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BTS2_THECC
ID   BTS2_THECC              Reviewed;         367 AA.
AC   A0A061FKL9;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Probable 7-methylxanthine methyltransferase 2 {ECO:0000305};
DE            EC=2.1.1.159 {ECO:0000250|UniProtKB:A0A061FMF5};
DE   AltName: Full=Theobromine synthase TCM_042578 {ECO:0000305};
GN   ORFNames=TCM_042578 {ECO:0000312|EMBL:EOY17875.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6;
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Livingstone D. III,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
RN   [2]
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: Involved in the biosynthesis of theobromine.
CC       {ECO:0000250|UniProtKB:A0A061FMF5}.
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=2.1.1.159;
CC         Evidence={ECO:0000250|UniProtKB:A0A061FMF5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC         Evidence={ECO:0000250|UniProtKB:A0A061FMF5};
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:A0A061FMF5}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; CM001888; EOY17874.1; -; Genomic_DNA.
DR   EMBL; CM001888; EOY17875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061FKL9; -.
DR   SMR; A0A061FKL9; -.
DR   EnsemblPlants; EOY17874; EOY17874; TCM_042578.
DR   EnsemblPlants; EOY17875; EOY17875; TCM_042578.
DR   Gramene; EOY17874; EOY17874; TCM_042578.
DR   Gramene; EOY17875; EOY17875; TCM_042578.
DR   eggNOG; ENOG502QQVK; Eukaryota.
DR   HOGENOM; CLU_019628_2_0_1; -.
DR   OMA; NNETHHQ; -.
DR   Proteomes; UP000026915; Chromosome 10.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..367
FT                   /note="Probable 7-methylxanthine methyltransferase 2"
FT                   /id="PRO_0000451784"
FT   BINDING         20
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         23..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         63..64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT   BINDING         99..102
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         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         260
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   SITE            149
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT   SITE            220
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT   SITE            264
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT   SITE            324
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FZN8"
SQ   SEQUENCE   367 AA;  40910 MW;  C88CAB8649902B57 CRC64;
     MAMKVKDIVF MNKGDGENSY VKSAGLTLKV IAKTQPIVQK AVQSLFTGTH STPLQVVNVA
     DLGCALGPQP LESMSIVIES IVEKCGELGC EMPEIQFHLN DLAGNDFNTL FKGLSVVQEK
     YKNVSWFAMG APGSFHGRLF PRNSMHLVHS CYSVHWLSKA PKITSEAGLP LNKGKIYMSK
     TSPPAVREGY LSQFEEDFSS VLRFRSPELA PDGRMVLILN GRQSADPTEK DICYLWDLLA
     EALSYLVSEG LIDEEKLDSF NVPYYNPSQE EVERVIDKEG SFTTEFSDTV VLEIGGKNAW
     SDPGLRIKGY RCFSEPILSH QFGEEVMDKL FDKAEEILAE DYKQGKEATK NISIVVVLKK
     KTNQTWT
 
 
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