ID   CMOB_SHELP              Reviewed;         330 AA.
AC   A3QEQ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Shew_2082;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-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; CP000606; ABO23948.1; -; Genomic_DNA.
DR   RefSeq; WP_011865880.1; NC_009092.1.
DR   AlphaFoldDB; A3QEQ0; -.
DR   SMR; A3QEQ0; -.
DR   STRING; 323850.Shew_2082; -.
DR   EnsemblBacteria; ABO23948; ABO23948; Shew_2082.
DR   KEGG; slo:Shew_2082; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_052665_0_0_6; -.
DR   OMA; CEWRSDF; -.
DR   OrthoDB; 1515497at2; -.
DR   Proteomes; UP000001558; 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_0000313968"
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;  37756 MW;  24056217A092091B CRC64;
     MISFSSFYQQ IADSNLQHWL EELPAILGQW QREHKHGNLP KWEKVLNKLH YPAPDRIDFT
     TRVEVGSGDQ LSKGQQEKLK NLLKLFCPWR KGPFDLHGIH IDTEWRSDWK WERVQPHISP
     LKNRTVLDVG CGSGYHMWRM LGDGAKRVVG IDPSPLFLCQ FEAVKRLAGN DHPVHLLPLG
     IEQLPPLDAF DTVFSMGVLY HRRSPIDHLL QLRDQLRTGG ELVLETLVVD GDENTVLVPG
     ERYGKMNNVW FLPSAKALEA WLKKADFVDV RCVDIDVTSL AEQRSTEWMP NESLVDYLDP
     NDVSLTVEGY PAPKRATFIA VKNQPNKDLV