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PCS2_CAMPL
ID   PCS2_CAMPL              Reviewed;         365 AA.
AC   Q2HXI5;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Probable 7-methylxanthine methyltransferase PCS2 {ECO:0000303|PubMed:16333668};
DE            EC=2.1.1.159 {ECO:0000250|UniProtKB:Q2HXI6};
DE   AltName: Full=Theobromine synthase PCS2 {ECO:0000303|PubMed:16333668};
GN   Name=PCS2 {ECO:0000303|PubMed:16333668};
OS   Camellia ptilophylla (Cocoa tea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Theaceae; Camellia.
OX   NCBI_TaxID=319931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=16333668; DOI=10.1007/s00438-005-0070-z;
RA   Yoneyama N., Morimoto H., Ye C.-X., Ashihara H., Mizuno K., Kato M.;
RT   "Substrate specificity of N-methyltransferase involved in purine alkaloids
RT   synthesis is dependent upon one amino acid residue of the enzyme.";
RL   Mol. Genet. Genomics 275:125-135(2006).
CC   -!- FUNCTION: No detectable N-methyltransferase activity.
CC       {ECO:0000269|PubMed:16333668}.
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:Q2HXI6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24605;
CC         Evidence={ECO:0000250|UniProtKB:Q2HXI6};
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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; AB207818; BAE79733.1; -; mRNA.
DR   AlphaFoldDB; Q2HXI5; -.
DR   SMR; Q2HXI5; -.
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; Transferase.
FT   CHAIN           1..365
FT                   /note="Probable 7-methylxanthine methyltransferase PCS2"
FT                   /id="PRO_0000451791"
FT   BINDING         19
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE70"
FT   BINDING         22..26
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         97..100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         134..136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         151..153
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         152..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A4GE69"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   BINDING         259
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         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT   SITE            149
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT   SITE            221
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT   SITE            265
FT                   /note="Involved in substrate discrimination"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT   SITE            313
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"
SQ   SEQUENCE   365 AA;  40722 MW;  037A871A9A4B9DBE CRC64;
     MKEVKEALFM NKGEGESSYA QNSSFTETVT SMTMPVLENA VETLFSKDFH LLQALNAVDL
     GCAAGPTTFT VISTIKKMME KKCRELNCQT LELQVYLNDL PGNDFNTLFK GLSSKVVGNN
     CEEVSCYVVG VPGSFHGRLF PRNSLHLVHS CYSVHWLTQA PKGLTSKEGL ALNKGKIYIS
     KTSPPVVREA YLSQFHEDFT MFLNSRSQEV VPNGCMVLIL RGRLSSDPSD MESCFTWELL
     AAAIAELVSQ GLIDEDKLDT FNVPSYFPSL EEVKDIVERN GSFTIDHMEG FELDSPQMQE
     NDKWVRGEKF ATVARASTEP IISNQFGHEI MDKLYEKFTH IVISDLEAKI PKVTSIILVL
     SKIVG
 
 
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