ID   TPMT_BORA1              Reviewed;         217 AA.
AC   Q2KV81;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, 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=BAV1018;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ48627.1; -; Genomic_DNA.
DR   RefSeq; YP_785541.1; -.
DR   GeneID; 6266584; -.
DR   GenomeReviews; AM167904_GR; BAV1018.
DR   KEGG; bav:BAV1018; -.
DR   NMPDR; fig|521.1.peg.2766; -.
DR   HOGENOM; Q2KV81; -.
DR   OMA; Q2KV81; 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    217       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_1000047202.
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   217 AA;  24508 MW;  119D02848A4E0515 CRC64;
     MDADFWLDRW REGKTGFHQD RVTPLLPKYW PRLALPTGAR VLVPLAGKSL DMVWLAEQGH
     EVLGVELSSL AVQQFFAEQG WAPRRWESAY GQHYAANGVE LICGDIFKLD DAALKDCLGV
     YDRAALVALP ETMRRAYANH VYGQMPAGYR GLLLTLDYPQ TQMEGPPFSV DEAEVQALFG
     EQAHLWDRRD ILEKEPKFAE RGVSRLDTLV FRLSAAS
//