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Entry: A0A0L1JQW4_9RHOB
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ID   A0A0L1JQW4_9RHOB        Unreviewed;       220 AA.
AC   A0A0L1JQW4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Thiopurine S-methyltransferase {ECO:0000256|ARBA:ARBA00011905, ECO:0000256|HAMAP-Rule:MF_00812};
DE            EC=2.1.1.67 {ECO:0000256|ARBA:ARBA00011905, ECO:0000256|HAMAP-Rule:MF_00812};
DE   AltName: Full=Thiopurine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00812};
GN   Name=tpm {ECO:0000256|HAMAP-Rule:MF_00812};
GN   ORFNames=ATO11_07615 {ECO:0000313|EMBL:KNG94102.1};
OS   Pseudaestuariivita atlantica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudaestuariivita.
OX   NCBI_TaxID=1317121 {ECO:0000313|EMBL:KNG94102.1, ECO:0000313|Proteomes:UP000036938};
RN   [1] {ECO:0000313|EMBL:KNG94102.1, ECO:0000313|Proteomes:UP000036938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S11-z3 {ECO:0000313|EMBL:KNG94102.1,
RC   ECO:0000313|Proteomes:UP000036938};
RA   Li G., Lai Q., Du Y., Liu X., Sun F., Shao Z.;
RT   "Aestuariivita atlantica sp. nov., isolated from deep sea sediment of the
RT   Atlantic Ocean.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-
CC         homocysteine + a thiopurine S-methylether.; EC=2.1.1.67;
CC         Evidence={ECO:0000256|ARBA:ARBA00000903, ECO:0000256|HAMAP-
CC         Rule:MF_00812};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00812}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000256|ARBA:ARBA00008145,
CC       ECO:0000256|HAMAP-Rule:MF_00812}.
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:KNG94102.1}.
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DR   EMBL; AQQZ01000003; KNG94102.1; -; Genomic_DNA.
DR   RefSeq; WP_050530247.1; NZ_AQQZ01000003.1.
DR   AlphaFoldDB; A0A0L1JQW4; -.
DR   STRING; 1317121.ATO11_07615; -.
DR   PATRIC; fig|1317121.7.peg.2130; -.
DR   OrthoDB; 9778208at2; -.
DR   Proteomes; UP000036938; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0010038; P:response to metal ion; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00812; Thiopur_methtran; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR022474; Thiopur_S-MeTfrase_Se/Te_detox.
DR   InterPro; IPR025835; Thiopurine_S-MeTrfase.
DR   InterPro; IPR008854; TPMT.
DR   NCBIfam; TIGR03840; TMPT_Se_Te; 1.
DR   PANTHER; PTHR10259; THIOPURINE S-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10259:SF11; THIOPURINE S-METHYLTRANSFERASE; 1.
DR   Pfam; PF05724; TPMT; 1.
DR   PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00812};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00812}; Reference proteome {ECO:0000313|Proteomes:UP000036938};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00812};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00812}.
FT   BINDING         18
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
SQ   SEQUENCE   220 AA;  24010 MW;  017DB0F4A3061195 CRC64;
     MTEKAKRTND PTQWHDRWRD GRIGFHQPEG NPLLRRHLPA LGLPRGARLF LPLCGKTGDI
     GWLMSQGFAV AGSELSRIAV DALFDDLGME PEVADHGPLT RMSGPGVDIW VGDMFDLTPA
     LLGPVDAVYD RAALVALPDD IRAVYAPHLA AITANAPHLL ITFDYDASTV SGPPFPVWQD
     EISALYVETH DVALLEDAEA KGGIKGVTPA REQVWHLIPR
//
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