ID CMOB_CAMJE Reviewed; 291 AA.
AC Q0P9S6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 27-MAR-2024, entry version 92.
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=Cj0976;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL35094.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL111168; CAL35094.1; ALT_INIT; Genomic_DNA.
DR PIR; E81372; E81372.
DR RefSeq; YP_002344371.1; NC_002163.1.
DR AlphaFoldDB; Q0P9S6; -.
DR SMR; Q0P9S6; -.
DR IntAct; Q0P9S6; 3.
DR STRING; 192222.Cj0976; -.
DR PaxDb; 192222-Cj0976; -.
DR DNASU; 905267; -.
DR EnsemblBacteria; CAL35094; CAL35094; Cj0976.
DR GeneID; 905267; -.
DR KEGG; cje:Cj0976; -.
DR PATRIC; fig|192222.6.peg.959; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_052665_1_0_7; -.
DR OrthoDB; 9765084at2; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00452; tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; 1.
DR Pfam; PF08003; Methyltransf_9; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..291
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_0000313905"
FT BINDING 61
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 75
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 80
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 100
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 122..124
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 149..150
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 169
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 284
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ SEQUENCE 291 AA; 33786 MW; DC37BE7D649FFB36 CRC64;
MQENLLEKQF LNHPLYAKIQ ELKALNLACN FSLGDSVNLS TNSQAKDEIL AIAKELKPWR
KGPFKIDDLF IDTEWQSFIK FNILKPFMNE ISQKCVADIG CNNGYYMFKM LEFNPAKLIG
FDPSIKYRLQ FELINALAKT PIKYELLGVE DLPSYSLKFD VIFCLGVIYH RSDPIKMLKD
LKAGLNKNGV VFLDTMYIED EREIALVPNK TYSKIPNIYF VPSISALKNW CERAGFKEFE
VLATKKTDEN EQRKTEWIDS FSLENFLDPK DKNLTIEGYE APKRVYIRIK I
//
