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Entry: A0A385Z5F4_9PSED
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Original site: A0A385Z5F4_9PSED 
ID   A0A385Z5F4_9PSED        Unreviewed;       319 AA.
AC   A0A385Z5F4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=cmoB {ECO:0000256|HAMAP-Rule:MF_01590,
GN   ECO:0000313|EMBL:AYC33911.1};
GN   ORFNames=D3880_16770 {ECO:0000313|EMBL:AYC33911.1};
OS   Pseudomonas cavernae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2320867 {ECO:0000313|EMBL:AYC33911.1, ECO:0000313|Proteomes:UP000265560};
RN   [1] {ECO:0000313|Proteomes:UP000265560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2W31S-8 {ECO:0000313|Proteomes:UP000265560};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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: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; CP032419; AYC33911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385Z5F4; -.
DR   KEGG; pcav:D3880_16770; -.
DR   OrthoDB; 9773188at2; -.
DR   Proteomes; UP000265560; 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 {ECO:0000313|Proteomes:UP000265560};
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   319 AA;  36077 MW;  CAC74A25703FB54B CRC64;
     MIDLAPLARR LAGTPLAAWA AGLQAQLDAK LEVGHGDLQR WQGALDALPP LNASRIELAD
     DFRLDGACDD AQRAQLRQAL FGLSPWRKGP FQLFDVHVDT EWRSDWKWAR VAPHLDLKGK
     RVLDVGCGNG YYMWRMLGAG ADSVIGVDPN WLFFCQFQAL QRYLPELPAW HLPFALEELP
     EKLEGFDSVF SMGVLYHRRS PIDHLLALKD CLRKGGELVL ETLVVDGDER QVLVPEDRYA
     QMRNVWFLPS APALALWLRR AGFVEVRCVD VSVTSVEEQR ATDWMRYQSL PDFLDPSDRS
     RTIEGLPAPK RAVLVARKP
//
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