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CS1_COFCA
ID   CS1_COFCA               Reviewed;         385 AA.
AC   A0A096VHZ6;
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=Probable caffeine synthase MTL1 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:A4GE70};
DE   AltName: Full=Methyltransferase-like 1 {ECO:0000303|PubMed:25249475};
DE            Short=CcMTL1 {ECO:0000303|PubMed:25249475};
GN   Name=MTL1 {ECO:0000303|PubMed:25249475};
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 [GENOMIC DNA], 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).
CC   -!- FUNCTION: May be involved in the biosynthesis of caffeine.
CC       {ECO:0000250|UniProtKB:A4GE70}.
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:A4GE70}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; JX978525; AFV60453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A096VHZ6; -.
DR   SMR; A0A096VHZ6; -.
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   3: Inferred from homology;
KW   Magnesium; Metal-binding; Methyltransferase; Transferase.
FT   CHAIN           1..385
FT                   /note="Probable caffeine synthase MTL1"
FT                   /id="PRO_0000451792"
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"
SQ   SEQUENCE   385 AA;  43319 MW;  CA5A247DA27D6ECB CRC64;
     MELQEVLHMN GGEGEASYAK NSSFNQLALA KVKPFLEQCI RELLRANLPN INKCIKVADL
     GCASGPNTLL TVRDTVQSID KVRQEMKNEL ERPTIQVFLT DLFQNDFNSV FMLLPSFYRK
     LEKENGRKIG SCLIAAMPGS FHGRLFPEES MHFLHSSYSL QFLSQVPSGL VTELGITANK
     RSIYSSKASP PPVQKAYLDQ FTKDFTTFLR MRSEELLSRG RMLLTCICKG DECDGPNTMD
     LLEMAINDLV VEGRLGEEKL DSFNVPIYTA SVEEVKCMVE EEGSFEILYL QTFKLRYDAG
     FSIDDDCQVR SHSPEYSDEH ARAAHVASLI RSVYEPILAS HFGEAIIPDI FHRFATNAAK
     VIRLGKGFYN NLIISLAKKP EKSDV
 
 
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