MNMC_HAEIN
ID MNMC_HAEIN Reviewed; 670 AA.
AC P44246; P44245;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=HI_1534/HI_1535;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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=AAC23184.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC Sequence=AAC23185.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23184.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L42023; AAC23185.1; ALT_FRAME; Genomic_DNA.
DR PIR; C64035; C64035.
DR PIR; D64035; D64035.
DR AlphaFoldDB; P44246; -.
DR SMR; P44246; -.
DR STRING; 71421.HI_1535; -.
DR DNASU; 950397; -.
DR EnsemblBacteria; AAC23184; AAC23184; HI_1534.
DR EnsemblBacteria; AAC23185; AAC23185; HI_1535.
DR KEGG; hin:HI_1534; -.
DR KEGG; hin:HI_1535; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_061971_2_1_6; -.
DR PhylomeDB; P44246; -.
DR Proteomes; UP000000579; 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..670
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_0000095017"
FT REGION 1..242
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 269..670
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 670 AA; 75691 MW; EB68D7BCA874B429 CRC64;
MTFSVQHAEI HFNQNHIPVS DQFDDVYFSN ENGLAETDYV FLQGNQLWER WITHKDANFV
IAETGFGTGL NFFAVTKLFR EFRQQHENHP LKRLNFISFE KYPLKITALL QAHLACPQFE
DLSAHLQRYW PSLILGCHRI HFGETTLDLW FGDVSENLPQ LGDYMNERIN AWFLDGFAPS
KNPEMWNDDL YNLMFRFTKP NGTFATFTAA SAVRKGLESA GFNVTKRKGF GKKRECLSGL
KIQSKSTALS TPWYLAQPAK MEKQDVAIIG GGIASLCAAI SLIKRGAKVT IYCEDDALAL
NASGNKQGAF YPQLSDDNAL TVDFYLHAFS YGRQLLDWAI EQNIVFEHEF CGVALCAYNE
KSAVKLTKIS QLGLPNEIFQ MLSAEQLSEK VGLPLNCEGG WIEQGAWLAP RQFVQNAFSF
LEKQGVVIKT AQKITALSQL EKGWELKNMQ GQKYCHEVVI LANGHKITDF VQTEKLPLYP
IRGQVSQIPT SENLLKLKSV LCYDGYLTPA NQLKTSHCIG ASMFRDNVDR DFSEQEQQEN
QQKLQQNIAQ PWTQDVDTSD NLARVGIRCS VRDLAPMVGN VPHFEQQQAD YYNLFNLRRR
KQPIQSAANF QNLFLIAALG SRGLTSAPLL GETLASIIYG EPLPISEGIL HNLSANRAWV
KKWLKGSKVE
