ID A0A0B4CMH6_9RHOB Unreviewed; 213 AA.
AC A0A0B4CMH6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=RA20_20250 {ECO:0000313|EMBL:KIC14669.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC14669.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIC14669.1}.
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DR EMBL; JWLD01000069; KIC14669.1; -; Genomic_DNA.
DR RefSeq; WP_039132934.1; NZ_JWLD01000069.1.
DR AlphaFoldDB; A0A0B4CMH6; -.
DR STRING; 1577896.RA20_20250; -.
DR OrthoDB; 9778208at2; -.
DR Proteomes; UP000031177; Unassembled WGS sequence.
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 213 AA; 23368 MW; 4D30702508F2758E CRC64;
MEQEFWQARW RENRIGFHEP APNTLLTKHF SRLGLEAGQS VFVPLCGKAL DLDWLLKQGL
RVTGAEFNQG AVEQVFARQG LEPEIENQGD LLRYQAGALT LFAGDFFALT AAQAGPVDAV
YDRAALVAVK PGDRTAYAAH LNRTTSTARQ LLIGFDYDQS LMEGPPFSVP GGLVQTLYQG
THAITLAEER PADGRIGERC NALEQAWLLS PLA
//