ID   TPMT_XANVE              Reviewed;         213 AA.
AC   A7IIX3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-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=Xaut_2726;
OS   Xanthobacter versatilis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / DSM 118458 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
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; CP000781; ABS67966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7IIX3; -.
DR   SMR; A7IIX3; -.
DR   STRING; 78245.Xaut_2726; -.
DR   KEGG; xau:Xaut_2726; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_085515_1_0_5; -.
DR   OrthoDB; 9778208at2; -.
DR   PhylomeDB; A7IIX3; -.
DR   Proteomes; UP000002417; 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: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; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..213
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_1000134083"
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         46
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
SQ   SEQUENCE   213 AA;  23278 MW;  6A8A9F92D73CC261 CRC64;
     MEPDFWHARW QTKQIQGFHE GKANAFLVKH FPRLPVAPGA RVFVPLCGKT RDIAWLLGEG
     FRVAGAELSR IAVEELFAEL GVVPEVTTQG AHTRFSAPGL DIFQGDIFAL TPDTLGPVDA
     VWDRAALVAL PKDMRARYAP HLVALTDTAP QLLVCFEYDQ PLLAGPPFSV PPEETRTLYG
     ADYVVAAIDT APVPGGLKGQ CEAVEHVWLL ERA
//