CMOM_ECO57
ID CMOM_ECO57 Reviewed; 261 AA.
AC Q8XDG3; Q7AG53;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=tRNA 5-carboxymethoxyuridine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02057};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02057};
DE AltName: Full=cmo5U methyltransferase {ECO:0000255|HAMAP-Rule:MF_02057};
GN Name=cmoM {ECO:0000255|HAMAP-Rule:MF_02057};
GN Synonyms=smtA {ECO:0000312|EMBL:AAG55406.1};
GN OrderedLocusNames=ECs1004 {ECO:0000312|EMBL:BAB34427.1},
GN Z1268 {ECO:0000312|EMBL:AAG55406.1};
GN ORFNames=AO055_05240 {ECO:0000312|EMBL:ALH89716.1},
GN ASO15_05275 {ECO:0000312|EMBL:KRQ16836.1};
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 / 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / WS4202;
RA Fellner L., Huptas C., Simon S., Krementowski A., Scherer S., Neuhaus K.;
RT "Draft genome sequence of three European lab-derivates from the
RT enterohemorrhagic E. coli O157:H7 strain EDL933, including two plasmids.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / G10;
RA Staji H., Salehi T.Z., Orsini M., Tonelli A.;
RT "Genome sequence of Escherichia coli O157:H7 strains isolated from cattle
RT in Javadabad, Iran.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:4HTF}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RA Filippova E.V., Minasov G., Shuvalova L., Kiryukhina O., Jedrzejczak R.,
RA Joachimiak A., Anderson W.F.;
RT "Crystal structure of S-adenosylmethionine-dependent methyltransferase from
RT Escherichia coli in complex with S-adenosylmethionine.";
RL Submitted (NOV-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U)
CC to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in
CC tRNAs. {ECO:0000255|HAMAP-Rule:MF_02057}.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoM family. {ECO:0000255|HAMAP-Rule:MF_02057}.
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DR EMBL; AE005174; AAG55406.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34427.1; -; Genomic_DNA.
DR EMBL; CP012802; ALH89716.1; -; Genomic_DNA.
DR EMBL; LMXL01000002; KRQ16836.1; -; Genomic_DNA.
DR PIR; B85618; B85618.
DR PIR; D90754; D90754.
DR RefSeq; NP_309031.1; NC_002695.1.
DR RefSeq; WP_001301572.1; NZ_SWKA01000005.1.
DR PDB; 4HTF; X-ray; 1.60 A; A/B=1-261.
DR PDBsum; 4HTF; -.
DR AlphaFoldDB; Q8XDG3; -.
DR SMR; Q8XDG3; -.
DR STRING; 155864.EDL933_1184; -.
DR DNASU; 917747; -.
DR EnsemblBacteria; AAG55406; AAG55406; Z1268.
DR EnsemblBacteria; BAB34427; BAB34427; ECs_1004.
DR GeneID; 917747; -.
DR KEGG; ece:Z1268; -.
DR KEGG; ecs:ECs_1004; -.
DR PATRIC; fig|386585.9.peg.1124; -.
DR eggNOG; COG2227; Bacteria.
DR HOGENOM; CLU_061533_0_1_6; -.
DR OMA; CHGVLEY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0097697; F:tRNA 5-carboxymethoxyuridine methyltransferase activity; IEA:UniProtKB-UniRule.
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 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..261
FT /note="tRNA 5-carboxymethoxyuridine methyltransferase"
FT /id="PRO_0000436068"
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02057,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:4HTF"
FT BINDING 52..53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02057,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:4HTF"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02057,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:4HTF"
FT BINDING 102..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02057,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:4HTF"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02057,
FT ECO:0000269|Ref.5, ECO:0007744|PDB:4HTF"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 188..197
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4HTF"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:4HTF"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:4HTF"
SQ SEQUENCE 261 AA; 29844 MW; FB9A4DA690A3DC1C CRC64;
MQDRNFDDIA EKFSRNIYGT TKGQLRQAIL WQDLDRVLAE MGPQKLRVLD AGGGEGQTAI
KMAERGHQVI LCDLSAQMID RAKQAAEAKG VSDNMQFIHC AAQDVASHLE TPVDLILFHA
VLEWVADPRS VLQTLWSVLR PGGVLSLMFY NAHGLLMHNM VAGNFDYVQA GMPKKKKRTL
SPDYPRDPTQ VYLWLEEAGW QIMGKTGVRV FHDYLREKHQ QRDCYEALLE LETRYCRQEP
YITLGRYIHV TARKPQSKDK V
