CMOB_VIBVU
ID CMOB_VIBVU Reviewed; 323 AA.
AC Q8DAP0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=VV1_2153;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AE016795; AAO10538.1; -; Genomic_DNA.
DR RefSeq; WP_011080032.1; NC_004459.3.
DR PDB; 7CT8; X-ray; 2.10 A; A/B=1-323.
DR PDB; 7CT9; X-ray; 2.30 A; A/B=1-323.
DR PDB; 7CTA; X-ray; 2.90 A; A/B=1-323.
DR PDBsum; 7CT8; -.
DR PDBsum; 7CT9; -.
DR PDBsum; 7CTA; -.
DR AlphaFoldDB; Q8DAP0; -.
DR SMR; Q8DAP0; -.
DR EnsemblBacteria; AAO10538; AAO10538; VV1_2153.
DR KEGG; vvu:VV1_2153; -.
DR HOGENOM; CLU_052665_0_0_6; -.
DR OMA; CEWRSDF; -.
DR Proteomes; UP000002275; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Transferase; tRNA processing.
FT CHAIN 1..323
FT /note="tRNA U34 carboxymethyltransferase"
FT /id="PRO_0000313989"
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 152..154
FT /ligand="carboxy-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:134278"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT BINDING 181..182
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"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:7CT8"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:7CT9"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 216..230
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:7CT8"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:7CT9"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:7CT8"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:7CT8"
SQ SEQUENCE 323 AA; 37271 MW; 2C750EF673364599 CRC64;
MFNFANFYQL IAQDTRLQPW LNVLPQQLTD WQNAEHGDFP RWLKALNKIP EGAPDQIDIK
HSVTISNDTP FHQGELKKLE SLLRTFHPWR KGPYTVHGIH IDTEWRSDWK WDRVLPHISP
LKNRSVLDVG CGNGYHMWRM LGEGARLCVG IDPSHLFLIQ FEAIRKLMGG DQRAHLLPLG
IEQLPKLEAF DTVFSMGVLY HRRSPLDHLI QLKDQLVSGG ELILETLVIE GDETAVLVPK
ERYAQMRNVY FFPSARALKV WLELVGFEDV RIVDENVTSV DEQRTTNWMT HNSLPDYLDQ
NDPSKTVEGY PAPRRAILVA KKP
