CAMT_VITVI
ID CAMT_VITVI Reviewed; 242 AA.
AC Q43237;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9390437; DOI=10.1104/pp.115.3.1039;
RA Busam G., Junghanns K.T., Kneusel R.E., Kassemeyer H.H., Matern U.;
RT "Characterization and expression of caffeoyl-coenzyme A 3-O-
RT methyltransferase proposed for the induced resistance response of Vitis
RT vinifera L.";
RL Plant Physiol. 115:1039-1048(1997).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z54233; CAA90969.1; -; mRNA.
DR RefSeq; NP_001268047.1; NM_001281118.1.
DR AlphaFoldDB; Q43237; -.
DR SMR; Q43237; -.
DR STRING; 29760.VIT_03s0063g00140.t01; -.
DR PRIDE; Q43237; -.
DR GeneID; 100233087; -.
DR KEGG; vvi:100233087; -.
DR eggNOG; KOG1663; Eukaryota.
DR OrthoDB; 1116724at2759; -.
DR BRENDA; 2.1.1.104; 6671.
DR UniPathway; UPA00711; -.
DR ExpressionAtlas; Q43237; baseline and differential.
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 2: Evidence at transcript level;
KW Lignin biosynthesis; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..242
FT /note="Caffeoyl-CoA O-methyltransferase"
FT /id="PRO_0000165703"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 82..83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 242 AA; 27234 MW; 6BBAA5E5BBE65F2A CRC64;
MATNQEAGRH QEVGHKSLLQ SDALYQYILE TSVYPREPES MKELRELTAQ HPWNIMTTSA
DEGQFLNMLL KLINAKNTME IGVYTGYSLL ATALALPDDG KILAMDINKE NYELGLPVIQ
KAGVAHKIDF KEGPALPVLD QMIEDGKYHG SFDFIFVDAD KDNYLNYHKR LIDLVKVGGI
IGYDNTLWNG SVVAPPDAPL RKYVRYYRDF VLELNKALAA DPRIEICMLP VGDGITLCRR
LS
