ID   TPMT_SHESM              Reviewed;         218 AA.
AC   Q0HMQ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=Shewmr4_0581;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000446; ABI37661.1; -; Genomic_DNA.
DR   RefSeq; YP_732718.1; -.
DR   GeneID; 4251704; -.
DR   GenomeReviews; CP000446_GR; Shewmr4_0581.
DR   KEGG; she:Shewmr4_0581; -.
DR   HOGENOM; Q0HMQ6; -.
DR   OMA; Q0HMQ6; PPFAVSP.
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_1000047224.
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;  24898 MW;  A400F49947800465 CRC64;
     MEPGFWHEKW QQQLIGFHQQ DINPFLVKYW QTLALPADAK VFVPLCGKSL DMCFLAEQGH
     QVIGCELNEL AVQQFFEENQ LPMNQSAEGE HQHYQTEQVS LYQGDIFTLP QSITAQVNGF
     YDRAALIAWP ESMRTQYAKQ LAQLLPSGSV GLLVTLDYPQ ETLSGPPFAV SPTWVETHLS
     DDFEIQALAC QDVLADNPRF VKKEVPWLNE AVYLLRRK
//