ID   TPMT_SHEB8              Reviewed;         218 AA.
AC   A6WSW9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   04-NOV-2026, entry version 84.
DE   RecName: Full=Thiopurine S-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812};
DE            EC=2.1.1.67 {ECO:0000255|HAMAP-Rule:MF_00812};
DE   AltName: Full=Thiopurine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812};
GN   Name=tpm {ECO:0000255|HAMAP-Rule:MF_00812};
GN   OrderedLocusNames=Shew185_3784;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00812};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00812}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000255|HAMAP-Rule:MF_00812}.
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DR   EMBL; CP000753; ABS09908.1; -; Genomic_DNA.
DR   RefSeq; WP_012090264.1; NC_009665.1.
DR   AlphaFoldDB; A6WSW9; -.
DR   SMR; A6WSW9; -.
DR   KEGG; sbm:Shew185_3784; -.
DR   HOGENOM; CLU_085515_1_0_6; -.
DR   OMA; AAFWHDK; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010038; P:response to metal ion; IEA:InterPro.
DR   FunFam; 3.40.50.150:FF:000101; Thiopurine S-methyltransferase; 1.
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; NF009732; PRK13255.1; 1.
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; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..218
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_1000047218"
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
SQ   SEQUENCE   218 AA;  24814 MW;  48026E6D6A123016 CRC64;
     MEPGFWHEKW HQQQIGFHQQ DINPFLVKYW QQLGLPADTQ VFVPLCGKSL DMCFLAEQGH
     QVIGCELNEL AVQHFFSDNQ LEMTQTTVGE HQHYHTEQIS LYQGDIFTLP KTITQAVTAF
     YDRAALIAWP ESMRAQYAKQ LASLLPSGSV GLLVTLDYPQ EALSGPPFAV SPTWVEQHLS
     DDFDIEVLAS QDVLADNPRF IKKAVPWLNE AAYLLKRK
//