ID A0A1H9WC53_9PSEU Unreviewed; 221 AA.
AC A0A1H9WC53;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=thiopurine S-methyltransferase {ECO:0000256|ARBA:ARBA00011905};
DE EC=2.1.1.67 {ECO:0000256|ARBA:ARBA00011905};
GN ORFNames=SAMN04487818_11064 {ECO:0000313|EMBL:SES31490.1};
OS Actinokineospora terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155974 {ECO:0000313|EMBL:SES31490.1, ECO:0000313|Proteomes:UP000199051};
RN [1] {ECO:0000313|EMBL:SES31490.1, ECO:0000313|Proteomes:UP000199051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44260 {ECO:0000313|EMBL:SES31490.1,
RC ECO:0000313|Proteomes:UP000199051};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000256|ARBA:ARBA00008145}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOGI01000010; SES31490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9WC53; -.
DR STRING; 155974.SAMN04487818_11064; -.
DR Proteomes; UP000199051; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR025835; Thiopurine_S-MeTrfase.
DR InterPro; IPR008854; TPMT.
DR PANTHER; PTHR10259; THIOPURINE S-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10259:SF11; THIOPURINE S-METHYLTRANSFERASE; 1.
DR Pfam; PF05724; TPMT; 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};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SES31490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199051};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SES31490.1}.
SQ SEQUENCE 221 AA; 24780 MW; 56562086856C8429 CRC64;
MFTIPRVETQ FWIDSWQEGG SKTSFHLPSV HPHARLLADR GLLDDATVLV PLCGKTADLL
FFAAHARSVV GVELVAQAID EFIAENGLSP RQPRPGVFTA GNLTILNRDL FDLAPEDIGP
VDLVYDRASL IAFPEDMRHR YVEAVTALTA PGAWYFINTL EYRPALPSPP FSVGPADVEA
YFGERFEIDH LLAEPRPEHR MVEKFGLDDL VEHGFLLRRF Q
//
