CMOB_CITBB
ID CMOB_CITBB Reviewed; 323 AA.
AC B5EIQ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_01590};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01590};
GN Name=cmoB {ECO:0000255|HAMAP-Rule:MF_01590}; OrderedLocusNames=Gbem_1402;
OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS Bem) (Geobacter bemidjiensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Citrifermentans.
OX NCBI_TaxID=404380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter bemidjiensis BEM.";
RL Submitted (JUL-2008) 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:0000255|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:0000255|HAMAP-
CC Rule:MF_01590};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01590}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoB family. {ECO:0000255|HAMAP-Rule:MF_01590}.
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DR EMBL; CP001124; ACH38421.1; -; Genomic_DNA.
DR RefSeq; WP_012529833.1; NC_011146.1.
DR AlphaFoldDB; B5EIQ6; -.
DR SMR; B5EIQ6; -.
DR STRING; 404380.Gbem_1402; -.
DR EnsemblBacteria; ACH38421; ACH38421; Gbem_1402.
DR KEGG; gbm:Gbem_1402; -.
DR eggNOG; COG0500; Bacteria.
DR HOGENOM; CLU_052665_0_0_7; -.
DR OMA; CEWRSDF; -.
DR OrthoDB; 1515497at2; -.
DR Proteomes; UP000008825; Chromosome.
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 Gene3D; 3.40.50.150; -; 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 Pfam; PF08003; Methyltransf_9; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00452; TIGR00452; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..323
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_1000201298"
FT BINDING 91
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 105
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 110
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 130
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 180..181
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 196
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 200
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 315
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ SEQUENCE 323 AA; 36907 MW; 1AE1F75E06AE0FFA CRC64;
MSNYDALYRQ LAAMGQERWA EQLQATLPDK LALESTAKMA GWQSAMQSLP EISPSRIELL
DTVTIGSSDD LGQVDREELM AHLQAFHPWR KGPYNFFGIE IDTEWRSDWK WERLLPHIQP
LAGRRVIDVG CGNGYHGWRM RGAGAEFVLG IEPFLLSVQQ FQVMQRYLCD PQHHVIPIGI
EEVPPNLACF DSVFSMGVLY HRRSPLDHLF ELKGCLRPGG ELILETLIVE GDRETIFMPP
GRYAKMRNVW FIPSIAAMTL WLERCGFTDI ACVDTNRTSR EEQRSTEWMR FESLADFLDP
DDAQKTIEGH PAPLRAIFTA TKP