TCS1D_CAMTA
ID TCS1D_CAMTA Reviewed; 369 AA.
AC A0A0S2PMA8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Caffeine synthase 1 {ECO:0000303|PubMed:26773541};
DE Short=TCS1d {ECO:0000303|PubMed:26773541};
DE EC=2.1.1.160 {ECO:0000269|PubMed:26773541};
GN Name=TCS1D {ECO:0000303|PubMed:26773541};
OS Camellia taliensis (Wild tea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=182317;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hoefler B.C., Straight P.D.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, MUTAGENESIS OF CYS-269, CATALYTIC ACTIVITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=26773541; DOI=10.1016/j.plaphy.2015.12.020;
RA Jin J.-Q., Yao M.-Z., Ma C.-L., Ma J.-Q., Chen L.;
RT "Natural allelic variations of TCS1 play a crucial role in caffeine
RT biosynthesis of tea plant and its related species.";
RL Plant Physiol. Biochem. 100:18-26(2016).
CC -!- FUNCTION: Involved in the biosynthesis of caffeine (PubMed:26773541).
CC Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine and
CC of theobromine to caffeine (PubMed:26773541).
CC {ECO:0000269|PubMed:26773541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + theobromine = caffeine + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:20944, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27732, ChEBI:CHEBI:28946, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.160;
CC Evidence={ECO:0000269|PubMed:26773541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20945;
CC Evidence={ECO:0000269|PubMed:26773541};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-methylxanthine + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + theobromine; Xref=Rhea:RHEA:24604,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28946, ChEBI:CHEBI:48991,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.160;
CC Evidence={ECO:0000269|PubMed:26773541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC Evidence={ECO:0000269|PubMed:26773541};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000250|UniProtKB:Q9FZN8}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; KT215399; ALP01721.1; -; mRNA.
DR AlphaFoldDB; A0A0S2PMA8; -.
DR SMR; A0A0S2PMA8; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102741; F:paraxanthine:S-adenosyl-L-methionine 3-N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102740; F:theobromine:S-adenosyl-L-methionine 1-N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Transferase.
FT CHAIN 1..369
FT /note="Caffeine synthase 1"
FT /id="PRO_0000451799"
FT BINDING 24
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 27..31
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 65..66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 101..104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 138..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 155..157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 156..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT SITE 153
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 225
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 269
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000269|PubMed:26773541"
FT SITE 317
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 332
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT MUTAGEN 269
FT /note="C->S: Strongly reduced caffeine synthase and
FT theobromine synthase activities."
FT /evidence="ECO:0000269|PubMed:26773541"
SQ SEQUENCE 369 AA; 41401 MW; 1BD972AD4FB99430 CRC64;
MELATTGKVN EVLFMNRGEG ESSYAQNSSF TQQVASMATP ALENAVETLF SKDFHLQALN
AVDLGCAAGP NTFAVISTIK RMMEKKCREL NCQTLELQVY LNDLFGNDFN TLFKGLSSEV
IGNKCEEVPC YVMGVPGSFH GRLFPRNSLH LVHSSYSVHW LTQAPKGLTN REGLALNKGK
IYISKTSPPI VREAYLTQFH EDFTMFLNAR SQEVVPNGCM VLILRSRQSS DPSDMQSCFT
WELLAKAIAE LVSQGLIDED KLDAFNIPCY FPSLEEVKDI VERDGSFTID HMEGFGLDSL
QMEENDKWVR GEKFTKVVRA FTEPIISNQF GHEIMDKLYD KFTHIVVSDF EAKLPKTTSI
ILVLSKIDG
