ID   TPMT_DANRE              Reviewed;         232 AA.
AC   Q504A5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable thiopurine S-methyltransferase;
DE            Short=Thiopurine methyltransferase;
DE            EC=2.1.1.67;
GN   Name=tpmt; ORFNames=zgc:109981;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) 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:0000250|UniProtKB:P51580};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TPMT family. {ECO:0000305}.
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DR   EMBL; BC095104; AAH95104.1; -; mRNA.
DR   AlphaFoldDB; Q504A5; -.
DR   SMR; Q504A5; -.
DR   STRING; 7955.ENSDARP00000072844; -.
DR   PaxDb; Q504A5; -.
DR   ZFIN; ZDB-GENE-050522-141; tpmt.1.
DR   eggNOG; ENOG502QSF5; Eukaryota.
DR   InParanoid; Q504A5; -.
DR   Reactome; R-DRE-156581; Methylation.
DR   Reactome; R-DRE-9748787; Azathioprine ADME.
DR   PRO; PR:Q504A5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008119; F:thiopurine S-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; 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; 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   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..232
FT                   /note="Probable thiopurine S-methyltransferase"
FT                   /id="PRO_0000284920"
FT   BINDING         14..25
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   232 AA;  26334 MW;  0EC5EF8310112559 CRC64;
     MSAQADRVMD LSEWENRWQE GRTGFHRSDV HNLLKANVDK LICGRREVRF FFPLCGKAVD
     MKWLADMGHT VVGVEFSEKG IKEFSQEQNL EYNEEAVADI PGAKLFKSTD GKISIYQCDL
     YKFSSAVAGH FGGIWDRGAL VAINPCDRQK YASLLVSLMS SDCRYLLDTL EYNPELYKGP
     PFFVSEDDIK TVFGGSCNID LLQSVDGFEE KHRSWGLDSL TEKLYLLTTK TQ