ID I1DZ15_9GAMM Unreviewed; 321 AA.
AC I1DZ15;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:GAB59293.1};
GN ORFNames=RNAN_2288 {ECO:0000313|EMBL:GAB59293.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB59293.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB59293.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB59293.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(2012).
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:GAB59293.1}.
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DR EMBL; BAFK01000012; GAB59293.1; -; Genomic_DNA.
DR RefSeq; WP_008221769.1; NZ_BAFK01000012.1.
DR AlphaFoldDB; I1DZ15; -.
DR STRING; 562729.RNAN_2288; -.
DR OrthoDB; 9773188at2; -.
DR Proteomes; UP000004374; 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:GAB59293.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004374};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:GAB59293.1};
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 152..154
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 180..181
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 195
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 199
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT BINDING 314
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ SEQUENCE 321 AA; 36691 MW; DB643D9228F2F682 CRC64;
MLDFSAFYAQ LAQNKLHRWL ETLPAQLANW SKEALHGDFK QWQKVITNLP PTSASQIELK
QQVQFGTAED ISAGQAQQIR YLLQQLKPWR KGPFNIHGIE IDTEWRSDFK WHRVLPHISA
LKGRTVLDVG CGSGYHLWRM RGEGADFVVG IDPSQLFYAQ FQAIKHFNPD PAVNLIPIGI
DEMPPLKQFD TVFSMGVLYH RRSPLDFLQQ LKNQLRPGGE LILETLVVEG DEHTVLVPGE
RYAKMRNVWF IPSVAALTHW LSRLGFSQVR LVDLNQTSLA EQRKTDWMDN ESLIDFLDAT
DHSKTIEGYP APLRAVIIAN N
//
