ID A0A1P8UK78_9GAMM Unreviewed; 219 AA.
AC A0A1P8UK78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Thiopurine S-methyltransferase {ECO:0000256|ARBA:ARBA00011905, ECO:0000256|HAMAP-Rule:MF_00812};
DE EC=2.1.1.67 {ECO:0000256|ARBA:ARBA00011905, ECO:0000256|HAMAP-Rule:MF_00812};
DE AltName: Full=Thiopurine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00812};
GN Name=tpm {ECO:0000256|HAMAP-Rule:MF_00812};
GN ORFNames=BW247_14830 {ECO:0000313|EMBL:APZ44204.1};
OS Acidihalobacter ferrooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ44204.1, ECO:0000313|Proteomes:UP000243807};
RN [1] {ECO:0000313|EMBL:APZ44204.1, ECO:0000313|Proteomes:UP000243807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V8 {ECO:0000313|EMBL:APZ44204.1,
RC ECO:0000313|Proteomes:UP000243807};
RA Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA Watkin E.L.J.;
RT "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT V8).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000903, ECO:0000256|HAMAP-
CC Rule:MF_00812};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00812}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000256|ARBA:ARBA00008145,
CC ECO:0000256|HAMAP-Rule:MF_00812}.
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DR EMBL; CP019434; APZ44204.1; -; Genomic_DNA.
DR RefSeq; WP_076837827.1; NZ_CP019434.1.
DR AlphaFoldDB; A0A1P8UK78; -.
DR STRING; 1765967.BW247_14830; -.
DR OrthoDB; 9778208at2; -.
DR Proteomes; UP000243807; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00812};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00812}; Reference proteome {ECO:0000313|Proteomes:UP000243807};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00812};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00812}.
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00812"
SQ SEQUENCE 219 AA; 24811 MW; C4D8CA5CE2703B23 CRC64;
MTPDFWLQRW QENRIGFHQS QINTHLETHW PTLGAAPGGT VFVPLCGKSL DMLWLAGQGY
RVRGVELSEI AVQSFFTENG LTPDIEPSGA FMRYRHGEIE ILCGDLFDLR PADLADVTAV
YDRASLIALP PEMRGRYAQH KRALLPDRPP VLLVTLDYPQ TERQGPPFAV SDAEVRNLYA
DAWTVERVAS VDLRTAGQHT DLSRFEEHVF ILRSQQPRT
//
