ID   CMOB_PSYA2              Reviewed;         350 AA.
AC   Q4FQB2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Psyc_1948;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19796.1; -; Genomic_DNA.
DR   RefSeq; WP_011281205.1; NC_007204.1.
DR   AlphaFoldDB; Q4FQB2; -.
DR   SMR; Q4FQB2; -.
DR   STRING; 259536.Psyc_1948; -.
DR   EnsemblBacteria; AAZ19796; AAZ19796; Psyc_1948.
DR   KEGG; par:Psyc_1948; -.
DR   eggNOG; COG2227; Bacteria.
DR   HOGENOM; CLU_052665_0_0_6; -.
DR   OMA; CEWRSDF; -.
DR   OrthoDB; 1515497at2; -.
DR   Proteomes; UP000000546; 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..350
FT                   /note="tRNA U34 carboxymethyltransferase"
FT                   /id="PRO_0000313954"
FT   BINDING         101
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         125
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         150
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         172..174
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         208..209
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         224
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         228
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
FT   BINDING         343
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   350 AA;  39507 MW;  FC91463B81C2F4C3 CRC64;
     MLNNTILHAE RELYLTLLAW AQQQPNAYEW LTQLPTWLND IKDKANYAHA PAYQASVARL
     PTLTVDNVQL NSDILTIDAQ LSDSERKQAT ALLKQLMPWR KGPFKIGSSQ NEGEQAEPIF
     IDTEWHSDWK WQRVAPHLGN LKGRRVLDVG GGSGYHGWRM AGAGADTVII IDPSCLFYHQ
     FMAIRHFVGS ADAHDIGRYR THYIPVPLEA LPDNSQLFDT VFSMGVLYHR QSPFEHLQQL
     KGQLVKGGEL VLETLVIEGD ANTVLVPHDR YAQMNNVYFL PSVAALIGWL EKAGFTEVRC
     VDVAVTSTDE QRKTEWMNYH SLADFLDPND PTKTIEGYPA PMRATLIAKK