ID   TPMT_VIBF1              Reviewed;         213 AA.
AC   Q5E4N9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Thiopurine S-methyltransferase;
DE            EC=2.1.1.67;
DE   AltName: Full=Thiopurine methyltransferase;
GN   Name=tpm; OrderedLocusNames=VF_1512;
OS   Vibrio fischeri (strain ATCC 700601 / ES114).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT   with pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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; CP000020; AAW86007.1; -; Genomic_DNA.
DR   RefSeq; YP_204895.1; -.
DR   GeneID; 3278795; -.
DR   GenomeReviews; CP000020_GR; VF_1512.
DR   KEGG; vfi:VF_1512; -.
DR   NMPDR; fig|312309.3.peg.1512; -.
DR   HOGENOM; Q5E4N9; -.
DR   OMA; Q5E4N9; PPFAVSP.
DR   BioCyc; VFIS312309:VF1512-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    213       Thiopurine S-methyltransferase.
FT                                /FTId=PRO_0000220134.
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     121    121       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   213 AA;  24538 MW;  057A64451F42851C CRC64;
     MEHEFWQKKW ASNVIGFHLP DTNPILTQYW SALEPKRNET VFVPLCGKSM DLDWLAERHN
     SVTGVELSQI AVRAFFAERL YTPTVTQLSS TLELYEFDEF TIYSGDYFVA PIEAADLIYD
     RAALVALPKE MREEYVQVLR SRLKEGGRIL LVTLDYDQNE MAGPPFSVPE NEVQALFSGM
     KITRLQRDEA DAEHPKIKKG LSRFAEEVWL IES
//