XMT2_COFAR
ID XMT2_COFAR Reviewed; 385 AA.
AC A0A096VHY7; A0A096VHY8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Xanthosine methyltransferase 2 {ECO:0000303|PubMed:25249475};
DE Short=CaXMT2 {ECO:0000303|PubMed:25249475};
DE EC=2.1.1.158 {ECO:0000250|UniProtKB:Q9AVK0};
GN Name=XMT2 {ECO:0000303|PubMed:25249475};
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 [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 [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 caffeine (By similarity).
CC Specific for xanthosine and could not use xanthosine 5'-monophosphate
CC (XMP) as substrate (By similarity). Catalyzes the 7-N-methylation
CC activity of xanthosine, but does not have 1-N- or 3-N-methylation
CC activity (By similarity). {ECO:0000250|UniProtKB:Q9AVK0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + xanthosine = 7-methylxanthosine + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:15025, ChEBI:CHEBI:18107,
CC ChEBI:CHEBI:49310, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.158; Evidence={ECO:0000250|UniProtKB:Q9AVK0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15026;
CC Evidence={ECO:0000250|UniProtKB:Q9AVK0};
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:Q9AVK0}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in young leaves but not in
CC mature leaves (PubMed:25249475). Barely detectable in fruits (grains)
CC (PubMed:25249475). {ECO:0000269|PubMed:25249475}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; JX978515; AFV60443.1; -; Genomic_DNA.
DR EMBL; JX978522; AFV60450.1; -; mRNA.
DR AlphaFoldDB; A0A096VHY7; -.
DR SMR; A0A096VHY7; -.
DR Proteomes; UP000515148; Genome assembly.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; 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 Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..385
FT /note="Xanthosine methyltransferase 2"
FT /id="PRO_0000451779"
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 99..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 140..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 157..159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 158..162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 179
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 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT SITE 155
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 267
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 344
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 8
FT /note="R -> Q (in Ref. 1; AFV60450)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="M -> V (in Ref. 1; AFV60450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43520 MW; 23EC17FBCDF9C4E8 CRC64;
MELQEVLRMN GGEGDTSYAK NSAYNHLVLN KVKPVLEQCI RELLRASLPN INKCIKVADL
GCASGPNTLL TVRDIVQSID KVGQEKKNEL ERPTIQIFLN DLFQNDFNSV FKLLPSFYRK
LEKENGRKIG SCLIGAMPGS FYSRLFPEES MHFLHSCYCL HWLSQVPSGL VTELGISTNK
GSIYSSKASR LPVQKAYLDQ FTKDFTTFLR IHSEELFSHG RMLLTCICKG VEFDALNAID
LLEMAINDLV VEGHLEEEKL DSFNLPVYIP SAEEVKCIVE EEGSFEILYL ETFKVLYDAG
FSIDDNYPVR SHVQVYSDEH IKAEYVASSV RAVYEPILAS HFGEAIIPDI FHRFAKHAAK
VLPLGKAYYN NLIISLAKKP EKSDM
