ID I7B4D1_PSEPT Unreviewed; 318 AA.
AC I7B4D1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_01590};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01590};
GN Name=cmoA {ECO:0000313|EMBL:AFO46158.1};
GN Synonyms=cmoB {ECO:0000256|HAMAP-Rule:MF_01590};
GN OrderedLocusNames=T1E_0299 {ECO:0000313|EMBL:AFO46158.1};
OS Pseudomonas putida (strain DOT-T1E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1196325 {ECO:0000313|EMBL:AFO46158.1, ECO:0000313|Proteomes:UP000006503};
RN [1] {ECO:0000313|Proteomes:UP000006503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOT-T1E {ECO:0000313|Proteomes:UP000006503};
RX PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT DOT-T1E deduced from its annotated genome.";
RL Microb. Biotechnol. 6:598-611(2013).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01590};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoB family. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01590}.
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DR EMBL; CP003734; AFO46158.1; -; Genomic_DNA.
DR RefSeq; WP_004575433.1; NZ_CP110782.1.
DR AlphaFoldDB; I7B4D1; -.
DR SMR; I7B4D1; -.
DR KEGG; ppx:T1E_0299; -.
DR PATRIC; fig|1196325.3.peg.300; -.
DR HOGENOM; CLU_052665_0_0_6; -.
DR Proteomes; UP000006503; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_01590};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT BINDING 88
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 102
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 107
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 126
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 176..177
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 192
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 196
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 311
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ SEQUENCE 318 AA; 36028 MW; 7DCA9F6658ED0054 CRC64;
MIDLSPLVRR LAGTPLASWS QGLQAQLDAK LEKGHGDLDR WRGALEALPA LQPSEVDLVN
GLRLDCDCDD ATRAQMRQAL MGLSPWRKGP FDLFGVHVDT EWRSDWKWSR VGPHLDLKGK
RVLDVGCGNG YYQWRMLGAG ADMVVGVDPN WLFFCQFQAV QQYLPELPAW HLPFALEDLP
ANLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVIEGDEN QVLVPEDRYA
QMRNVWYLPS VPALARWLRR AGFSDVRCVD VSVTSVEEQR STDWMRYQSL SDFLDPNDHS
KTVEGLPAPR RATLLARK
//
