ID K6YLH5_9ALTE Unreviewed; 210 AA.
AC K6YLH5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:GAC17483.1};
GN ORFNames=GARC_0502 {ECO:0000313|EMBL:GAC17483.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC17483.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC17483.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC17483.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC17483.1}.
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DR EMBL; BAEO01000007; GAC17483.1; -; Genomic_DNA.
DR RefSeq; WP_007616315.1; NZ_BAEO01000007.1.
DR AlphaFoldDB; K6YLH5; -.
DR STRING; 493475.GARC_0502; -.
DR eggNOG; COG0500; Bacteria.
DR OrthoDB; 9778208at2; -.
DR Proteomes; UP000006327; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006327};
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 210 AA; 23735 MW; 107EC0BA06C6E070 CRC64;
MKESYWHQKW ADNDIAFHEN DGNPLLKKHV SLLNLAISSR VFIPLCGKTL DIAWLLSKGY
QVVGAELSQF AVQELFKNLG IEPNVSKNGK FDHYQAVNLD IFVGDIFNLS TDIIGSVDAI
YDRAALVALP VELRNKYTHH LIEITNKAPQ LLICFEYDQS VMAGPPFSIK HENIQQYYSP
DYAIKFIERK NVTGGIKGQT PGNEAVWLLQ
//
