TCS3_CAMSI
ID TCS3_CAMSI Reviewed; 368 AA.
AC A0A0S2PM82;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Caffeine synthase 3 {ECO:0000303|Ref.1};
DE Short=TCS1e {ECO:0000303|PubMed:26773541};
DE EC=2.1.1.160 {ECO:0000269|PubMed:26773541};
GN Name=TCS1E {ECO:0000303|PubMed:26773541};
OS Camellia sinensis (Tea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=4442;
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, CATALYTIC ACTIVITY, GENE FAMILY, AND 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; KT215397; ALP01719.1; -; mRNA.
DR AlphaFoldDB; A0A0S2PM82; -.
DR SMR; A0A0S2PM82; -.
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..368
FT /note="Caffeine synthase 3"
FT /id="PRO_0000451796"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 26..30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 100..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 137..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 154..156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 155..159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 264
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 SITE 152
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 224
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 268
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:A0A0S2PMA8"
FT SITE 316
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 331
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
SQ SEQUENCE 368 AA; 41183 MW; FB6D135036758AE1 CRC64;
MELAMGKVNE VLFMNRGEGE SSYAQNSSFT QQVASMARPA LENAVKTLFS KDFHLQALNA
ADLGCAAGPN TFAVISTTKR MMEKKCRELN CQTLELQVYL NDLFGNDFNT LFKGLSSEVV
GNKCEEVPCY VMGVPGSFHG RLFPRSSLHL VHSSYSVHWL TQAPKGLTSR EGLALNKGKI
YISKTSPPVV REAYLSQFHE DFTMFLNARS QEVVPNGCMV LILRGRKASD PSDMESCFTW
ELLAIAIAEL VSQGLIDEDK LDTFNIPCYF PSLEEVKDIV ERDGSFTIDH MEGFELDSLQ
MQENDKWVRG ENFTKVVRAF TEPIISNQFG HEIMGKLYDK FTHIVVSDLE AKLPKTTSII
LVLSKIDG
