CS4_COFAR
ID CS4_COFAR Reviewed; 385 AA.
AC Q9AVL9; A0A096X776; Q8H0F8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable caffeine synthase 4 {ECO:0000303|PubMed:12527364};
DE Short=CtCS4 {ECO:0000303|PubMed:12527364};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q8H0D2};
DE AltName: Full=Methyltransferase-like 1 {ECO:0000303|PubMed:11108716, ECO:0000303|PubMed:25249475};
DE Short=CaMTL1 {ECO:0000303|PubMed:11108716, ECO:0000303|PubMed:25249475};
GN Name=CS4 {ECO:0000303|PubMed:12527364};
GN Synonyms=MTL1 {ECO:0000303|PubMed:11108716, 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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Caturra;
RX PubMed=11108716; DOI=10.1074/jbc.m009480200;
RA Ogawa M., Herai Y., Koizumi N., Kusano T., Sano H.;
RT "7-Methylxanthine methyltransferase of coffee plants. Gene isolation and
RT enzymatic properties.";
RL J. Biol. Chem. 276:8213-8218(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=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).
CC -!- FUNCTION: May be involved in the biosynthesis of caffeine.
CC {ECO:0000250|UniProtKB:Q8H0D2}.
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:Q8H0D2}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, young and old leaves.
CC {ECO:0000269|PubMed:11108716}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB039725; BAB39213.1; -; mRNA.
DR EMBL; AB054843; BAC43759.1; -; mRNA.
DR EMBL; KF743059; AHA82523.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AVL9; -.
DR SMR; Q9AVL9; -.
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: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; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..385
FT /note="Probable caffeine synthase 4"
FT /id="PRO_0000408308"
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 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 22
FT /note="S -> L (in Ref. 3; AHA82523)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="K -> R (in Ref. 2; BAC43759 and 3; AHA82523)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> V (in Ref. 3; AHA82523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43243 MW; 003A5837FF0AE300 CRC64;
MELQEVLHMN GGEGEASYAK NSSFNQLVLA KVKPVLEQCV RELLRANLPN INKCIKVADL
GCASGPNTLL TVWDTVQSID KVKQEMKNEL ERPTIQVFLT DLFQNDFNSV FMLLPSFYRK
LEKENGRKIG SCLIAAMPGS FHGRLFPEES MHFLHSSYSL QFLSQVPSGL VTELGITANK
RSIYSSKASP PPVQKAYLDQ FTKDFTTFLR MRSEELLSRG RMLLTCICKG DECDGPNTMD
LLEMAINDLV AEGRLGEEKL DSFNVPIYTA SVEEVKCMVE EEGSFEILYL QTFKLRYDAG
FSIDDDCQVR SHSPVYSDEH ARAAHVASLI RSVYEPILAS HFGEAIIPDI FHRFATNAAK
VIRLGKGFYN NLIISLAKKP EKSDI
