TCS2_CAMSI
ID TCS2_CAMSI Reviewed; 365 AA.
AC Q68CM3; B9VI89; F4YFI8; K9MPP6; Q5ECF6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Probable caffeine synthase 2 {ECO:0000303|Ref.1};
DE EC=2.1.1.160 {ECO:0000250|UniProtKB:Q9FZN8};
GN Name=TCS2 {ECO:0000303|Ref.1};
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 Kato M., Mizuno K., Fujimura T., Ashihara H.;
RT "Molecular cloning and expression analysis of cDNA sequence encoding
RT caffeine synthase from Camellia sinensis.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rani A., Kumar S., Ahuja P.S.;
RT "Cloning and characterization of caffeine synthase from Camellia
RT sinensis(L.) O.Kuntze cv. UPASI-9.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jin J.Q., Chen L., Yao M.Z., Ma C.L.;
RT "Cloning and analysis of the N-methyltransferase gene family involving in
RT caffeine biosynthesis of tea plant.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-150.
RC STRAIN=cv. Kangra jat;
RX PubMed=19479388; DOI=10.1007/s12033-009-9188-2;
RA Mohanpuria P., Kumar V., Joshi R., Gulati A., Ahuja P.S., Yadav S.K.;
RT "Caffeine biosynthesis and degradation in tea [Camellia sinensis (L.) O.
RT Kuntze] is under developmental and seasonal regulation.";
RL Mol. Biotechnol. 43:104-111(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-359.
RX PubMed=23315209; DOI=10.1007/s12010-012-0070-5;
RA Thirugnanasambantham K., Prabu G., Palanisamy S., Chandrabose S.R.S.,
RA Mandal A.K.A.;
RT "Analysis of dormant bud (Banjhi) specific transcriptome of tea (Camellia
RT sinensis (L.) O. Kuntze) from cDNA library revealed dormancy-related
RT genes.";
RL Appl. Biochem. Biotechnol. 169:1405-1417(2013).
RN [6]
RP REVIEW ON CAFFEINE BIOSYNTHESIS.
RX PubMed=18068204; DOI=10.1016/j.phytochem.2007.10.029;
RA Ashihara H., Sano H., Crozier A.;
RT "Caffeine and related purine alkaloids: biosynthesis, catabolism, function
RT and genetic engineering.";
RL Phytochemistry 69:841-856(2008).
CC -!- FUNCTION: May be involved in the biosynthesis of caffeine (By
CC similarity). Catalyzes the conversion of 7-methylxanthine (7mX) to
CC theobromine and of theobromine to caffeine (By similarity). Has 1-N-
CC methylation activity (By similarity). {ECO:0000250|UniProtKB:Q9FZN8}.
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:0000250|UniProtKB:Q9FZN8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC Evidence={ECO:0000250|UniProtKB:Q9FZN8};
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:0000250|UniProtKB:Q9FZN8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20945;
CC Evidence={ECO:0000250|UniProtKB:Q9FZN8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,7-dimethylxanthine + S-adenosyl-L-methionine = caffeine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10280,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25858, ChEBI:CHEBI:27732,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.160;
CC Evidence={ECO:0000250|UniProtKB:Q9FZN8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10281;
CC Evidence={ECO:0000250|UniProtKB:Q9FZN8};
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; AB031281; BAD42854.1; -; mRNA.
DR EMBL; AY907710; AAW88351.1; -; mRNA.
DR EMBL; JX647691; AFV99129.1; -; Genomic_DNA.
DR EMBL; FJ554589; ACM07420.1; -; mRNA.
DR EMBL; HM003356; AEC11049.1; -; mRNA.
DR AlphaFoldDB; Q68CM3; -.
DR SMR; Q68CM3; -.
DR BRENDA; 2.1.1.160; 1084.
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:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alkaloid metabolism; Magnesium; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..365
FT /note="Probable caffeine synthase 2"
FT /id="PRO_0000408311"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 22..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 61..62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 97..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 134..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 151..153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 152..156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 261
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 SITE 149
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 221
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 265
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 313
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 328
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 39
FT /note="N -> T (in Ref. 4; ACM07420)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="L -> H (in Ref. 4; ACM07420)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="M -> V (in Ref. 2; AAW88351)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="P -> Q (in Ref. 2; AAW88351 and 4; ACM07420)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="F -> S (in Ref. 2; AAW88351)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="N -> D (in Ref. 2; AAW88351)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="F -> L (in Ref. 2; AAW88351 and 5; AEC11049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40824 MW; 010BA6F7B3075C2E CRC64;
MKEVKEALFM NKGEGESSYA QNSSFTQTVT SMTMPVLENA VETLFSKDFH LLQALNAVDL
GCAAGPTTFT VISTIKRMME KKCRELNCQT LELQVYLNDL PGNDFNTLFK GLPSKVVGNK
CEEVSCYVVG VPGSFHGRLF PRNSLHLVHS CYSVHWLTQA PKGLTSKEGL ALNKGKIYIS
KTSPPVVREA YLSQFHEDFT MFLNSRSQEV VPNGCMVLIL RGRLSSDPSD MGSCFTWELL
AVAIAELVSQ GLIDEDKLDT FNVPSYFPSL EEVKDIVERN GSFTIDHMEG FELDSPEMQE
NDKWVRGEKF ATVARAFTEP IISNQFGHEI MDKLYEKFTH IVVSDFEAKI PKITSIILVL
SKIVG
