ID   TPMT_XANC8              Reviewed;         218 AA.
AC   Q4UST1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=XC_2843;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY49892.1; -; Genomic_DNA.
DR   RefSeq; YP_243912.1; -.
DR   GeneID; 3381377; -.
DR   GenomeReviews; CP000050_GR; XC_2843.
DR   KEGG; xcb:XC_2843; -.
DR   HOGENOM; Q4UST1; -.
DR   OMA; Q4UST1; PPFAVSP.
DR   BioCyc; XCAM314565:XC_2843-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_1000047229.
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;  24228 MW;  887F06E595ABF197 CRC64;
     MDTDFWLQRW QDGQTGFHQD EVMPLLQKHW PALQLPAHAR VLVPLCGKTL DLHWLAAQGH
     RVLGVEISPL AVTQFFDDAG LQPQRHTSRA GEHCIAGPIE IICGDAFTLD ASVLGDCTAV
     YDRAALVALP AALRQRYLET VYARLPAGCR GLLITLDYPQ AEKAGPPFSV DAAEVHALFG
     TQWKVQELEH RDILDQEPRF RADGVTALST GVYRLQRD
//