ID A0A498DHT5_9PROT Unreviewed; 329 AA.
AC A0A498DHT5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, 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:RLL55543.1};
GN ORFNames=D8Y20_01160 {ECO:0000313|EMBL:RLL55543.1};
OS Mariprofundus sp. EBB-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=2650971 {ECO:0000313|EMBL:RLL55543.1, ECO:0000313|Proteomes:UP000270267};
RN [1] {ECO:0000313|Proteomes:UP000270267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EBB-1 {ECO:0000313|Proteomes:UP000270267};
RA Lopez A., Barco R., Canela R., Emerson D., Tully B., Abuyen K.,
RA Broomell S., Albino D., Beraki S., Dingmon T., Estrada S., Fernandez M.,
RA Amend J.;
RT "Genome Sequence of Zetaproteobacterium sp. EBB-1: a novel, marine, iron-
RT oxidizing chemolithoautotroph isolated from an iron-sulfide mineral.";
RL Submitted (OCT-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: 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:RLL55543.1}.
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DR EMBL; RCFQ01000002; RLL55543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498DHT5; -.
DR Proteomes; UP000270267; Unassembled WGS sequence.
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:UP000270267};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01590};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT BINDING 97
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 111
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 116
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 136
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 158..160
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 186..187
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 202
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 206
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 321
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ SEQUENCE 329 AA; 37260 MW; 3F055B790B88F0AA CRC64;
MNHYKDQEAL LLQHHLQDSA LGEYSKELLG LYEKGWQKIL KHGDLKRWQG GFELLPDVTP
SALNFNCSAL KIGTADDTSM THDEIKSALQ QMHPWRKGPF DLFGVHIDTE WRSDWKWDRL
ADAITPLEGR TILDVGCGSG YHLWRMLGAD AKLVIGIDPT PLFSMHFATV KRYSPNAPAF
ILPVGIEHMQ VNMGCFDTVF SMGILYHRKS PIDHLIELKN LLNTGGELVI DTLVIEGNAN
QCLMPQGRYA KMRNVWFIPS VEMLKIWLKR AGFKSVNLID VCPTTVQEQR PTEWMTFESL
PDFLDPEDHS LTIEGYPAPV RAVLTASTS
//
