MNMC_ECO57
ID MNMC_ECO57 Reviewed; 668 AA.
AC Q8XCQ7;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=Z3587, ECs3208;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-247.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of the N-terminal domain of UPF0209 protein yfcK from
RT Escherichia coli O157:H7.";
RL Submitted (AUG-2007) to the PDB data bank.
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=AAG57453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB36631.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57453.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36631.1; ALT_INIT; Genomic_DNA.
DR PIR; A85874; A85874.
DR PIR; H91029; H91029.
DR RefSeq; NP_311235.2; NC_002695.1.
DR RefSeq; WP_000683769.1; NZ_SDVX01000004.1.
DR PDB; 2QY6; X-ray; 2.00 A; A/B=2-247.
DR PDBsum; 2QY6; -.
DR AlphaFoldDB; Q8XCQ7; -.
DR SMR; Q8XCQ7; -.
DR STRING; 155864.EDL933_3491; -.
DR DNASU; 913957; -.
DR EnsemblBacteria; AAG57453; AAG57453; Z3587.
DR EnsemblBacteria; BAB36631; BAB36631; ECs_3208.
DR GeneID; 913957; -.
DR KEGG; ece:Z3587; -.
DR KEGG; ecs:ECs_3208; -.
DR PATRIC; fig|386585.9.peg.3349; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_1_0_6; -.
DR OMA; NFLCAWQ; -.
DR EvolutionaryTrace; Q8XCQ7; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome;
KW 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_0000095014"
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"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2QY6"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2QY6"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2QY6"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:2QY6"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2QY6"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:2QY6"
SQ SEQUENCE 668 AA; 74468 MW; 698D0E08AD0908BF CRC64;
MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNQLEA RFPEHPHPLF
VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF EKFPLTRADL ALAHQHWPEL
APWAEQLQAQ WPMPLPGCHR LLLDEGRVTL DLWFGDINEL ISQLDDSLNQ KVDAWFLDGF
APAKNPDMWT QNLFNAMARL ARPGGTLATF TSAGFVRRGL QEAGFTMQKR KGFGRKREML
CGVMEQTLPL PCSTPWFNRT GSSKREVAII GGGIASALLS LALLRRGWQV TLYCADEAPA
LGASGNRQGA LYPLLSKHDE ALNRFFSNGF TFARRLYDSL PVKFDHDWCG VTQLGWDEKS
QHKIAQMLSM DLPEELAVAV EANAVEQITG VTTNCSGITY PQGGWLCPAE LTRNVLELAQ
QQGLQIYYQY QLQDLSRKDD CWLLTFAGDQ QATHSVVVLA NGHQISRFSQ TSSLPVYSVA
GQVSHIPTTP ELAKLKQVLC YDGYLTPQNP ANQHHCIGAS YHRGSEETAY SEDNQQQNRQ
RLIDCFPHAQ WAKTVDVSKK EARCGVRCAT RDHLPMVGNV PDYEATLVEY ASLAEQKDKA
VSAPVFDDLF MFAALGSRGL CSAPLCAEIL AAQMSDEPIP MDASTLAALN PNRLWVRKLL
KGKAVKAG
