General rule information
[?]
Accession |
PRU00918 |
Dates |
25-NOV-2011 (Created) 14-MAY-2022 (Last updated, Version 12) |
Predictors |
PROSITE; PS51585; SAM_MT_TPMT
|
Name |
Thiopurine or thiol or thiocyanate S-methyltransferase (TPMT). |
Function |
Thiol S-methyltransferase (EC 2.1.1.9) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to a thiol to form a thioether and S-adenosyl-L-homocysteine. Thiocyanate S-methyltransferase (EC 2.1.1.n4) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to thiocyanate to form methyl thiocyanate and S-adenosyl-L-homocysteine. Thiopurine S-methyltransferase (EC 2.1.1.67) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to a thiopurine to form methyl a thiopurine S-methylether and S-adenosyl-L-homocysteine. |
Propagated annotation
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Similarity |
Belongs to the class I-like SAM-binding methyltransferase superfamily. TPMT family. |
GO:0008172; Molecular function: S-methyltransferase activity.
GO:0008757; Molecular function: S-adenosylmethionine-dependent methyltransferase activity.
GO:0032259; Biological process: methylation.
From: PS51585 |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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BINDING
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70
|
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70
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/ligand="S-adenosyl-L-methionine" /ligand_id="59789
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W
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BINDING
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125
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125
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/ligand="S-adenosyl-L-methionine" /ligand_id="59789
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D
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Additional information
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Size range |
unlimited amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
Q6AWU6 (HOL3_ARATH) |
Scope |
Eukaryota; Brassicaceae |
Comments |
None |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see
prosite_license.html.
UniProtKB rule member sequences
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