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CAMT3_PETHY
ID   CAMT3_PETHY             Reviewed;         248 AA.
AC   A0A0S2UWA5;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Caffeoyl-CoA O-methyltransferase 3 {ECO:0000303|PubMed:26620524};
DE            Short=PhCCoAOMT3 {ECO:0000303|PubMed:26620524};
DE            EC=2.1.1.104 {ECO:0000255|PROSITE-ProRule:PRU01019, ECO:0000269|PubMed:26620524};
DE   AltName: Full=5-hydroxyferuloyl-CoA O-methyltransferase 1 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000269|PubMed:26620524};
GN   Name=CCOAOMT3 {ECO:0000303|PubMed:26620524};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=cv. Mitchell; TISSUE=Corolla;
RX   PubMed=26620524; DOI=10.1104/pp.15.01646;
RA   Shaipulah N.F.M., Muhlemann J.K., Woodworth B.D., Van Moerkercke A.,
RA   Verdonk J.C., Ramirez A.A., Haring M.A., Dudareva N., Schuurink R.C.;
RT   "CCoAOMT down-regulation activates anthocyanin biosynthesis in petunia.";
RL   Plant Physiol. 170:717-731(2016).
CC   -!- FUNCTION: Involved in the production of floral volatile
CC       phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell
CC       and cv. V26) from cinnamic acid, a common precursor with the
CC       anthocyanin biosynthesis pathway involved in flower pigmentation (By
CC       similarity). Methylates caffeoyl-CoA to feruloyl-CoA, also able to
CC       methylate 5-hydroxyferuloyl-CoA (PubMed:26620524).
CC       {ECO:0000250|UniProtKB:A0A0S2UWC9, ECO:0000269|PubMed:26620524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01019,
CC         ECO:0000269|PubMed:26620524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16926;
CC         Evidence={ECO:0000269|PubMed:26620524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-5-hydroxyferuloyl-CoA + S-adenosyl-L-methionine = (E)-
CC         sinapoyl-CoA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:64860, ChEBI:CHEBI:15378, ChEBI:CHEBI:57393,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156249;
CC         Evidence={ECO:0000269|PubMed:26620524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64861;
CC         Evidence={ECO:0000269|PubMed:26620524};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q40313};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:Q40313};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=15.0 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate
CC         {ECO:0000269|PubMed:26620524};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC       {ECO:0000250|UniProtKB:A0A0S2UWC9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:A0A0S2UWC9}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in petal limbs and tubes, and, at
CC       low levels, in stems, roots and leaves. {ECO:0000269|PubMed:26620524}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during flower development with highest
CC       levels in open flowers, at anthesis, and fades out as flowers are
CC       senescing. {ECO:0000269|PubMed:26620524}.
CC   -!- INDUCTION: Circadian-regulation with peak levels occurring at the end
CC       of the light period in flowers. {ECO:0000269|PubMed:26620524}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR   EMBL; KT223508; ALP75648.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2UWA5; -.
DR   SMR; A0A0S2UWA5; -.
DR   UniPathway; UPA00711; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0080076; F:caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lignin biosynthesis; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..248
FT                   /note="Caffeoyl-CoA O-methyltransferase 3"
FT                   /id="PRO_0000451496"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         64
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         88..89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         164
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         191
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q40313"
SQ   SEQUENCE   248 AA;  27856 MW;  F14DA54D49E85DA4 CRC64;
     MAENGASQET TQVAKHQEVG HKSLLQSDAL YQYILETSVY PREPEPMKEL REITAKHPWN
     LMTTSADEGQ FLNMLLKLIN AKNTMEIGVY TGYSLLATAL ALPDDGKILA MDINRENYEI
     GLPVIQKAGV AHKIDFREGP ALPVLDLMVE DKSNHGTYDF IFVDADKDNY INYHKRIIEL
     VKVGGVIGYD NTLWNGSVVA PPDAPLRKYV RYYRDFVLEL NKALAADPRI EICMLPVGDG
     ITLCRRVS
 
 
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