ID A0A1Q2M4Z3_9GAMM Unreviewed; 210 AA.
AC A0A1Q2M4Z3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=Mag101_09120 {ECO:0000313|EMBL:AQQ67784.1};
OS Microbulbifer agarilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ67784.1, ECO:0000313|Proteomes:UP000188219};
RN [1] {ECO:0000313|EMBL:AQQ67784.1, ECO:0000313|Proteomes:UP000188219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP101 {ECO:0000313|EMBL:AQQ67784.1,
RC ECO:0000313|Proteomes:UP000188219};
RA Jung J., Bae S.S., Baek K.;
RT "Genome of Microbulbifer agarilyticus GP101.";
RL Submitted (FEB-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; CP019650; AQQ67784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2M4Z3; -.
DR STRING; 260552.Mag101_09120; -.
DR KEGG; maga:Mag101_09120; -.
DR OrthoDB; 9778208at2; -.
DR Proteomes; UP000188219; 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:UP000188219};
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 210 AA; 23216 MW; 1668A0BFFFA0D1BD CRC64;
MEHKFWLDKW HKNEIGFHNP DAHPLLVEHL DALRLSAGAR IFLPLCGKTL DIAWLLQHGY
RVVGAELSEV AIQQLFAQLD VDPQVAKVGN AKLYSTGQLE VFVGDFFELT RDALGSIDAV
YDRAALVALP EAMRTAYAAH LIALTEGADQ LLLAIDYDQS QLPGPPFCVD AAEVHRLYDS
AYKTEQLGSA EIDGGLKGKV PAREVVWLLR
//
