MNMC_CROS8
ID MNMC_CROS8 Reviewed; 670 AA.
AC A7MH59;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 74.
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=ESA_00892;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABU76162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000783; ABU76162.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041460426.1; NC_009778.1.
DR AlphaFoldDB; A7MH59; -.
DR SMR; A7MH59; -.
DR EnsemblBacteria; ABU76162; ABU76162; ESA_00892.
DR KEGG; esa:ESA_00892; -.
DR PATRIC; fig|290339.8.peg.791; -.
DR HOGENOM; CLU_022427_1_0_6; -.
DR OrthoDB; 912110at2; -.
DR Proteomes; UP000000260; 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 SUPFAM; SSF53335; SSF53335; 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..670
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000347981"
FT REGION 1..245
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 271..670
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 670 AA; 72979 MW; AA51BBE6F18A2FB1 CRC64;
MKPIAIQPAS LTFNNEGTPV SRDFDDVYFS NDDGLEETRY VFLDGNQLPE RFMTHPRDSF
IVAESGFGTG LNFLTLWQAF AAFRDAHPDA TLQRLHFISF EKFPLTPADL KSAHAHWPEL
APWAQQLQAQ WPMALPGCQR LVLDGGRVTL DLWLGDINEL VDTLDDTHNR QVDAWFLDGF
APSKNPEMWT PGLFTAMARL ARPGGTLATF TSAGFVRRGL IEAGFDVVKR KGFGRKREML
TGALSHDAPP PARAPWYARR PASGDKDVAV VGGGIASALL ALGLLRRGWQ VTLYCEDDAP
AQGASGNRQG ALYPLLSHHD AALAAFFPAA FTFARRLYDA LPVSFDKDWC GVTQLGWDEK
SQTKINQMLD LALPDTLAHG VDAREVRERC GVKTGCGGIE YPQGGWLCPA QLTAGVLELA
QAHGLRVHYG HRVSALHRED LDWQLDFANG AQARHAAVVL ANGHQLSGFP QTEKLPVYPV
GGQVSHIPTT PGLGALRQVL CYDGYLTPQN PANAMHCIGA SYHRGVSEMR YQEEDQQRNR
QRLIDCLPAA SWAQEVDVSA GDARCGVRCA TRDHLPMVGN APDYAATLRD YATLSQDASA
PETVMPAPVL KNLFVLGALG SRGLCSAPLA AEILASQMSG EPLPLDGATL AALNPNRLWV
RKLLKGRAAS
