ID   TPMT_SHEFN              Reviewed;         219 AA.
AC   Q07XD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Sfri_3498;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI73326.1; -; Genomic_DNA.
DR   RefSeq; WP_011638917.1; NC_008345.1.
DR   AlphaFoldDB; Q07XD8; -.
DR   SMR; Q07XD8; -.
DR   STRING; 318167.Sfri_3498; -.
DR   EnsemblBacteria; ABI73326; ABI73326; Sfri_3498.
DR   KEGG; sfr:Sfri_3498; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_085515_1_0_6; -.
DR   OMA; LWCGDFF; -.
DR   OrthoDB; 2049098at2; -.
DR   Proteomes; UP000000684; Chromosome.
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; -; 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   Pfam; PF05724; TPMT; 1.
DR   PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR03840; TMPT_Se_Te; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..219
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_1000047220"
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   219 AA;  25239 MW;  3A6031EFEB18E3A5 CRC64;
     MEPSFWHEKW QLQQIGFHQN QVNPFLVKYW SHIGLNENTE VFVPLCGKSL DMFYLAEQRH
     TVLGCELNTL AVEQFFTDNG LTYQVNHTDE HVVFSTDQVT LYQGDIFTLP KSATASISGF
     YDRAALIAWP EEMRQQYVKA LAALIPANVS GLLITLDYLQ ETLKGPPFAV SPRWVESYLT
     PYFDVELLEC VDVLADNPRF MNKHVPWLNE AVYKLTRKS