ID TPMT_PSEPF Reviewed; 217 AA. AC Q3K932; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 30. DE RecName: Full=Thiopurine S-methyltransferase; DE EC=2.1.1.67; DE AltName: Full=Thiopurine methyltransferase; GN Name=tpm; OrderedLocusNames=Pfl01_3985; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA75722.1; -; Genomic_DNA. DR RefSeq; YP_349713.1; -. DR GeneID; 3714011; -. DR GenomeReviews; CP000094_GR; Pfl01_3985. DR KEGG; pfo:Pfl01_3985; -. DR HOGENOM; Q3K932; -. DR OMA; Q3K932; PPFAVSP. DR BioCyc; PFLU205922:PFL_3985-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 1 217 Thiopurine S-methyltransferase. FT /FTId=PRO_1000047214. 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; 24762 MW; BF10193406CA7382 CRC64; MQPEFWHKKW ESNQIGFHQL EVNPYLQRHW PDLAIPVQAR VLVPLCGKSL DLLWLAGRGH QVLGVELSEK AVEDFFHEQQ LQPQVSEQGD FKVYRADAVE LWCGDFFSLT MADVAGCTAL YDRAAVIALP PAMRERYAAH LQSILPACRG LLVTLDYDQS QMPGPPFSVD DAEVQRLLGS VWRVEMLEQQ DVLGDSWKFV QAGVTRLEER VYRIRGV //