ID A0A1E7Q5N9_9GAMM Unreviewed; 255 AA.
AC A0A1E7Q5N9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tRNA 5-carboxymethoxyuridine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_02057};
DE AltName: Full=cmo5U methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057};
GN Name=cmoM {ECO:0000256|HAMAP-Rule:MF_02057};
GN ORFNames=BI198_07910 {ECO:0000313|EMBL:OEY69494.1};
OS Rheinheimera salexigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY69494.1, ECO:0000313|Proteomes:UP000242258};
RN [1] {ECO:0000313|Proteomes:UP000242258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH87 {ECO:0000313|Proteomes:UP000242258};
RA Wan X., Hou S.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U)
CC to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in
CC tRNAs. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine
CC = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54080, Rhea:RHEA-COMP:13383, Rhea:RHEA-
CC COMP:13781, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136879,
CC ChEBI:CHEBI:138053; Evidence={ECO:0000256|HAMAP-Rule:MF_02057};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. CmoM family. {ECO:0000256|HAMAP-Rule:MF_02057}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02057}.
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:OEY69494.1}.
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DR EMBL; MKEK01000001; OEY69494.1; -; Genomic_DNA.
DR RefSeq; WP_070049064.1; NZ_MKEK01000001.1.
DR AlphaFoldDB; A0A1E7Q5N9; -.
DR STRING; 1628148.BI198_07910; -.
DR OrthoDB; 4697647at2; -.
DR Proteomes; UP000242258; Unassembled WGS sequence.
DR GO; GO:0097697; F:tRNA (5-carboxymethoxyuridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02057; tRNA_methyltr_CmoM; 1.
DR InterPro; IPR033664; Cmo5U_methylTrfase.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43861:SF1; TRANS-ACONITATE 2-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02057,
KW ECO:0000313|EMBL:OEY69494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242258};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02057};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02057}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_02057}.
FT DOMAIN 44..155
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 52..53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
SQ SEQUENCE 255 AA; 28556 MW; DB7CE5864F41CEF0 CRC64;
MQKPDRNFDD IAAKFGRNIY DTTKGKIRQQ VLLRDLGQLA VLQQPCHILD VGAGQGQIAL
HLAAQGHSVL LTDISSEMLA TAKQAADTLN LTTVDFQQIS LSELVQQQQQ KAQYKLILCH
AMLEWLAEPE QAIAQLKQLL APGGILSLMF YNIDAKRLSN IIYGNFAYVA ADMQVKKKVR
LSPQNPLQPN AVLSWCQAAG LTLIAKTGVR CFHDYLRNLE QQQTEFEQLL ALELAYNRIE
PYASLGRYQH LLLQG
//
