TPMT_PSEU5
ID TPMT_PSEU5 Reviewed; 235 AA.
AC Q93JT2; A4VJ56;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Thiopurine S-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812};
DE EC=2.1.1.67 {ECO:0000255|HAMAP-Rule:MF_00812};
DE AltName: Full=Thiopurine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00812};
GN Name=tpm {ECO:0000255|HAMAP-Rule:MF_00812}; Synonyms=tmpA;
GN OrderedLocusNames=PST_1312;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12904565; DOI=10.1099/mic.0.26270-0;
RA Desnoues N., Lin M., Guo X., Ma L., Carreno-Lopez R., Elmerich C.;
RT "Nitrogen fixation genetics and regulation in a Pseudomonas stutzeri strain
RT associated with rice.";
RL Microbiology 149:2251-2262(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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:0000255|HAMAP-Rule:MF_00812};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00812}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000255|HAMAP-Rule:MF_00812}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC44176.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ297529; CAC44176.3; ALT_INIT; Genomic_DNA.
DR EMBL; CP000304; ABP79007.1; -; Genomic_DNA.
DR RefSeq; WP_011912491.1; NC_009434.1.
DR AlphaFoldDB; Q93JT2; -.
DR SMR; Q93JT2; -.
DR STRING; 379731.PST_1312; -.
DR EnsemblBacteria; ABP79007; ABP79007; PST_1312.
DR KEGG; psa:PST_1312; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_085515_1_0_6; -.
DR OMA; ELWIREF; -.
DR Proteomes; UP000000233; 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 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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..235
FT /note="Thiopurine S-methyltransferase"
FT /id="PRO_0000220131"
FT REGION 199..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT BINDING 48
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00812"
SQ SEQUENCE 235 AA; 26502 MW; 410021AD19465711 CRC64;
MTDHDNQRWL QLWRERRTDF HQHGVNLLLS RFWPAFAPAT PSRVFVPLCG KSLDMLWLAE
QGHDVIGVEL SPLAIEAFFR ENHLPPSKRR QGRFTLWRHG RIGILCGDYF ALSEADLGPV
DSVYDRAALT ALPPILRSRY VAQLRRIVPD TARVFLLTLE DAEADATLQQ ALGVDEELAA
LYTAGFEIAL AHVESLFEPD PQNGAPRRVE HKVYQLTGKR PASPEADGRA AETED