DNA.
DR   EMBL; AJ231075; CAA13117.1; -; Genomic_DNA.
DR   PIR; D82118; D82118.
DR   RefSeq; NP_231741.1; NC_002505.1.
DR   AlphaFoldDB; Q9KQ91; -.
DR   SMR; Q9KQ91; -.
DR   STRING; 243277.VC_2110; -.
DR   PRIDE; Q9KQ91; -.
DR   DNASU; 2613366; -.
DR   EnsemblBacteria; AAF95255; AAF95255; VC_2110.
DR   KEGG; vch:VC_2110; -.
DR   PATRIC; fig|243277.26.peg.2017; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG4121; Bacteria.
DR   HOGENOM; CLU_022427_2_1_6; -.
DR   OMA; NFLCAWQ; -.
DR   BioCyc; VCHO:VC2110-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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..674
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000095029"
FT   REGION          1..246
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          272..674
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
FT   CONFLICT        145
FT                   /note="N -> D (in Ref. 2; CAA13117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..149
FT                   /note="LV -> FI (in Ref. 2; CAA13117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="L -> F (in Ref. 2; CAA13117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="A -> V (in Ref. 2; CAA13117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="N -> G (in Ref. 2; CAA13117)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   674 AA;  74791 MW;  F0691F4091C9C927 CRC64;
     MFIMSSISHA QLGWNDAGTP VSDQFDDVYF SNVNGLAETR YVFLEQNHLP QRWHNDDQRR
     FVIAETGFGT GLNFLAVWQA FVAFREANPD AKLKELHFIS FEKYPLSKSD LIQAHQAWPE
     LAQFAQKLHK HYPLAIPECQ RIVLNDGLVT LDLWFGDIKD CLPKVATQEQ GLVDAWFLDG
     FAPSKNPEMW NQNLFAGMAK LAKHGCTCAT FTSAGFVRRG LIDAGFAMKK VKGFGTKREM
     IAGSLSEKVP YTNIAPEFRF EATHGLQEVA IIGGGIASAT LATTLARRGV AVTLYCADEK
     PAQGASGNRQ GAVYPLLSGD HNAVSRVFAP AFLFARQWIE QAAEQINFDH DWCGVTQLMW
     DEKATDKLKS MLEGNFPTQL VHGLSAEQTN QQVGVPVDKA SVHYPLGGWL SPAELTQGLI
     HLLEQQGKLT AHYQTPIDAL TWQPETQLWQ LRSGDTLMSH QCVVIASGHQ FDSLSQTAEL
     PLGKVKGQVS HIPTTETLSK INSVLCYDGY MTPVSQQNGY HCIGASYDRQ HLDATFDPQA
     QHENAQKLIH CLPEQTWPLE VDVSGNQSRQ GVRCVSRDHL PFVGNVGEFS KITEQYRDLA
     QQHQAEPIAL YPQLYALVGL GSRGLSSAPL MAELLASQMC GDPMPLGVDL LEQLHPSRMW
     VRKLRKGKAL TQKV