MNMC_HAEDU
ID MNMC_HAEDU Reviewed; 667 AA.
AC Q7VM59;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=HD_1141;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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; AE017143; AAP96002.1; -; Genomic_DNA.
DR RefSeq; WP_010945051.1; NC_002940.2.
DR AlphaFoldDB; Q7VM59; -.
DR SMR; Q7VM59; -.
DR STRING; 233412.HD_1141; -.
DR EnsemblBacteria; AAP96002; AAP96002; HD_1141.
DR KEGG; hdu:HD_1141; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_2_1_6; -.
DR OMA; NFLCAWQ; -.
DR Proteomes; UP000001022; 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; -; 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..667
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000095016"
FT REGION 1..241
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 268..667
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 667 AA; 75805 MW; 3851745E43E57FF0 CRC64;
MHKLTFAQLS FNSDNTPVSE QFDDIYFSTE DGVQESYYVF QDGNQLWQKW QNHHRSAFVI
AETGFGTGLN FLAVAEKFQQ FRSTFPDSPL KRLYFISFEK YPLTQQQLAD IHQHYPQFTQ
LSATLIACWQ PRQAGCQRYH FDDVYLDIWF GEMLENLPQL GDLYNATVDS WFLDGFSPDK
NPTMWHEQLY QHMFRLTRVG GSFATFTAAS HVRCGLQAVG FTVYKRKGFA KKREMLCGEK
AQKSQTAEVN FPYFYSPPAI VNDDIAIVGG GIASLFVALS LLERGKQVTL YCQDSQVAQK
ASGNAQGAIY PQLSDDDPRN VRFYVHCFDY ALQRLKQFEK LVPFEHALTG VVLSAYNEKT
AQKLQKIARQ TQNQDLFKWC QAEELTEYLG VAIANEGAFI PQAGWLSPVQ FVQQAFAYLQ
TKGLKIVLNH TVTDPQFVEG KWQWQYQGVQ FAHHILVLAN GHSFTQFSQA EGIPLYPVRG
QVSQIPTTPA LQKLKCVICY DGYLTPMATN GYHCIGASHV RDNTDMAFSA IEHQQNLAKL
QQNIGAYHWT QGIDLSANLA KQGIRSALRD RVPMVGPIPH FAVQKQQYSN IYNLLRRKKA
VENAVNFPHL YMVNGLASRG LTTAPLLGEM LASLIVNEPI PISQDIWHAL LPNRTWLRKW
LKGSKVV