BTS5_THECC
ID BTS5_THECC Reviewed; 364 AA.
AC A0A061FKM4; A0A061FLA5; A0A061FLB1; A0A061FMG9; A0A061FTC7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Probable 7-methylxanthine methyltransferase 5 {ECO:0000305};
DE EC=2.1.1.159 {ECO:0000250|UniProtKB:A0A061FMF5};
DE AltName: Full=Theobromine synthase TCM_042587/TCM_042590 {ECO:0000305};
GN ORFNames=TCM_042587 {ECO:0000312|EMBL:EOY17880.1,
GN ECO:0000312|EMBL:EOY17881.1}, TCM_042590 {ECO:0000312|EMBL:EOY17885.1,
GN ECO:0000312|EMBL:EOY17887.1};
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] (ISOFORMS 1; 2; 3 AND 4).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A0A061FKM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A061FKM4-2; Sequence=VSP_060870;
CC Name=3;
CC IsoId=A0A061FKM4-3; Sequence=VSP_060868, VSP_060869;
CC Name=4;
CC IsoId=A0A061FKM4-4; Sequence=VSP_060867;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; CM001888; EOY17880.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY17881.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY17884.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY17885.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY17886.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY17887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FKM4; -.
DR SMR; A0A061FKM4; -.
DR EnsemblPlants; EOY17880; EOY17880; TCM_042587. [A0A061FKM4-1]
DR EnsemblPlants; EOY17881; EOY17881; TCM_042587. [A0A061FKM4-2]
DR EnsemblPlants; EOY17884; EOY17884; TCM_042590.
DR EnsemblPlants; EOY17885; EOY17885; TCM_042590. [A0A061FKM4-1]
DR EnsemblPlants; EOY17886; EOY17886; TCM_042590. [A0A061FKM4-3]
DR EnsemblPlants; EOY17887; EOY17887; TCM_042590. [A0A061FKM4-4]
DR Gramene; EOY17880; EOY17880; TCM_042587. [A0A061FKM4-1]
DR Gramene; EOY17881; EOY17881; TCM_042587. [A0A061FKM4-2]
DR Gramene; EOY17884; EOY17884; TCM_042590.
DR Gramene; EOY17885; EOY17885; TCM_042590. [A0A061FKM4-1]
DR Gramene; EOY17886; EOY17886; TCM_042590. [A0A061FKM4-3]
DR Gramene; EOY17887; EOY17887; TCM_042590. [A0A061FKM4-4]
DR eggNOG; ENOG502QQVK; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR OMA; INIMDAT; -.
DR OrthoDB; 689338at2759; -.
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 Alternative splicing; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="Probable 7-methylxanthine methyltransferase 5"
FT /id="PRO_0000451787"
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 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 325
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 4)"
FT /id="VSP_060867"
FT VAR_SEQ 250..260
FT /note="GLVDEGKLDSF -> AKCQIFNSFLI (in isoform 3)"
FT /id="VSP_060868"
FT VAR_SEQ 261..364
FT /note="Missing (in isoform 3)"
FT /id="VSP_060869"
FT VAR_SEQ 363..364
FT /note="Missing (in isoform 2)"
FT /id="VSP_060870"
FT CONFLICT 247..249
FT /note="Missing (in Ref. 1; EOY17884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40757 MW; BDF0F38A19F19FA2 CRC64;
MEAVKDVLCM NNGVGENSYV KAEALTIKVM AITKPIVPKA VQSLFTETDH SIPLQVVNVA
DLGCAVGPQP LEFMSTVIES ILKKCGEMGR EMPEIQFFLN DLVGNDFNTL FKGLSVVQEK
YKKVSWFAMG APGSFHGRLF PRNSMHLVYS CYSVHWLSEA PKITNEAGLP LNKGKIYMSK
TSPPAVTKAY LSQFQEDFSS LLKFRSQELA PNGRVVLIFN GRQTADPTNK DTCYTWDLLA
EALSYLVSQG LVDEGKLDSF NVPYYNPSQE EIKYLVDKEG SLTIEFIDTI ELEIGGPNGY
WSSPESRIRG HRCFTEPLLS HQFGERLMDK LYDKATQILV EDYKHGKEAT KNIGIAVVLK
KKKL
