TPMT_PSESJ
ID TPMT_PSESJ Reviewed; 218 AA.
AC O86262;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Tellurite-resistance determinant;
DE Short=TEL-R determinant;
DE AltName: Full=Thiopurine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812};
GN Name=tpm {ECO:0000255|HAMAP-Rule:MF_00812};
OS Pseudomonas syringae pv. pisi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=59510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9565678; DOI=10.1016/s0167-4781(98)00020-7;
RA Cournoyer B., Watanabe S., Vivian A.;
RT "A tellurite-resistance genetic determinant from phytopathogenic
RT pseudomonads encodes a thiopurine methyltransferase: evidence of a widely-
RT conserved family of methyltransferases.";
RL Biochim. Biophys. Acta 1397:161-168(1998).
RN [2]
RP STRUCTURE BY NMR OF 18-218.
RX PubMed=14556746; DOI=10.1016/j.jmb.2003.08.039;
RA Scheuermann T.H., Lolis E., Hodsdon M.E.;
RT "Tertiary structure of thiopurine methyltransferase from Pseudomonas
RT syringae, a bacterial orthologue of a polymorphic, drug-metabolizing
RT enzyme.";
RL J. Mol. Biol. 333:573-585(2003).
CC -!- FUNCTION: Involved in the biological cycling of tellurium and selenium.
CC Tellurium resistance (Ter) mechanism.
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.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000255|HAMAP-Rule:MF_00812}.
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DR EMBL; L49178; AAC27664.1; -; Genomic_DNA.
DR PDB; 1PJZ; NMR; -; A=18-218.
DR PDBsum; 1PJZ; -.
DR AlphaFoldDB; O86262; -.
DR BMRB; O86262; -.
DR SMR; O86262; -.
DR EvolutionaryTrace; O86262; -.
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 GO; GO:0046690; P:response to tellurium ion; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 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 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Tellurium resistance; Transferase.
FT CHAIN 1..218
FT /note="Thiopurine S-methyltransferase"
FT /id="PRO_0000220129"
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"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1PJZ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:1PJZ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1PJZ"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1PJZ"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1PJZ"
SQ SEQUENCE 218 AA; 24446 MW; 5CD188EA5F9D171F CRC64;
MKADFWLQRW SAGQIGFHQS EVNKDLQQYW SSLNVVPGAR VLVPLCGKSQ DMSWLSGQGY
HVVGAELSEA AVERYFTERG EQPHITSQGD FKVYAAPGIE IWCGDFFALT ARDIGHCAAF
YDRAAMIALP ADMRERYVQH LEALMPQACS GLLITLEYDQ ALLEGPPFSV PQTWLHRVMS
GNWEVTKVGG QDTLHSSARG LKAGLERMDE HVYVLERV
