ID CMOB_PSEPK Reviewed; 318 AA.
AC Q88MX8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=PP_1440;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67062.1; -; Genomic_DNA.
DR RefSeq; NP_743598.1; NC_002947.4.
DR RefSeq; WP_010952540.1; NC_002947.4.
DR AlphaFoldDB; Q88MX8; -.
DR SMR; Q88MX8; -.
DR STRING; 160488.PP_1440; -.
DR PaxDb; 160488-PP_1440; -.
DR GeneID; 83682025; -.
DR KEGG; ppu:PP_1440; -.
DR PATRIC; fig|160488.4.peg.1528; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_052665_0_0_6; -.
DR OrthoDB; 9773188at2; -.
DR PhylomeDB; Q88MX8; -.
DR BioCyc; PPUT160488:G1G01-1532-MONOMER; -.
DR Proteomes; UP000000556; 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 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 PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43464:SF92; TRNA U34 CARBOXYMETHYLTRANSFERASE; 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..318
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_0000313949"
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; 36056 MW; 513CAE5635DA14B2 CRC64;
MIDLSPLVRR LAGTPLASWS QGLQAQLDAK LEKGHGDLDR WRGALEALPA LQPSEIDLVN
GLRLDCDCDD ATRAQMRQAL MGLSPWRKGP FDLFGVHVDT EWRSDWKWSR VGPHLDLQGK
RVLDVGCGNG YYQWRMLGAG ADMVIGVDPN WLFFCQFQAV QQYLPELPAW HLPFALEDLP
ANLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVIEGDEN QVLVPEDRYA
QMRNVWYLPS VPALARWLRR AGFSDVRCVD VSVTSVEEQR STDWMRYQSL SDFLDPNDHS
KTVEGLPAPR RATLLARK
//
