MNMC_ECOK1
ID MNMC_ECOK1 Reviewed; 668 AA.
AC A1ADH3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-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}; OrderedLocusNames=Ecok1_22190;
GN ORFNames=APECO1_4240;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01713.1; -; Genomic_DNA.
DR RefSeq; WP_000683753.1; NC_008563.1.
DR AlphaFoldDB; A1ADH3; -.
DR SMR; A1ADH3; -.
DR EnsemblBacteria; ABJ01713; ABJ01713; APECO1_4240.
DR KEGG; ecv:APECO1_4240; -.
DR HOGENOM; CLU_022427_1_0_6; -.
DR OMA; NFLCAWQ; -.
DR Proteomes; UP000008216; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..668
FT /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT bifunctional protein MnmC"
FT /id="PRO_1000064994"
FT REGION 1..245
FT /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT REGION 270..668
FT /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ SEQUENCE 668 AA; 74368 MW; 774729A085048EE4 CRC64;
MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNHLEA RFPEHPHPLF
VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF EKFPLTRADL ALAHQHWPEL
APWAEQLQAQ WPLPLPGCHR LLLDEGRITL DLWFGDINEL TSQLDDSLNQ KVDAWFLDGF
APAKNPDMWT QNLFNAMARL ARPGSTLATF TSAGFVRRGL QEAGFTMQKR KGFGRKREML
CGVMEQTLPL PCSTPWFNRT GSNKQEAAII GGGIASALLS LALLRRGWQV TLYCADEAPA
LGASGNRQGA LYPLLSKHDE ALNRFFSNAF TFARRFYDLL PVKFDHDWCG VTQLGWDEKS
QHKIAQMLSM DLPAELAVAV EANAVEQITG VATNCSGITY PQGGWLCPAE LTRNVLKLAQ
QQGLQIHYQY QLQDLSRKDD GWLLNFAGDQ QATHSVVVLA NGHQISRFSQ TSSLPVYSVA
GQVSHIPTTP ELAELKQVLC YDGYLTPQNT ANQHHCIGAS YHRGSEETAY SDEDQQQNRQ
RLIDCFPHAQ WAKEVDVSGK EARCGVRCAT RDHLPMVGNV PDYDATLVEY ASLAEKKDEA
VSAPVYDDLF MFAALGSRGL CSAPLCAEIL AAQMSEEPIP MDASTLAALN PNRLWVRKLL
KGKAVKAG
