ID   CMOB_CAMC1              Reviewed;         289 AA.
AC   A7ZEA2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Ccon26_12550; ORFNames=CCC13826_2062;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) 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; CP000792; EAT98738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7ZEA2; -.
DR   SMR; A7ZEA2; -.
DR   STRING; 360104.CCC13826_2062; -.
DR   EnsemblBacteria; EAT98738; EAT98738; CCC13826_2062.
DR   KEGG; cco:CCC13826_2062; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_052665_1_0_7; -.
DR   OMA; CEWRSDF; -.
DR   Proteomes; UP000001121; 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..289
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_1000201288"
FT   BINDING         60
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         74
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         79
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         98
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         120..122
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         147..148
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         167
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         282
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   289 AA;  33431 MW;  23733CEAFD860C6E CRC64;
     MDLSKFNEQQ KQILNRIENL ANFDCEFSLS DSVNVKFKNL DQAKKDEIYN LALSLKPWRK
     GPFLLDDIYI DSEWQSFIKF NILAPHLNLA GKCVADVGCN NGYYMFKMLS YDPKSITGFD
     PSVHTYLQFK FLNKFIRSNI NYQLLGVESL PEYAAKFDTI FCLGVIYHRS DPIKMLKELK
     TALNTGGELF LDTMYIDMDG DFALSPKDRY SKIPNIYFVP TLSALQNWCE RAKFKDFTLL
     ETKATDLNEQ RKTQWIDGES LSNFLDPADN TKTIEGYPAP KRAYVRVKI