ID TPMT_MARHV Reviewed; 219 AA. AC A1U560; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 22-JUL-2015, entry version 50. DE RecName: Full=Thiopurine S-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812}; DE EC=2.1.1.67 {ECO:0000255|HAMAP-Rule:MF_00812}; DE AltName: Full=Thiopurine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812}; GN Name=tpm {ECO:0000255|HAMAP-Rule:MF_00812}; GN OrderedLocusNames=Maqu_3055; OS Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / OS VT8). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=351348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Edwards K., Richardson P.; RT "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."; RL Submitted (DEC-2006) 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 {ECO:0000255|HAMAP-Rule:MF_00812}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00812}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TPMT family. {ECO:0000255|HAMAP- CC Rule:MF_00812}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000514; ABM20129.1; -; Genomic_DNA. DR RefSeq; WP_011786497.1; NC_008740.1. DR ProteinModelPortal; A1U560; -. DR STRING; 351348.Maqu_3055; -. DR EnsemblBacteria; ABM20129; ABM20129; Maqu_3055. DR KEGG; maq:Maqu_3055; -. DR PATRIC; 22461466; VBIMarAqu65105_3475. DR eggNOG; COG0500; -. DR HOGENOM; HOG000276919; -. DR KO; K00569; -. DR OrthoDB; EOG6K3ZZV; -. DR BioCyc; MHYD351348:GHYZ-3114-MONOMER; -. DR Proteomes; UP000000998; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010038; P:response to metal ion; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00812; Thiopur_methtran; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR022474; Thiopur_S-MeTfrase_Se/Te_detox. DR InterPro; IPR025835; Thiopurine_S-MeTrfase. DR InterPro; IPR008854; TPMT. DR Pfam; PF05724; TPMT; 1. DR PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR03840; TMPT_Se_Te; 1. DR PROSITE; PS51585; SAM_MT_TPMT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 219 Thiopurine S-methyltransferase. FT /FTId=PRO_1000047206. FT BINDING 10 10 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00812}. FT BINDING 45 45 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00812}. FT BINDING 66 66 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00812}. FT BINDING 123 123 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00812}. SQ SEQUENCE 219 AA; 25493 MW; 370A45E003976AF0 CRC64; MEHEFWHERW AKDQIGFHEG TVNQYLHDHW PELAGNGTDA VFVPLCGKAH DMWWLHDRGH PIIGVELSEV ACKDFFEEAQ EKASVHPGEP FTTFRHDDLQ IWCGDYFQLV PDDLKHIRLV YDRAALIALP PEMRKSYVNH LTAIIPDDTR ILLITLDYDS SEMQGPPFNV TDDEVFRLYG EDYEINQVLK RDMARDNPFA KRRGLRNGAT ESVFTLVKK //