ID   MNMC_LEGPC              Reviewed;         666 AA.
AC   A5IC27;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=LPC_0953;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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; CP000675; ABQ54927.1; -; Genomic_DNA.
DR   RefSeq; WP_011946533.1; NC_009494.2.
DR   AlphaFoldDB; A5IC27; -.
DR   SMR; A5IC27; -.
DR   KEGG; lpc:LPC_0953; -.
DR   HOGENOM; CLU_022427_1_0_6; -.
DR   OMA; NFLCAWQ; -.
DR   BioCyc; LPNE400673:LPC_RS08005-MON; -.
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..666
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000347990"
FT   REGION          1..253
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          283..666
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   666 AA;  74957 MW;  7391B92C15C8589E CRC64;
     MSSPFAPIIT ADIDWRDDLP YSLQFDDIYY SAEGGINQSL YVFVEGNNLI NRWQQLPTNE
     SNVFTIAETG FGTGMNFLLT WKLWEKFAPQ NARLHYISCD KHPLKKNDLI KCLQKWPELS
     VQAEKLIEHY PVLTPGYHHL AFSNNQITLT LMLGDVLECY EQLLFCGDIN LEQQLRESYV
     NAWYLDGFSP SKNQSMWSDN LLTVIAMLSK EGTTVATYSA SSIVKTALTN AGFVIEKRKG
     FGPKRHMLCA YYEKAYSSSK KNRHTPWHIN YPVTKDERTA LIVGGGLAGC FIANSLAKRG
     WEVTILEEKE KVGCGGSANQ QAVLFPKLST YKSPFTQFML YSFLYANDVY KELLKHYDLG
     ELKGSLLLAH NEREKANQQS LIHWLELYPE LGQLVDEKQS SELSGISLPC GGLFIPSSGW
     INSPELCDIL IDNKRISLIT GNRVQSINYN QKNWVVNDIE ASVLILANGQ QVNYFHETNH
     LPVKAIRGQI TTIQSTQEST KLKIPLCAEG HVLPALNNSH RVGASYDIGT SEPELNALDD
     QLNLDRLKRI APDIMWSQNV LDHWAGIRAA SPDYLPIVGP LPNALEFKEV YSELKSNSKR
     WIAEAAPCYP NLYVCAAFGS RGLTTIPLAT EWLAGLINKE ISILPRKLIQ AISPARFLRK
     KIIQGP