ID K6XRN6_9ALTE Unreviewed; 251 AA.
AC K6XRN6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=smtA {ECO:0000313|EMBL:GAC14316.1};
GN Synonyms=cmoM {ECO:0000256|HAMAP-Rule:MF_02057};
GN ORFNames=GLIP_1683 {ECO:0000313|EMBL:GAC14316.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC14316.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC14316.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC14316.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC14316.1}.
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DR EMBL; BAEN01000035; GAC14316.1; -; Genomic_DNA.
DR AlphaFoldDB; K6XRN6; -.
DR STRING; 1127673.GLIP_1683; -.
DR eggNOG; COG2227; Bacteria.
DR Proteomes; UP000006334; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43464:SF96; TRNA 5-CARBOXYMETHOXYURIDINE METHYLTRANSFERASE; 1.
DR Pfam; PF08241; Methyltransf_11; 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:GAC14316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006334};
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 51..143
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT BINDING 29
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 54..55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02057"
SQ SEQUENCE 251 AA; 28481 MW; F69969C9FC4A21E7 CRC64;
MSKNTDQSFD TLMHKFAHNI YGSSKGKLRH ELLVNNLWQY IKPEGEPLEI IDVGGGTGIM
CKTLLELGHT LTFNDLSADA VTMAKQNLAD YQNVTFHCGS LNALNDSKQF DMVICHAVLE
WLSSPFDAIT SLIDLVKPGG IISLSFFNKD AHRFGNLLYG NFDYVEADMK NKNTVRLNPN
NALEPKQVLA HLEELPVNVL NTYGIRCFHD YLRDISKQTS EYEKIKAAEI KYGHLEPYKW
LGKYFQVVIQ C
//
