ID   TPMT_PSEF5              Reviewed;         222 AA.
AC   Q4K8U2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=PFL_4249;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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; CP000076; AAY93505.1; -; Genomic_DNA.
DR   RefSeq; YP_261341.1; -.
DR   GeneID; 3477375; -.
DR   GenomeReviews; CP000076_GR; PFL_4249.
DR   KEGG; pfl:PFL_4249; -.
DR   NMPDR; fig|220664.3.peg.6061; -.
DR   HOGENOM; Q4K8U2; -.
DR   OMA; Q4K8U2; PPFAVSP.
DR   BioCyc; PFLU220664:PFL_4249-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    222       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_0000220127.
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   222 AA;  25217 MW;  6F44DDDC028B27EE CRC64;
     MQADFWQKRW ERDQIGFHLA EVNPYLQQYW PALGLAAQSR VLVPLCGKSL DLIWLADQGF
     EVLGIELAEK AVEDFFREHQ LQPQISQHGV FKVYAHGPIE LWCGDFFALT AEDTADCTAL
     YDRAAMIALP SPMRQRYAAH LNGLLPNGSK GLLITMDYAQ EQLDGPPFAV LDDEVRQRLG
     GVWQLQVETE RDILGESWKF LQGGVTRLVE RVYRLSKQGA AR
//