ID   CMOB_HELAH              Reviewed;         262 AA.
AC   Q17Y58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Hac_0607;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99418.1; -; Genomic_DNA.
DR   RefSeq; WP_011577532.1; NC_008229.1.
DR   AlphaFoldDB; Q17Y58; -.
DR   SMR; Q17Y58; -.
DR   STRING; 382638.Hac_0607; -.
DR   EnsemblBacteria; CAJ99418; CAJ99418; Hac_0607.
DR   KEGG; hac:Hac_0607; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_052665_1_0_7; -.
DR   OMA; CEWRSDF; -.
DR   OrthoDB; 1515497at2; -.
DR   BioCyc; HACI382638:HAC_RS02675-MON; -.
DR   Proteomes; UP000000775; 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..262
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_0000313927"
FT   BINDING         25
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         39
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         44
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         63
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         114..115
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         135
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         250
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   262 AA;  29961 MW;  8BBBFD72A856B1C2 CRC64;
     MLICNDNLNQ KTLLEEIMAL RPWRKGPFEI SKIKIDSEWD SSIKWDLVKN ATSLKDKIVA
     DVGCNNGYYL FKMLEHGPKS LVGFDPGVLV KKQFEFLAPF FDKEKKIIYK SLGVEDLNEK
     YPNAFDVIFC LGVLYHRKSP LETLKALYHA LKIGGELVLD TLIIDSPLDI ALCPKKTYAK
     MKNAYFIPSI SALKGWCERV GFGDFEIISV LKTTPKEQRK TDFILGQSLE DFLDKKDHSK
     TLEGYDAPLR GYFKMLKSSS KR