CMOB_ECO8A
ID CMOB_ECO8A Reviewed; 323 AA.
AC B7M2G2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_01590};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01590};
GN Name=cmoB {ECO:0000255|HAMAP-Rule:MF_01590}; OrderedLocusNames=ECIAI1_1958;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-
CC methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-
CC carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_01590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine
CC = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:52848, Rhea:RHEA-COMP:13381, Rhea:RHEA-
CC COMP:13383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:134278,
CC ChEBI:CHEBI:136877, ChEBI:CHEBI:136879; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01590};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01590}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoB family. {ECO:0000255|HAMAP-Rule:MF_01590}.
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DR EMBL; CU928160; CAQ98811.1; -; Genomic_DNA.
DR RefSeq; WP_000564745.1; NC_011741.1.
DR AlphaFoldDB; B7M2G2; -.
DR SMR; B7M2G2; -.
DR GeneID; 66674238; -.
DR KEGG; ecr:ECIAI1_1958; -.
DR HOGENOM; CLU_052665_0_0_6; -.
DR OMA; CEWRSDF; -.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01590; tRNA_carboxymethyltr_CmoB; 1.
DR InterPro; IPR010017; CmoB.
DR InterPro; IPR027555; Mo5U34_MeTrfas-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08003; Methyltransf_9; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00452; TIGR00452; 1.
PE 3: Inferred from homology;
KW Transferase; tRNA processing.
FT CHAIN 1..323
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_1000201296"
FT BINDING 91
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 105
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 110
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 130
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 152..154
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 181..182
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 196
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 200
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 315
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ SEQUENCE 323 AA; 37127 MW; 34E26B50D7156CC6 CRC64;
MIDFGNFYSL IAKNHLSHWL ETLPAQIANW QREQQHGLFK QWSNAVEFLP EIKPYRLDLL
HSVTAESEEP LSTGQIKRIE TLMRNLMPWR KGPFSLYGVN IDTEWRSDWK WDRVLPHLSD
LTGRTILDVG CGSGYHMWRM IGAGAHLAVG IDPTQLFLCQ FEAVRKLLGN DQRAHLLPLG
IEQLPALKAF DTVFSMGVLY HRRSPLEHLW QLKDQLVNEG ELVLETLVID GDENTVLVPG
DRYAQMRNVY FIPSALALKN WLKKCGFVDI RIVDVCVTTT EEQRRTEWMV TESLSDFLDP
HDPSKTVEGY PAPKRAVLIA RKP