A0A6C0WW36 · CKTCS_CAMSB
- Protein1,3,7-trimethyluric acid N-methyltransferase CkTcS
- GeneTCS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Involved in the biosynthesis of theacrine, a caffeine-like xanthine alkaloid with diverse beneficial biological activities including anti-depressive, sedative, and hypnotic activities, improving learning and memory, increasing exercise activity, and preventing nonalcoholic fatty liver disease (PubMed:32193380).
Mediates the conversion of 1,3,7-trimethyluric acid to theacrine (PubMed:32193380).
Mediates the conversion of 1,3,7-trimethyluric acid to theacrine (PubMed:32193380).
Miscellaneous
Caffeine is catabolized to produce theacrine in Camellia sinensis var. assamica cv. Kucha, but not in cv. Puer.
Catalytic activity
- 1,3,7-trimethylurate + S-adenosyl-L-methionine = theacrine + S-adenosyl-L-homocysteine + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.68 μM | 1,3,7-trimethyluric acid |
kcat is 0.01142 sec-1 with 1,3,7-trimethyluric acid as substrate.
Pathway
Alkaloid biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 24 | substrate | ||||
Sequence: Y | ||||||
Binding site | 27-31 | substrate | ||||
Sequence: NSSFT | ||||||
Binding site | 66 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 66-67 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GC | ||||||
Binding site | 67 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 72 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 102-105 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: MNDL | ||||||
Binding site | 139-141 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SFH | ||||||
Site | 154 | Involved in substrate discrimination | ||||
Sequence: H | ||||||
Binding site | 156-158 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SYS | ||||||
Binding site | 157-161 | substrate | ||||
Sequence: YSVHW | ||||||
Binding site | 178 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 226 | Involved in substrate discrimination | ||||
Sequence: R | ||||||
Binding site | 264 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 266 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 267 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 270 | Involved in substrate discrimination | ||||
Sequence: C | ||||||
Site | 318 | Involved in substrate discrimination | ||||
Sequence: I | ||||||
Site | 333 | Involved in substrate discrimination | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | S-adenosylmethionine-dependent methyltransferase activity | |
Biological Process | alkaloid metabolic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name1,3,7-trimethyluric acid N-methyltransferase CkTcS
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Theaceae > Camellia
Accessions
- Primary accessionA0A6C0WW36
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451802 | 1-370 | 1,3,7-trimethyluric acid N-methyltransferase CkTcS | |||
Sequence: MELATRGKVKEVLFMNTGEGESSYVQNSSFTEKVASMAMPALENAVETLFSKDFHLFQAINAADLGCATGPNTFAVISTIKRMMEKKCRELNCQTLELQVYMNDLFGNDFNTLFKGLSSKVIGNKCEEVSCYVMGVPGSFHGRLFPRNSLHLVHSSYSVHWLTQAPKGLTSREGLALNKGRIYISKTSPPVVREAYLSQFHEDFTMFLNARSQEVVPNGCMVLILRGRQSSDPSDMQSCFIWELLAIAIAELVSQGLIDEDKLDTFNIPCYFPSLEEVKDIVERDGSFTIDHMEGFELDSLQMQENDKWVRGEKFAKIVRAFTEPIISNQFGHEIMDKLYDKFTHIVVSDLEAKLPKTTSIILVLSKIVG |
Expression
Tissue specificity
Expressed in leaves of cv. Kucha, but not in cv. Puer.
Structure
Family & Domains
Sequence similarities
Belongs to the methyltransferase superfamily. Type-7 methyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length370
- Mass (Da)41,606
- Last updated2020-06-17 v1
- Checksum49C72A7198F3C45B
Keywords
- Technical term