ID A0A097R1M8_HAFAL Unreviewed; 323 AA.
AC A0A097R1M8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=AT03_09720 {ECO:0000313|EMBL:AIU72632.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU72632.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU72632.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU72632.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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; CP009706; AIU72632.1; -; Genomic_DNA.
DR RefSeq; WP_025801905.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R1M8; -.
DR KEGG; hav:AT03_09720; -.
DR PATRIC; fig|1453496.5.peg.1950; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_052665_0_0_6; -.
DR OrthoDB; 9773188at2; -.
DR Proteomes; UP000029986; Chromosome.
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:AIU72632.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:AIU72632.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT BINDING 91
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 105
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 110
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 130
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 181..182
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 200
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 315
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ SEQUENCE 323 AA; 36798 MW; 65A649656EE0B5E5 CRC64;
MIEFGNFYQR IANSPLSHWL EVLPAQLAAW QRESLHGKFK DWFNAVDRLP EITPHALDLL
HGVSAQAEPE LGPGQKEGIE KMLRALMPWR KGPFDLYGIH INTEWRSDWK WERVLPHISP
LEGRTILDVG CGSGYHLWRM IGAGAHFAVG IDPMQLFLCQ FEAVRKLLGG DQRAHLLPLG
IEQLPELAAF DTVFSMGVLY HRRSPLDHLY QLKNQLVKDG ELVLETLVIE GDENQVLVPG
DRYAQMRNVY FIPSAKALVK WLEKCGFVDV RIVDSCVTTL DEQRRTDWMI SESLAEFLDP
NDQTKTVEGY PAPIRAVIVA RKP
//
