CAMT_PETCR
ID CAMT_PETCR Reviewed; 241 AA.
AC P28034;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE Short=CCoAMT;
DE Short=CCoAOMT;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1894629; DOI=10.1016/s0021-9258(19)47389-4;
RA Schmitt D., Pakusch A.-E., Matern U.;
RT "Molecular cloning, induction and taxonomic distribution of caffeoyl-CoA 3-
RT O-methyltransferase, an enzyme involved in disease resistance.";
RL J. Biol. Chem. 266:17416-17423(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=9037150; DOI=10.1023/a:1005780529457;
RA Grimmig B., Matern U.;
RT "Structure of the parsley caffeoyl-CoA O-methyltransferase gene, harbouring
RT a novel elicitor responsive cis-acting element.";
RL Plant Mol. Biol. 33:323-341(1997).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=16667940; DOI=10.1104/pp.95.1.137;
RA Pakusch A.-E., Matern U., Schiltz E.;
RT "Elicitor-inducible caffeoyl-coenzyme A 3-O-methyltransferase from
RT Petroselinum crispum cell suspensions.";
RL Plant Physiol. 95:137-143(1991).
CC -!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
CC hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of
CC feruloylated polysaccharides. Involved in the reinforcement of the
CC plant cell wall. Also involved in the responding to wounding or
CC pathogen challenge by the increased formation of cell wall-bound
CC ferulic acid polymers.
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 -!- 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 -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Roots and leaves.
CC -!- INDUCTION: By infection, plant wounding, or elicitor treatment of cell
CC cultures.
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; M69184; AAA33851.1; -; mRNA.
DR EMBL; Z54183; CAA90894.1; -; Genomic_DNA.
DR EMBL; Z33878; CAA83943.1; -; Genomic_DNA.
DR PIR; S49342; A40975.
DR AlphaFoldDB; P28034; -.
DR SMR; P28034; -.
DR UniPathway; UPA00711; -.
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:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Direct protein sequencing; Lignin biosynthesis; Metal-binding;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..241
FT /note="Caffeoyl-CoA O-methyltransferase"
FT /id="PRO_0000165688"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 81..82
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 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 183
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 184
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT MOD_RES 1
FT /note="Blocked amino end (Met)"
SQ SEQUENCE 241 AA; 27096 MW; B6A07E4A038418F7 CRC64;
MASNGESKHS EVGHKSLLQS DALYQYILET SVYPREPEAM KELREVTAKH PWNLMTTSAD
EGQFLNMLLK LINAKNTMEI GVYTGYSLLA TALALPDDGK ILAMDINREN YEIGLPIIEK
AGVGHKIDFR EGPALPVLDH MLEDGKYHGT FDFVFVDADK DNYINYHKRL IDLVKIGGLI
GYDNTLWNGS VAQPADAPMR KYVRYYRDFV IELNKALAAD PRIEICMLPV GDGVTLCRRI
S
