DXMT2_COFAR
ID DXMT2_COFAR Reviewed; 384 AA.
AC Q8H0D3; G9BZJ8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=3,7-dimethylxanthine N-methyltransferase 2 {ECO:0000303|PubMed:25249475};
DE Short=CaDXMT2 {ECO:0000303|PubMed:25249475};
DE EC=2.1.1.160 {ECO:0000269|PubMed:12527364};
DE AltName: Full=Caffeine synthase 1 {ECO:0000303|PubMed:25249475};
DE AltName: Full=Caffeine synthase 6 {ECO:0000303|PubMed:12527364};
DE Short=CtCS6 {ECO:0000303|PubMed:12527364};
GN Name=DXMT2 {ECO:0000303|PubMed:25249475};
GN Synonyms=CCS1 {ECO:0000303|PubMed:25249475},
GN CS6 {ECO:0000303|PubMed:12527364};
OS Coffea arabica (Arabian coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=13443;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=12527364; DOI=10.1016/s0014-5793(02)03781-x;
RA Mizuno K., Okuda A., Kato M., Yoneyama N., Tanaka H., Ashihara H.,
RA Fujimura T.;
RT "Isolation of a new dual-functional caffeine synthase gene encoding an
RT enzyme for the conversion of 7-methylxanthine to caffeine from coffee
RT (Coffea arabica L.).";
RL FEBS Lett. 534:75-81(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Caturra, and cv. ET39;
RX PubMed=25249475; DOI=10.1007/s00425-014-2170-7;
RA Perrois C., Strickler S.R., Mathieu G., Lepelley M., Bedon L., Michaux S.,
RA Husson J., Mueller L., Privat I.;
RT "Differential regulation of caffeine metabolism in Coffea arabica (Arabica)
RT and Coffea canephora (Robusta).";
RL Planta 241:179-191(2015).
RN [3]
RP FUNCTION, AND 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 caffeine. Catalyzes the
CC conversion of 7-methylxanthine (7mX) to theobromine and of theobromine
CC to caffeine. Has 1-N-methylation activity.
CC {ECO:0000269|PubMed:12527364, ECO:0000303|PubMed:18068204}.
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:12527364};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC Evidence={ECO:0000269|PubMed:12527364};
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:12527364};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20945;
CC Evidence={ECO:0000269|PubMed:12527364};
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:0000269|PubMed:12527364};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10281;
CC Evidence={ECO:0000269|PubMed:12527364};
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=125.6 uM for 7-methylxanthine for the recombinant protein
CC {ECO:0000269|PubMed:12527364};
CC KM=30.8 uM for paraxanthine for the recombinant protein
CC {ECO:0000269|PubMed:12527364};
CC KM=157.0 uM for theobromine for the recombinant protein
CC {ECO:0000269|PubMed:12527364};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:12527364}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing endosperm
CC (PubMed:12527364). Detected in young leaves and flower buds
CC (PubMed:12527364, PubMed:25249475). Present in immature fruits
CC (grains), but barely in mature fruits (PubMed:25249475).
CC {ECO:0000269|PubMed:12527364, ECO:0000269|PubMed:25249475}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB086414; BAC43760.1; -; mRNA.
DR EMBL; HQ724310; AEV57593.1; -; Genomic_DNA.
DR EMBL; KJ577792; AIG53793.1; -; Genomic_DNA.
DR EMBL; KJ577793; AIG53794.1; -; mRNA.
DR AlphaFoldDB; Q8H0D3; -.
DR SMR; Q8H0D3; -.
DR KEGG; ag:BAC43760; -.
DR BRENDA; 2.1.1.159; 1559.
DR BRENDA; 2.1.1.160; 1559.
DR SABIO-RK; Q8H0D3; -.
DR Proteomes; UP000515148; Genome assembly.
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 1: Evidence at protein level;
KW Alkaloid metabolism; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..384
FT /note="3,7-dimethylxanthine N-methyltransferase 2"
FT /id="PRO_0000408309"
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 60..61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 98..101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 139..141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 156..158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 157..161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 260
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 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT SITE 154
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 266
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 SITE 343
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 177
FT /note="A -> V (in Ref. 2; AEV57593/AIG53793/AIG53794)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..193
FT /note="GPPIK -> RPPIQ (in Ref. 2; AEV57593/AIG53793/
FT AIG53794)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> V (in Ref. 2; AEV57593/AIG53793/AIG53794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43276 MW; 5DC3ED92FD94BEF3 CRC64;
MELQEVLHMN GGEGDTSYAK NSSYNLFLIR VKPVLEQCIQ ELLRANLPNI NKCFKVGDLG
CASGPNTFST VRDIVQSIDK VGQEKKNELE RPTIQIFLND LFQNDFNSVF KLLPSFYRNL
EKENGRKIGS CLIGAMPGSF YSRLFPEESM HFLHSCYCLH WLSQVPSGLV TELGISANKG
CIYSSKASGP PIKKAYLDQF TKDFTTFLRI HSEELISRGR MLLTFICKED EFDHPNSMDL
LEMSINDLVI EGHLEEEKLD SFNVPIYAPS TEEVKRIVEE EGSFEILYLE TFYAPYDAGF
SIDDDYQGRS HSPVSCDEHA RAAHVASVVR SIYEPILASH FGEAILPDLS HRIAKNAAKV
LRSGKGFYDS VIISLAKKPE KADM
