BTS1_THECC
ID BTS1_THECC Reviewed; 363 AA.
AC A0A061FMF5; Q2HXL8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=7-methylxanthine methyltransferase 1 {ECO:0000303|PubMed:16333668};
DE EC=2.1.1.159 {ECO:0000269|PubMed:16333668};
DE AltName: Full=Theobromine synthase BTS1 {ECO:0000303|PubMed:16333668};
GN Name=BTS1 {ECO:0000303|PubMed:16333668};
GN Synonyms=BCS1 {ECO:0000303|PubMed:16333668};
GN ORFNames=TCM_042576 {ECO:0000312|EMBL:EOY17872.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16333668; DOI=10.1007/s00438-005-0070-z;
RA Yoneyama N., Morimoto H., Ye C.-X., Ashihara H., Mizuno K., Kato M.;
RT "Substrate specificity of N-methyltransferase involved in purine alkaloids
RT synthesis is dependent upon one amino acid residue of the enzyme.";
RL Mol. Genet. Genomics 275:125-135(2006).
RN [2]
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 [3]
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 (PubMed:16333668). Catalyzes the conversion of 7-methylxanthine (7mX)
CC to theobromine but not able to convert paraxanthine to caffeine
CC (PubMed:16333668). {ECO:0000269|PubMed:16333668}.
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:0000269|PubMed:16333668};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC Evidence={ECO:0000269|PubMed:16333668};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for 7-methylxanthine (in the presence of 50 uM S-adenosyl-
CC L-methionine) {ECO:0000269|PubMed:16333668};
CC pH dependence:
CC Optimum pH is 9.0-9.5. {ECO:0000269|PubMed:16333668};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:16333668}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB096699; BAE79730.1; -; mRNA.
DR EMBL; CM001888; EOY17872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FMF5; -.
DR SMR; A0A061FMF5; -.
DR EnsemblPlants; EOY17872; EOY17872; TCM_042576.
DR Gramene; EOY17872; EOY17872; TCM_042576.
DR eggNOG; ENOG502QQVK; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR OMA; NALCKEW; -.
DR OrthoDB; 689338at2759; -.
DR BRENDA; 2.1.1.160; 6277.
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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..363
FT /note="7-methylxanthine methyltransferase 1"
FT /id="PRO_0000451783"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
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 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 97..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 132..134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 149..151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 150..154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 171
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 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT SITE 147
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 219
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 263
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 321
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 84
FT /note="T -> S (in Ref. 1; BAE79730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40900 MW; FB835D5923AD71ED CRC64;
MEVKEMLFMN KGDGENSYVK TSGYTQKVAA VTQPVVYRAA QSLFTGRNSC SYQVLNVADL
GCSSGPNTFT VMSTVIESTR DKCTELNWQM PEIQFYLNDL VGNDFNTLFK GLSVIQDKYK
NVSCFAMGAP GSFHGRLFPQ NSMHLIHSSY GVQWLSKVPK MTSEGGLSPP NKGKIYISKT
SPPAVWKAYL SQFQEDFLSF LRCRSPELVP DGRMVLIIHG RKSADPTTRE SCYTWEVLAD
AISYQVSQGL IDEEKLNSFN VPYYIPSQEE VRDLVNKEGS FLTEFVDTIE VELEGIWTGP
ENGAKNLRSF TEPMISHQFG EEVMDKLYDK VKDILVEDCK QEKQSTRGVS IVLELKKKES
HLS
