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Database: UniProt
Entry: A0A0U3L3C6_9BURK
LinkDB: A0A0U3L3C6_9BURK
Original site: A0A0U3L3C6_9BURK 
ID   A0A0U3L3C6_9BURK        Unreviewed;       219 AA.
AC   A0A0U3L3C6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ECO:0000313|EMBL:ALU90924.1};
GN   ORFNames=Hrubri_3767 {ECO:0000313|EMBL:ALU90924.1};
OS   Herbaspirillum rubrisubalbicans M1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU90924.1, ECO:0000313|Proteomes:UP000069903};
RN   [1] {ECO:0000313|EMBL:ALU90924.1, ECO:0000313|Proteomes:UP000069903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1 {ECO:0000313|EMBL:ALU90924.1,
RC   ECO:0000313|Proteomes:UP000069903};
RA   Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA   Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA   Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT   "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL   Submitted (DEC-2015) 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; CP013737; ALU90924.1; -; Genomic_DNA.
DR   RefSeq; WP_058896641.1; NZ_CP013737.1.
DR   AlphaFoldDB; A0A0U3L3C6; -.
DR   STRING; 1078773.Hrubri_3767; -.
DR   KEGG; hrb:Hrubri_3767; -.
DR   OrthoDB; 9778208at2; -.
DR   Proteomes; UP000069903; 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};
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;  24739 MW;  A85947F59CAE4573 CRC64;
     MEAQFWLERW REGRTHFHQS RVTPLLQKYW PQLGLPRGST VLVPLCGKSL DMLWLAQQGH
     RVLGVELSEL AITQFFSEHQ LTPAIHESAQ GRHYVAGNIE LICGDIFALE DATLAACAGA
     YDRAALIALP PPMRADYVTQ TYGRLPAQAR SLLITLEYDQ QKMDGPPFSV AEEEVLRLYA
     AHSEAVAIDR RDILEKEPKF LERGLTALET AVYRLQRQA
//
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