ID   TPMT_SHEDO              Reviewed;         218 AA.
AC   Q12RU3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=Sden_0541;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a thiopurine = S-
CC       adenosyl-L-homocysteine + a thiopurine S-methylether.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TPMT
CC       family.
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DR   EMBL; CP000302; ABE53833.1; -; Genomic_DNA.
DR   RefSeq; YP_561556.1; -.
DR   GeneID; 4016875; -.
DR   GenomeReviews; CP000302_GR; Sden_0541.
DR   KEGG; sdn:Sden_0541; -.
DR   NMPDR; fig|318161.14.peg.523; -.
DR   HOGENOM; Q12RU3; -.
DR   OMA; Q12RU3; PPFAVSP.
DR   BioCyc; SDEN318161:SDEN_0541-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   HAMAP; MF_00812; -; 1.
DR   InterPro; IPR008854; Thiopurine_S-MeTrfase.
DR   InterPro; IPR016822; Thiopurine_S-MeTrfase_sub.
DR   Pfam; PF05724; TPMT; 1.
DR   PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    218       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_1000047219.
FT   BINDING      10     10       S-adenosyl-L-methionine (By similarity).
FT   BINDING      45     45       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING      66     66       S-adenosyl-L-methionine (By similarity).
FT   BINDING     123    123       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   218 AA;  25076 MW;  76F33423FE7CEFA7 CRC64;
     MEPNFWHDKW HQQLIGFHQA SVNALLLTHW QQLEIKPQGQ VFVPLCGKSL DMCYLAELGH
     NVLGCELNLS AVEQFYAENQ LTVTCEPIGE HQFFDCEQVQ IWQGDIFTLA PKITQDISGF
     YDRAALIAWP ESLRQAYVKQ LAKLIPQGCR GLLVTLDYPQ ETLQGPPFAV SPTWVETHLS
     EYFDITLLAC RDVLDDNPRF IKKDVPWLNE SAYLLKRK
//