ID   TPMT_LEGPH              Reviewed;         221 AA.
AC   Q5ZRP5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=lpg2835;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU28883.1; -; Genomic_DNA.
DR   RefSeq; WP_010948522.1; NC_002942.5.
DR   RefSeq; YP_096830.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZRP5; -.
DR   SMR; Q5ZRP5; -.
DR   STRING; 272624.lpg2835; -.
DR   PaxDb; Q5ZRP5; -.
DR   EnsemblBacteria; AAU28883; AAU28883; lpg2835.
DR   GeneID; 66492006; -.
DR   KEGG; lpn:lpg2835; -.
DR   PATRIC; fig|272624.6.peg.3020; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_085515_1_0_6; -.
DR   OMA; LWCGDFF; -.
DR   Proteomes; UP000000609; 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..221
FT                   /note="Thiopurine S-methyltransferase"
FT                   /id="PRO_0000220122"
FT   BINDING         12
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
SQ   SEQUENCE   221 AA;  25383 MW;  77E830A2C150ACBB CRC64;
     MNKGQYFWNE LWCEGRISFH KEEVNPDLIA YISSLNIPAK GRVLVPLCGK SVDMLWLVRQ
     GYHVVGIELV EKAILQFVQE HQITVRENTT GQAKQYFTDN LNLWITDIFA LNAALIEPVD
     AIYDRAALVA LPKKLRPAYV DICLKWLKPG GSILLKTLQY NQEKVQGPPY SVSPEEIALS
     YQQCAKIELL KSQKRIREPN DHLFNLGISE VNDYVWRIRK G