MXMT1_COFCA
ID MXMT1_COFCA Reviewed; 378 AA.
AC Q4U5S1; Q2L8A5; Q5EBW9; Q5EBX0; Q7FRH9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=7-methylxanthine methyltransferase 1 {ECO:0000303|PubMed:25249475};
DE Short=CcMXMT1 {ECO:0000303|PubMed:25249475};
DE EC=2.1.1.159 {ECO:0000250|UniProtKB:Q9AVJ9};
DE AltName: Full=7-methylxanthine N-methyltransferase 1 {ECO:0000305};
DE AltName: Full=N-methyltransferase {ECO:0000303|PubMed:16043251};
DE AltName: Full=Theobromine synthase MXMT1 {ECO:0000305};
GN Name=MXMT1 {ECO:0000303|PubMed:25249475};
GN Synonyms=NMT {ECO:0000303|PubMed:16043251};
GN ORFNames=GSCOC_T00004719001 {ECO:0000312|EMBL:CDP21124.1};
OS Coffea canephora (Robusta 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=49390;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Kretschmar J.A., Baumann T.W.;
RT "N-methyltransferases in the genus Coffea.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA de Kochko A., Moreau C., Noirot M., Chrestin H., Lesage A., Campa C.;
RT "Genetic diversity of N-methyltransferase genes involved in caffeine
RT biosynthesis in coffee trees.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. S-274;
RX PubMed=16043251; DOI=10.1016/j.jbiotec.2005.06.008;
RA Satyanarayana K.V., Kumar V., Chandrashekar A., Ravishankar G.A.;
RT "Isolation of promoter for N-methyltransferase gene associated with
RT caffeine biosynthesis in Coffea canephora.";
RL J. Biotechnol. 119:20-25(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. S-274;
RA Satyanarayana K.V., Chandrashekar A., Ravishankar G.A.;
RT "Intra and inter species conservation of non-coding regions of N-
RT methyltransferase genes associated with caffeine biosynthesis in coffee.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=23376454; DOI=10.1016/j.gene.2013.01.035;
RA Mohanan S., Gowda K., Kandukuri S.V., Chandrashekar A.;
RT "Involvement of a novel intronic microRNA in cross regulation of N-
RT methyltransferase genes involved in caffeine biosynthesis in Coffea
RT canephora.";
RL Gene 519:107-112(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. DH200-94;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. DH200-94;
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
RN [8]
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 Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine and
CC of paraxanthine to caffeine (By similarity).
CC {ECO:0000250|UniProtKB:Q9AVJ9}.
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:Q9AVJ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC Evidence={ECO:0000250|UniProtKB:Q9AVJ9};
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:Q9AVJ9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLN8}.
CC -!- TISSUE SPECIFICITY: Mainly expressed, at low levels, in leaves and
CC fruits (grains) (PubMed:25249475, PubMed:25190796). Also present, at
CC lower levels, in roots, stamens and pistils (PubMed:25190796).
CC {ECO:0000269|PubMed:25190796, ECO:0000269|PubMed:25249475}.
CC -!- DEVELOPMENTAL STAGE: In leaves, mostly expressed in young tissues
CC (PubMed:25249475). In fruits, mostly expressed in green grains but
CC fades out as they are yellowing to disappear in red mature grains
CC (PubMed:25249475, PubMed:25190796). {ECO:0000269|PubMed:25190796,
CC ECO:0000269|PubMed:25249475}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF494414; AAM18504.1; -; mRNA.
DR EMBL; AY273814; AAQ16155.1; -; Genomic_DNA.
DR EMBL; AY918124; AAX07284.1; -; Genomic_DNA.
DR EMBL; AY918126; AAX07285.1; -; Genomic_DNA.
DR EMBL; DQ010011; AAY56107.1; -; Genomic_DNA.
DR EMBL; DQ348077; ABC74575.1; -; Genomic_DNA.
DR EMBL; HQ616707; ADR30039.1; -; mRNA.
DR EMBL; JX978507; AFV60435.1; -; Genomic_DNA.
DR EMBL; JX978517; AFV60445.1; -; mRNA.
DR EMBL; HG741650; CDP21124.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4U5S1; -.
DR SMR; Q4U5S1; -.
DR EnsemblPlants; CDP21124; CDP21124; GSCOC_T00004719001.
DR Gramene; CDP21124; CDP21124; GSCOC_T00004719001.
DR OMA; ISSERCW; -.
DR PhylomeDB; Q4U5S1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alkaloid metabolism; Cytoplasm; Magnesium; Metal-binding;
KW Methyltransferase; Transferase.
FT CHAIN 1..378
FT /note="7-methylxanthine methyltransferase 1"
FT /id="PRO_0000451780"
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 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 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 362
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 337
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 4
FT /note="Q -> R (in Ref. 4; ABC74575)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> P (in Ref. 4; ABC74575)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..255
FT /note="LLE -> RLG (in Ref. 3; AAX07285)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..271
FT /note="IPFFTPSA -> VPIYTASV (in Ref. 3; AAX07285)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="F -> S (in Ref. 3; AAX07284)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="I -> M (in Ref. 3; AAX07285)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Y -> N (in Ref. 4; ABC74575)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="I -> V (in Ref. 3; AAX07284)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="T -> R (in Ref. 1; AAM18504, 2; AAQ16155, 5;
FT ADR30039, 3; AAX07284 and 4; ABC74575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42692 MW; F4F81AF3D5219DA9 CRC64;
MELQEVLHMN EGEGDTSYAK NASYNLALAK VKPFLEQCIR ELLRANLPNI NKCIKVADLG
CASGPNTLLT VRDIVQSIDK VGQEEKNELE RPTIQIFLND LFQNDFNSVF KLLPSFYRKL
EKENGRKIGS CLISAMPGSF YGRLFPEESM HFLHSCYSVH WLSQVPSGLV IELGIGANKG
SIYSSKGCRP PVQKAYLDQF TKDFTTFLRI HSKELFSRGR MLLTCICKVD EFDEPNPLDL
LDMAINDLIV EGLLEEEKLD SFNIPFFTPS AEEVKCIVEE EGSCEILYLE TFKAHYDAAF
SIDDDYPVTS HEQIKAEYVA SLIRSVYEPI LASHFGEAIM PDLFHRLAKH AAKVLHMGKG
CYNNLIISLA KKPEKSDV
