CMOB_SHEFN
ID CMOB_SHEFN Reviewed; 330 AA.
AC Q081N2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Sfri_2187;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI72033.1; -; Genomic_DNA.
DR RefSeq; WP_011637643.1; NC_008345.1.
DR AlphaFoldDB; Q081N2; -.
DR SMR; Q081N2; -.
DR STRING; 318167.Sfri_2187; -.
DR EnsemblBacteria; ABI72033; ABI72033; Sfri_2187.
DR KEGG; sfr:Sfri_2187; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_052665_0_0_6; -.
DR OMA; CEWRSDF; -.
DR OrthoDB; 1515497at2; -.
DR Proteomes; UP000000684; Chromosome.
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 Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..330
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_0000313967"
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 330 AA; 37730 MW; 849802E7A06EE912 CRC64;
MINFSSFYKD IADSNLQHWL ETLPAILGKW QRDHKHGNLP KWEKVLNKLH YPQPDNIDFS
SSVTIGTGEQ LSPGQVEKLT NLLEVFQPWR KGPFSVHGIQ IDTEWRSDWK WDRVKNFISP
LKNRTVLDVG CGSGYHMWRM LGDGATRVVG IDPSPLFLCQ FEAIKRVAGN QHPVYLLPLG
IEELPPLDAF DTVFSMGVLY HRRSPIDHLL QLRDQLRVGG ELVLETLVID GDENAVLVPQ
DRYGKMNNVW FIPSVAALML WLKKCEFIDI RCVDIDITSL AEQRSTHWMK NESLVDYLDP
NDVSLTVEGY PAPKRAIIIA TKNQPNHDLV