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Database: UniProt
Entry: A0A0C3EAQ2_9VIBR
LinkDB: A0A0C3EAQ2_9VIBR
Original site: A0A0C3EAQ2_9VIBR 
ID   A0A0C3EAQ2_9VIBR        Unreviewed;       323 AA.
AC   A0A0C3EAQ2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, 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=SU60_06790 {ECO:0000313|EMBL:KIN11503.1};
OS   Vibrio mytili.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN11503.1, ECO:0000313|Proteomes:UP000031977};
RN   [1] {ECO:0000313|EMBL:KIN11503.1, ECO:0000313|Proteomes:UP000031977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN11503.1,
RC   ECO:0000313|Proteomes:UP000031977};
RA   Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT   "Draft genome of Vibrio mytili type strain CAIM 528.";
RL   Submitted (JAN-2015) 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: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:KIN11503.1}.
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DR   EMBL; JXOK01000019; KIN11503.1; -; Genomic_DNA.
DR   RefSeq; WP_041154850.1; NZ_JXOK01000019.1.
DR   AlphaFoldDB; A0A0C3EAQ2; -.
DR   STRING; 50718.SU60_06790; -.
DR   OrthoDB; 9773188at2; -.
DR   Proteomes; UP000031977; 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:KIN11503.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01590, ECO:0000313|EMBL:KIN11503.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01590}.
FT   BINDING         91
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         105
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         110
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         130
FT                   /ligand="carboxy-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:134278"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01590"
FT   BINDING         152..154
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   323 AA;  37134 MW;  9537C44B259768F6 CRC64;
     MFNFANFYQL IAQDTRLQPW LNVLPQQLTD WQNAEHGDFG RWLKALNKIP EGSPNQIDIQ
     HSVTISNDTP FHEGELKKLE NLLRTFHPWR KGPYTVHGIH IDTEWRSDWK WDRVLPHISP
     LKNRSVLDVG CGNGYHMWRM LGEGARLCVG IDPSHLFLIQ FEAIRKLMGD DQRAHLLPLG
     IEQLPKLEAF DTVFSMGVLY HRRSPLDHLI QLKDQLVSGG ELVLETLVIE GDENAVLVPT
     SRYAQMRNVY FFPSAKALKV WLELVGFENV RIVDESITTT GEQRTTDWMT HNSLPDYLDP
     NDPSKTVEGY PAPRRAVLIA DKP
//
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