ID   TPMT_XANAC              Reviewed;         218 AA.
AC   Q8PMI8;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=XAC1439;
OS   Xanthomonas axonopodis pv. citri (Citrus canker).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=92829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE011776; AAM36310.1; -; Genomic_DNA.
DR   RefSeq; NP_641774.1; -.
DR   HSSP; O86262; 1PJZ.
DR   GeneID; 1155510; -.
DR   GenomeReviews; AE008923_GR; XAC1439.
DR   KEGG; xac:XAC1439; -.
DR   NMPDR; fig|190486.1.peg.1418; -.
DR   HOGENOM; Q8PMI8; -.
DR   OMA; Q8PMI8; PPFAVSP.
DR   BioCyc; XAXO190486:XAC1439-MON; -.
DR   BRENDA; 2.1.1.67; 289771.
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_0000220138.
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;  24607 MW;  E42AF9AC12211124 CRC64;
     MDTNFWLERW QLGHTGFHQQ EVLPLLQKHW HALDLPKESR VLVPLCGKTL DMHWLASQGH
     RVLGVELSPL AVTQFFDEAG LQPQRHTSAA GEHFIAGPIE IICGDAFALD ASVLADCTAV
     YDRAALVALP AELRQRYLQT VYVQLPTHCR GLLITLEYPQ AEKAGPPFSV DATHVHALFD
     AAWQVDQLER RDILDQEPRF RDEGVTGLST AVYRLQRR
//