ID   MNMC_CAMHC              Reviewed;         667 AA.
AC   A7I2T7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CHAB381_1277;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) 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; CP000776; ABS51710.1; -; Genomic_DNA.
DR   RefSeq; WP_012109129.1; NC_009714.1.
DR   AlphaFoldDB; A7I2T7; -.
DR   SMR; A7I2T7; -.
DR   STRING; 360107.CHAB381_1277; -.
DR   EnsemblBacteria; ABS51710; ABS51710; CHAB381_1277.
DR   KEGG; cha:CHAB381_1277; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG4121; Bacteria.
DR   HOGENOM; CLU_022427_2_1_7; -.
DR   OMA; NFLCAWQ; -.
DR   OrthoDB; 912110at2; -.
DR   Proteomes; UP000002407; 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; -; 2.
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   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 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..667
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000347969"
FT   REGION          1..215
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          240..667
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   667 AA;  75913 MW;  AF1AF30AFBFECC3C CRC64;
     MKFINGILFN ENFKDFYSNF KNPFGESEFV FGSAVNEILK TQNRVIVAEL GFGLGRNFLN
     IAAKFKNSDK ILHFVSIEKF PLQKEILAKF YENFKFEGAK KLLKLYPTLE SGFHRIKFSK
     NITLDLLFGD AECVLKECEF KADIWLMDGF SPSKNPDMWS DEITSQIARL CRIKAKIATY
     SASKKVQKSL ENAGFCVVKT PGFNGKREMI RAYFNGNSGE IKDYFFERPS FKSGKNVLII
     GAGIAGIVTA IKFQNLGYKT VIAEKACSVA ANASGNFCGV LEPLITKKGV KLGEMHKYAF
     KMAVKFYKKN VPKNLAKFCG AKEFAYNDDI LKRFETHDKS EIFDFNRKDL PYASIFIKNA
     ALLRPRKICE FFSKKLNIKF GYEFSDFVES NGGYIVNFVG KKPLKCDILI FAMGSESEEL
     FGGGKNVRAN FDDAMQISSV RGQITLLRPF LKTPIPLGAR GYICPKIGKR QLIGATYDRK
     DYENQARTFD DERNLQNVAE LLNKNFVKNT DTRNLNDKKF KFEILDKNVD FNVSKQNLNF
     KMHTQNKELA FKNQILNVKI LGSRVGFRGY SGDRFPLIGA LPDCEYFKEK YKILPWQKNR
     AKNLPPKYLK NIYINTSHGA RGLCTAILGA EILADLVTNR PFCLPKSLIN ELAPSRFLIR
     KLKKGLK