CMOM_ECOLI
ID CMOM_ECOLI Reviewed; 261 AA.
AC P36566; P77586;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=tRNA 5-carboxymethoxyuridine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02057, ECO:0000305};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02057, ECO:0000269|PubMed:26681692};
DE AltName: Full=cmo5U methyltransferase {ECO:0000255|HAMAP-Rule:MF_02057, ECO:0000303|PubMed:26681692};
GN Name=cmoM {ECO:0000255|HAMAP-Rule:MF_02057, ECO:0000303|PubMed:26681692};
GN Synonyms=smtA {ECO:0000303|PubMed:8566713}, ycbD;
GN OrderedLocusNames=b0921, JW0904;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7513784; DOI=10.1007/bf00280310;
RA Feng J., Yamanaka K., Niki H., Ogura T., Hiraga S.;
RT "New killing system controlled by two genes located immediately upstream of
RT the mukB gene in Escherichia coli.";
RL Mol. Gen. Genet. 243:136-147(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RX PubMed=8566713; DOI=10.1111/j.1574-6968.1995.tb07861.x;
RA Yamanaka K., Ogura T., Niki H., Hiraga S.;
RT "Characterization of the smtA gene encoding an S-adenosylmethionine-
RT dependent methyltransferase of Escherichia coli.";
RL FEMS Microbiol. Lett. 133:59-63(1995).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-26; ASP-73; TRP-124;
RP TYR-150; ARG-209; ASP-213; ARG-246 AND TYR-247.
RC STRAIN=K12 / BW25113;
RX PubMed=26681692; DOI=10.1093/nar/gkv1470;
RA Sakai Y., Miyauchi K., Kimura S., Suzuki T.;
RT "Biogenesis and growth phase-dependent alteration of 5-
RT methoxycarbonylmethoxyuridine in tRNA anticodons.";
RL Nucleic Acids Res. 44:509-523(2016).
CC -!- FUNCTION: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U)
CC to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in
CC tRNAs. Four tRNAs (tRNA(Ala1), tRNA(Ser1), tRNA(Pro3) and tRNA(Thr4))
CC are fully modified with mcmo5U in stationary-phase E.coli. Also present
CC at low frequency in tRNA(Leu3) and tRNA(Val1).
CC {ECO:0000269|PubMed:26681692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine
CC = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54080, Rhea:RHEA-COMP:13383, Rhea:RHEA-
CC COMP:13781, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136879,
CC ChEBI:CHEBI:138053; Evidence={ECO:0000255|HAMAP-Rule:MF_02057,
CC ECO:0000269|PubMed:26681692};
CC -!- INDUCTION: Expression is positively regulated by H-NS.
CC {ECO:0000269|PubMed:8566713}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoM family. {ECO:0000255|HAMAP-Rule:MF_02057,
CC ECO:0000305}.
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DR EMBL; D26440; BAA05456.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74007.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35667.1; -; Genomic_DNA.
DR PIR; H64831; H64831.
DR RefSeq; NP_415441.1; NC_000913.3.
DR RefSeq; WP_001298300.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P36566; -.
DR SMR; P36566; -.
DR BioGRID; 4261464; 139.
DR IntAct; P36566; 11.
DR STRING; 511145.b0921; -.
DR jPOST; P36566; -.
DR PaxDb; P36566; -.
DR PRIDE; P36566; -.
DR EnsemblBacteria; AAC74007; AAC74007; b0921.
DR EnsemblBacteria; BAA35667; BAA35667; BAA35667.
DR GeneID; 945547; -.
DR KEGG; ecj:JW0904; -.
DR KEGG; eco:b0921; -.
DR PATRIC; fig|1411691.4.peg.1355; -.
DR EchoBASE; EB2086; -.
DR eggNOG; COG2227; Bacteria.
DR HOGENOM; CLU_061533_0_1_6; -.
DR InParanoid; P36566; -.
DR OMA; CHGVLEY; -.
DR PhylomeDB; P36566; -.
DR BioCyc; EcoCyc:EG12167-MON; -.
DR BioCyc; MetaCyc:EG12167-MON; -.
DR PRO; PR:P36566; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0097697; F:tRNA 5-carboxymethoxyuridine 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 HAMAP; MF_02057; tRNA_methyltr_CmoM; 1.
DR InterPro; IPR033664; Cmo5U_methylTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..261
FT /note="tRNA 5-carboxymethoxyuridine methyltransferase"
FT /id="PRO_0000071990"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8XDG3, ECO:0000255|HAMAP-
FT Rule:MF_02057"
FT BINDING 52..53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8XDG3, ECO:0000255|HAMAP-
FT Rule:MF_02057"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8XDG3, ECO:0000255|HAMAP-
FT Rule:MF_02057"
FT BINDING 102..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8XDG3, ECO:0000255|HAMAP-
FT Rule:MF_02057"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8XDG3, ECO:0000255|HAMAP-
FT Rule:MF_02057"
FT MUTAGEN 26
FT /note="R->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 73
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 124
FT /note="W->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 150
FT /note="Y->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 209
FT /note="R->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 213
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 246
FT /note="R->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT MUTAGEN 247
FT /note="Y->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:26681692"
FT CONFLICT 180
FT /note="L -> V (in Ref. 1; BAA05456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29814 MW; EB8B4CB681A2DC1C CRC64;
MQDRNFDDIA EKFSRNIYGT TKGQLRQAIL WQDLDRVLAE MGPQKLRVLD AGGGEGQTAI
KMAERGHQVI LCDLSAQMID RAKQAAEAKG VSDNMQFIHC AAQDVASHLE TPVDLILFHA
VLEWVADPRS VLQTLWSVLR PGGVLSLMFY NAHGLLMHNM VAGNFDYVQA GMPKKKKRTL
SPDYPRDPAQ VYLWLEEAGW QIMGKTGVRV FHDYLREKHQ QRDCYEALLE LETRYCRQEP
YITLGRYIHV TARKPQSKDK V
