CAMT1_PETHY
ID CAMT1_PETHY Reviewed; 249 AA.
AC A0A0S2UWC9;
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 1 {ECO:0000303|PubMed:26620524};
DE Short=PhCCoAOMT1 {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=CCOAOMT1 {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, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, PATHWAY, INDUCTION BY ODO1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND BIOPHYSICOCHEMICAL PROPERTIES.
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
CC (PubMed:26620524). Methylates caffeoyl-CoA to feruloyl-CoA, also able
CC to methylate 5-hydroxyferuloyl-CoA (PubMed:26620524).
CC {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=5.8 pmol/sec/mg enzyme with (E)-caffeoyl-CoA as substrate
CC {ECO:0000269|PubMed:26620524};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:26620524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26620524}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in petal limbs and tubes, and, at
CC low levels, in flower buds, stamens, pistils, stems, roots and leaves.
CC {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: Promoted by ODO1 (PubMed:26620524). Circadian-regulation
CC with peak levels occurring in the afternoon in flowers
CC (PubMed:26620524). {ECO:0000269|PubMed:26620524}.
CC -!- DISRUPTION PHENOTYPE: Reduction of eugenol production but not of
CC isoeugenol associated with abnormally purple-colored leaves and stems
CC (e.g. especially in vascular bundles), and pink flowers due to the
CC accumulation of anthocyanins (e.g. petunidin, delphinidin, malvidin and
CC peonidin); purple floral buds and pink blush upon petals opening that
CC fade in older flowers (PubMed:26620524). Disturbed CoA esters
CC homeostasis and reduced lignin levels, but accumulation of anthocyanins
CC associated with perturbated biosynthetic gene expression
CC (PubMed:26620524). {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; KT223506; ALP75646.1; -; mRNA.
DR AlphaFoldDB; A0A0S2UWC9; -.
DR SMR; A0A0S2UWC9; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0080076; F:caffeoyl CoA:S-adenosyl-L-methionine O-methyltransferase activity; IDA: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:0010597; P:green leaf volatile biosynthetic process; IMP: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; IDA: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..249
FT /note="Caffeoyl-CoA O-methyltransferase 1"
FT /id="PRO_0000451494"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 89..90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 192
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 249 AA; 28090 MW; 3D183D4E669C79A4 CRC64;
MAENGAAVQE NQNVIRHQEV GHKSLLQSDA LYQYILETSV YPREPESMKE LRELTAKHPW
NLMTTSADEG QFLNMLLKLI NAKNTMEIGV YTGYSLLATA LAIPHDGKIL AMDINRENYE
IGLPVIEKAG VAHKIDFREG PALPVLDQLV EDKNNHGTYD FIFVDADKDN YINYHKRIID
LVKVGGLIGY DNTLWNGSLV APADTPMRKY VRYYRDFILE LNKALAADPR IEICMLPVGD
GITLGRRIS
