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Database: UniProt
Entry: A0A010RU11_PSEFL
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ID   A0A010RU11_PSEFL        Unreviewed;       318 AA.
AC   A0A010RU11;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ORFNames=HK44_011150 {ECO:0000313|EMBL:EXF92439.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF92439.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF92439.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF92439.1,
RC   ECO:0000313|Proteomes:UP000022611};
RX   PubMed=21742869; DOI=10.1128/JB.05530-11;
RA   Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA   Karpinets T.V., Brown S.D., Sayler G.S.;
RT   "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT   genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT   HK44.";
RL   J. Bacteriol. 193:5009-5010(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF92439.1}.
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DR   EMBL; AFOY02000017; EXF92439.1; -; Genomic_DNA.
DR   RefSeq; WP_019693430.1; NZ_AFOY02000017.1.
DR   AlphaFoldDB; A0A010RU11; -.
DR   PATRIC; fig|1042209.11.peg.4635; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_052665_0_0_6; -.
DR   OrthoDB; 9773188at2; -.
DR   Proteomes; UP000022611; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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:SF19; UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08003; Methyltransf_9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EXF92439.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022611};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:EXF92439.1};
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         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;  36186 MW;  86F23F8D956741FD CRC64;
     MIDLSPLARR LAGTPLADWA NTLQAQLDVK MEKGHGDLER WQSALDALPK LQPSEVDLLN
     GLTLDTDCDD ETRAQMRTAL MGLSPWRKGP FDLFGVHVDT EWRSDWKWSR VAPHLDLKGK
     RILDVGCGNG YYMWRMLGAG ADSVIGVDPN WLFFCQFQAV QRYLSEPNAW HLPFPFEDLP
     PNLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVIEGDEQ QVLVPEDRYA
     QMRNVWFLPS VPALMLWLRR AGFSDVRCVD VSVTTVEEQR GTEWMKYQSL SDFLDPEDHS
     KTIEGLPAPM RAVIVAKK
//
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