ID I7C8Y8_PSEPT Unreviewed; 249 AA.
AC I7C8Y8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=tRNA 5-carboxymethoxyuridine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02057};
DE AltName: Full=cmo5U methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
GN Name=smtA {ECO:0000313|EMBL:AFO49581.1};
GN Synonyms=cmoM {ECO:0000256|HAMAP-Rule:MF_02057};
GN OrderedLocusNames=T1E_3749 {ECO:0000313|EMBL:AFO49581.1};
OS Pseudomonas putida (strain DOT-T1E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1196325 {ECO:0000313|EMBL:AFO49581.1, 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 the methylation of 5-carboxymethoxyuridine (cmo5U)
CC to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in
CC tRNAs. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine
CC = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54080, Rhea:RHEA-COMP:13383, Rhea:RHEA-
CC COMP:13781, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136879,
CC ChEBI:CHEBI:138053; Evidence={ECO:0000256|HAMAP-Rule:MF_02057};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoM family. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02057}.
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DR EMBL; CP003734; AFO49581.1; -; Genomic_DNA.
DR AlphaFoldDB; I7C8Y8; -.
DR KEGG; ppx:T1E_3749; -.
DR PATRIC; fig|1196325.3.peg.3711; -.
DR HOGENOM; CLU_061533_0_1_6; -.
DR Proteomes; UP000006503; Chromosome.
DR GO; GO:0097697; F:tRNA (5-carboxymethoxyuridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02057; tRNA_methyltr_CmoM; 1.
DR InterPro; IPR033664; Cmo5U_methylTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43464:SF96; TRNA 5-CARBOXYMETHOXYURIDINE METHYLTRANSFERASE; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057,
KW ECO:0000313|EMBL:AFO49581.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02057};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02057}.
FT BINDING 26
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 49..50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
SQ SEQUENCE 249 AA; 28346 MW; 7C8D49126029DE28 CRC64;
MNDRHFDELA TRFAEKIYGG AKGAIRLAVL QADLAEALPD RPLRILDIGA GLGHMALWLA
ERGHQLTLAE PAAPMLDGAR ARFAEAGQTA TFIQAPWQDL LGQLTERYDL VLCHAVLEWL
AEPESILPVL HQFTAPGGWL SLAFYNRDAL VYRNLLKGHF RKLRSNRLEG EKQSLTPQKP
LDPRELKAQL EPMWQVESES GVRVFHDYMP KEFQSKAELL DLLEMELAHR RHPTFAGLGR
YLHWVCRPR
//
