ID   CMOB_PSEPG              Reviewed;         318 AA.
AC   B0KV20;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
GN   OrderedLocusNames=PputGB1_4367;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) 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; CP000926; ABZ00256.1; -; Genomic_DNA.
DR   RefSeq; WP_012273921.1; NC_010322.1.
DR   AlphaFoldDB; B0KV20; -.
DR   SMR; B0KV20; -.
DR   STRING; 76869.PputGB1_4367; -.
DR   EnsemblBacteria; ABZ00256; ABZ00256; PputGB1_4367.
DR   KEGG; ppg:PputGB1_4367; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_052665_0_0_6; -.
DR   OMA; CEWRSDF; -.
DR   Proteomes; UP000002157; 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   Transferase; tRNA processing.
FT   CHAIN           1..318
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_1000087969"
FT   BINDING         88
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         102
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         107
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         126
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         176..177
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         192
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         311
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   318 AA;  36107 MW;  E27A56E4847F0F0A CRC64;
     MIDLSPLVRR LAGTPLASWS QGLQAQLEAK LEKGHGDLDR WRGALQALPT LQPSEIDLVN
     GLRLDCDCDD ATRAQMRQAL MGLSPWRKGP FDLFGVHVDT EWHSDWKWSR VSPHLNLKGK
     RVLDVGCGNG YYQWRMLGAG ADMVIGVDPN WLFFCQFQAV QQYLPELPAW HLPFALEDLP
     ANLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVIEGDEN QVLVPEDRYA
     QMRNVWYLPS VPALARWLRR AGFSDVRCVD VSVTSVEEQR STEWMRYQSL GDFLDPNDHS
     KTLEGLPAPR RATLLARK