ID   CAMT_PINPS              Reviewed;          24 AA.
AC   P81081;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Probable 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;
DE   AltName: Full=Water stress-responsive protein 13;
DE   Flags: Fragments;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=9747804; DOI=10.1023/a:1006006132120;
RA   Costa P., Bahrman N., Frigerio J.-M., Kremer A., Plomion C.;
RT   "Water-deficit-responsive proteins in maritime pine.";
RL   Plant Mol. Biol. 38:587-596(1998).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=10344291;
RX   DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA   Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA   Frigerio J.-M., Plomion C.;
RT   "Separation and characterization of needle and xylem maritime pine
RT   proteins.";
RL   Electrophoresis 20:1098-1108(1999).
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   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.2,
CC       its MW is: 30 kDa.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P81081; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lignin biosynthesis; Metal-binding;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           <1..>24
FT                   /note="Probable caffeoyl-CoA O-methyltransferase"
FT                   /id="PRO_0000165689"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         24
SQ   SEQUENCE   24 AA;  2447 MW;  AABE842F9EEB0CF0 CRC64;
     VGGLIAYDNI EISQIPVGDG VTLC