ID TPMT_MARN8 Reviewed; 219 AA. AC A1U560; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 13-SEP-2023, entry version 83. 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}; OrderedLocusNames=Maqu_3055; OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter OS aquaeolei). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Marinobacteraceae; Marinobacter. OX NCBI_TaxID=351348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8; RX PubMed=21335390; DOI=10.1128/aem.01866-10; RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A., RA Edwards K.J.; RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical RT 'opportunitroph'."; RL Appl. Environ. Microbiol. 77:2763-2771(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L- CC homocysteine + a thiopurine S-methylether.; EC=2.1.1.67; CC Evidence={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 methyltransferase CC superfamily. TPMT family. {ECO:0000255|HAMAP-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 AlphaFoldDB; A1U560; -. DR SMR; A1U560; -. DR STRING; 351348.Maqu_3055; -. DR EnsemblBacteria; ABM20129; ABM20129; Maqu_3055. DR GeneID; 31822364; -. DR KEGG; maq:Maqu_3055; -. DR eggNOG; COG0500; Bacteria. DR HOGENOM; CLU_085515_1_0_6; -. DR OMA; LWCGDFF; -. DR OrthoDB; 9778208at2; -. DR Proteomes; UP000000998; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0010038; P:response to metal ion; IEA:InterPro. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00812; Thiopur_methtran; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR022474; Thiopur_S-MeTfrase_Se/Te_detox. DR InterPro; IPR025835; Thiopurine_S-MeTrfase. DR InterPro; IPR008854; TPMT. DR NCBIfam; TIGR03840; TMPT_Se_Te; 1. DR PANTHER; PTHR10259; THIOPURINE S-METHYLTRANSFERASE; 1. DR PANTHER; PTHR10259:SF11; THIOPURINE S-METHYLTRANSFERASE; 1. DR Pfam; PF05724; TPMT; 1. DR PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51585; SAM_MT_TPMT; 1. PE 3: Inferred from homology; KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..219 FT /note="Thiopurine S-methyltransferase" FT /id="PRO_1000047206" FT BINDING 10 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812" FT BINDING 45 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812" FT BINDING 66 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812" FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="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 //