MNMC_ECOLI
ID MNMC_ECOLI Reviewed; 668 AA.
AC P77182;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC;
DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein;
DE Includes:
DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase;
DE EC=2.1.1.61;
DE Includes:
DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase;
DE EC=1.5.-.-;
GN Name=mnmC; Synonyms=yfcK; OrderedLocusNames=b2324, JW5380;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN MNM(5)S(2)U34 BIOSYNTHESIS, AND COFACTOR.
RX PubMed=15247431; DOI=10.1261/rna.7470904;
RA Bujnicki J.M., Oudjama Y., Roovers M., Owczarek S., Caillet J.,
RA Droogmans L.;
RT "Identification of a bifunctional enzyme MnmC involved in the biosynthesis
RT of a hypermodified uridine in the wobble position of tRNA.";
RL RNA 10:1236-1242(2004).
RN [5]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF GLU-64; ASP-178; PHE-180; GLY-271;
RP ARG-567 AND ARG-618.
RX PubMed=18186482; DOI=10.1002/prot.21918;
RA Roovers M., Oudjama Y., Kaminska K.H., Purta E., Caillet J., Droogmans L.,
RA Bujnicki J.M.;
RT "Sequence-structure-function analysis of the bifunctional enzyme MnmC that
RT catalyses the last two steps in the biosynthesis of hypermodified
RT nucleoside mnm5s2U in tRNA.";
RL Proteins 71:2076-2085(2008).
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:0000269|PubMed:15247431,
CC ECO:0000269|PubMed:18186482}.
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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15247431, ECO:0000269|PubMed:18186482};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC75384.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16181.2; -; Genomic_DNA.
DR PIR; B65005; B65005.
DR RefSeq; NP_416827.4; NC_000913.3.
DR RefSeq; WP_000683799.1; NZ_LN832404.1.
DR PDB; 3AWI; X-ray; 3.00 A; A/B/C/D/E/F=1-668.
DR PDBsum; 3AWI; -.
DR AlphaFoldDB; P77182; -.
DR SMR; P77182; -.
DR BioGRID; 4261069; 20.
DR DIP; DIP-28058N; -.
DR IntAct; P77182; 1.
DR STRING; 511145.b2324; -.
DR jPOST; P77182; -.
DR PaxDb; P77182; -.
DR PRIDE; P77182; -.
DR EnsemblBacteria; AAC75384; AAC75384; b2324.
DR EnsemblBacteria; BAA16181; BAA16181; BAA16181.
DR GeneID; 66673793; -.
DR GeneID; 946800; -.
DR KEGG; ecj:JW5380; -.
DR KEGG; eco:b2324; -.
DR PATRIC; fig|511145.12.peg.2420; -.
DR EchoBASE; EB3867; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG4121; Bacteria.
DR HOGENOM; CLU_022427_1_0_6; -.
DR InParanoid; P77182; -.
DR OMA; NFLCAWQ; -.
DR PhylomeDB; P77182; -.
DR BioCyc; EcoCyc:G7199-MON; -.
DR BioCyc; MetaCyc:G7199-MON; -.
DR BRENDA; 2.1.1.229; 2026.
DR PRO; PR:P77182; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; IDA:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; IMP:EcoCyc.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:EcoCyc.
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 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_0000095012"
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 MUTAGEN 64
FT /note="E->A: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:18186482"
FT MUTAGEN 178
FT /note="D->A: Strong decrease in methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:18186482"
FT MUTAGEN 180
FT /note="F->A: Strong decrease in methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:18186482"
FT MUTAGEN 271
FT /note="G->Q: 4-fold decrease in activity, but no change in
FT FAD binding."
FT /evidence="ECO:0000269|PubMed:18186482"
FT MUTAGEN 567
FT /note="R->A: Loss of activity, but no change in FAD
FT binding."
FT /evidence="ECO:0000269|PubMed:18186482"
FT MUTAGEN 618
FT /note="R->A: Loss of activity, but no change in FAD
FT binding."
FT /evidence="ECO:0000269|PubMed:18186482"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 289..300
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 320..339
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 408..421
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 469..473
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 477..487
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 497..505
FT /evidence="ECO:0007829|PDB:3AWI"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 583..588
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:3AWI"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 619..634
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:3AWI"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:3AWI"
SQ SEQUENCE 668 AA; 74434 MW; DD246362C5B6971B CRC64;
MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNQLEV RFPEHPHPLF
VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF EKFPLTRADL ALAHQHWPEL
APWAEQLQAQ WPMPLPGCHR LLLDEGRVTL DLWFGDINEL TSQLDDSLNQ KVDAWFLDGF
APAKNPDMWT QNLFNAMARL ARPGGTLATF TSAGFVRRGL QDAGFTMQKR KGFGRKREML
CGVMEQTLPL PCSAPWFNRT GSSKREAAII GGGIASALLS LALLRRGWQV TLYCADEAPA
LGASGNRQGA LYPLLSKHDE ALNRFFSNAF TFARRFYDQL PVKFDHDWCG VTQLGWDEKS
QHKIAQMLSM DLPAELAVAV EANAVEQITG VATNCSGITY PQGGWLCPAE LTRNVLELAQ
QQGLQIYYQY QLQNLSRKDD CWLLNFAGDQ QATHSVVVLA NGHQISRFSQ TSTLPVYSVA
GQVSHIPTTP ELAELKQVLC YDGYLTPQNP ANQHHCIGAS YHRGSEDTAY SEDDQQQNRQ
RLIDCFPQAQ WAKEVDVSDK EARCGVRCAT RDHLPMVGNV PDYEATLVEY ASLAEQKDEA
VSAPVFDDLF MFAALGSRGL CSAPLCAEIL AAQMSDEPIP MDASTLAALN PNRLWVRKLL
KGKAVKAG
