ID A0A0Q1CLB6_9PSED Unreviewed; 318 AA.
AC A0A0Q1CLB6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AQS70_00885 {ECO:0000313|EMBL:KQB55720.1};
OS Pseudomonas endophytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB55720.1, ECO:0000313|Proteomes:UP000050342};
RN [1] {ECO:0000313|EMBL:KQB55720.1, ECO:0000313|Proteomes:UP000050342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSTT44 {ECO:0000313|EMBL:KQB55720.1,
RC ECO:0000313|Proteomes:UP000050342};
RA Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT isolated from raw cows milk.";
RL Submitted (OCT-2015) 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}.
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:KQB55720.1}.
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DR EMBL; LLWH01000001; KQB55720.1; -; Genomic_DNA.
DR RefSeq; WP_055101061.1; NZ_LLWH01000001.1.
DR AlphaFoldDB; A0A0Q1CLB6; -.
DR STRING; 1563157.AQS70_00885; -.
DR OrthoDB; 9773188at2; -.
DR Proteomes; UP000050342; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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: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 Methyltransferase {ECO:0000313|EMBL:KQB55720.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:KQB55720.1};
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; 35995 MW; AD4AEEB923A78A96 CRC64;
MIDLSPLARR LAGTPLAEWA ATVQAQLDVK MDKGHGDLER WQSALDALPN VVPSEIDLLN
GLTLDTACDD ATRAQMRQAL LGLSPWRKGP FDLFGVHVDT EWHSDWKWSR VAPHIDLKGK
RILDVGCGNG YYMWRMLGAG AHSVIGVDPN WLFFCQFQAV QRFLQQEAVW HLPFPFEDLP
PNLEGFDTVF SMGVFYHRRS PIEHLLALKD CLVKGGELVL ETLVIEGDVN QVLVPEDRYA
QMRNVWFLPS IAALERWLRR AGFSDVRCVD VSITTVEEQR ATEWMKFQSL SDYLDPNDPS
KTIEGLPAPM RAVIVAKK
//
