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
