MNMC_VIBC3
ID MNMC_VIBC3 Reviewed; 674 AA.
AC A5F6E9; C3M2U2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
GN OrderedLocusNames=VC0395_A1694, VC395_2224;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ21228.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10216.1; -; Genomic_DNA.
DR AlphaFoldDB; A5F6E9; -.
DR SMR; A5F6E9; -.
DR STRING; 345073.VC395_2224; -.
DR EnsemblBacteria; ABQ21228; ABQ21228; VC0395_A1694.
DR KEGG; vco:VC0395_A1694; -.
DR KEGG; vcr:VC395_2224; -.
DR PATRIC; fig|345073.21.peg.2149; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_2_1_6; -.
DR OMA; NFLCAWQ; -.
DR Proteomes; UP000000249; Chromosome 2.
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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..674
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_1000073028"
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"
SQ SEQUENCE 674 AA; 74766 MW; 92BF9B56DD69611E CRC64;
MFIMSSISHA QLGWNDAGTP VSDQFDDVYF SNVNGLAETR YVFLEQNHLP QRWHNDDQRR
FVIAETGFGT GLNFLAVWQA FVAFREANPD AKLKELHFIS FEKYPLSKSD LIQAHQAWPE
LAQFAQKLHK HYPLAIPECQ RIVLDDGLIT LDLWFGDIKD CLPKVATQEQ GLVDAWFLDG
FAPSKNPEMW NQGLFAGMAK LAKHGCTCAT FTSAGFVRRG LIDAGFAMKK VKGFGTKREM
IAGSLSEKVP YTNIAPEFRF EATHGLQEVA IIGGGIASAT LATTLARRGV AVTLYCADEK
PAQGASGNRQ GAVYPLLSGD HNAVSRVFAP AFLFARQWIE QAAEQINFDH DWCGVTQLMW
DEKATDKLKS MLEGDFPTQL VRGLSAEQTN QQVGVPVDKA SVHYPLGGWL CPAELTQGLI
HLLAQQGKLT AHYQTPIDEL TWQPETQLWQ LRSGDTLMSH QCVVIASGHQ FDSLSQTAEL
PLGKVKGQVS HIPTTETLSK INSVLCYDGY MTPVSQQNGY HCIGASYDRQ HLDATFDPQA
QRENAQKLIH CLPEQTWPLE VDVGGNQSRQ GVRCVSRDHL PFVGNVGEFS KITEQYRDLA
QQQEAEPIAL YPQLYALVGL GSRGLSSAPL MAELLASQMC GDPMPLGVDL LEQLHPSRMW
VRKLRKGKAL TQKV
