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Database: UniProt
Entry: U1JXN9_9GAMM
LinkDB: U1JXN9_9GAMM
Original site: U1JXN9_9GAMM 
ID   U1JXN9_9GAMM            Unreviewed;       322 AA.
AC   U1JXN9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_01590};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01590};
GN   Name=cmoB {ECO:0000256|HAMAP-Rule:MF_01590};
GN   ORFNames=PMAN_16010 {ECO:0000313|EMBL:ERG25052.1};
OS   Pseudoalteromonas marina DSM 17587.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG25052.1, ECO:0000313|Proteomes:UP000016528};
RN   [1] {ECO:0000313|EMBL:ERG25052.1, ECO:0000313|Proteomes:UP000016528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01590};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01590}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. CmoB family. {ECO:0000256|HAMAP-Rule:MF_01590}.
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:ERG25052.1}.
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DR   EMBL; AHCB02000055; ERG25052.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1JXN9; -.
DR   Proteomes; UP000016528; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00452; tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; 1.
DR   PANTHER; PTHR43464; METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43464:SF19; UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08003; Methyltransf_9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:ERG25052.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:ERG25052.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT   BINDING         92
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         106
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         111
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         131
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         153..155
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         181..182
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         196
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         200
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         315
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
SQ   SEQUENCE   322 AA;  36803 MW;  59C33CAF2DB916FB CRC64;
     MSQWFNQFYA AIAQSPLSHW LETLPAQLKH WQLEASHGDL PQWQKVLKNL PEINTTHVDI
     ATKVEIGAPG EMSEGQQKQT THLLKRMMPW RKGPFSVHGI EINTEWRSDW KWDRLLPHIE
     PLKGRTVLDI GCGSGYHLWR MRGEGAEFVV GIDPSDLFLC QFQAIKHFNP DENVHLLPLG
     VEALPELKAF DTVFSMGVLY HRRSPIDFLA QLKAQLRPGG ELVLETLVIE GDENTVLVPT
     DRYAKMRNVW FIPSTAALKL WMERVGFKDV QIKDCAITTL DEQRKTDWME NESLVDFLDP
     TDTSKTIEGY PAPLRAILTA KA
//
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