CAMT_STELP
ID CAMT_STELP Reviewed; 241 AA.
AC Q43161;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Stellaria longipes (Longstalk starwort) (Alsine longipes).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Alsineae; Stellaria.
OX NCBI_TaxID=19744;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf, and Stem;
RX PubMed=7784517; DOI=10.1104/pp.108.1.429;
RA Zhang X.-H., Dickson E.E., Chinnappa C.C.;
RT "Nucleotide sequence of a cDNA clone encoding caffeoyl-coenzyme A 3-O-
RT methyltransferase of Stellaria longipes (Caryophyllaceae).";
RL Plant Physiol. 108:429-430(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf, and Stem;
RA Zhang X.-H., Chinnappa C.C.;
RT "Molecular characterization of a cDNA encoding caffeoyl-coenzyme A 3-O-
RT methyltransferase of Stellaria longipes.";
RL J. Biosci. 22:161-175(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}.
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DR EMBL; L22203; AAB61680.1; -; mRNA.
DR AlphaFoldDB; Q43161; -.
DR SMR; Q43161; -.
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 2: Evidence at transcript level;
KW Lignin biosynthesis; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..241
FT /note="Caffeoyl-CoA O-methyltransferase"
FT /id="PRO_0000165696"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 241 AA; 26725 MW; 380D0DA403F8248C CRC64;
MLTKTMGNFF TEVKDTGLLQ SEQLHQYILD TSVFPRESEH LKELRKATES HPMSFMGTSP
LAGQLLSFML KTVKPKKTIE VGVFTGYSLL ATALSIPDDG KITAVDIDRE AYNVGLALIK
KAGVESKISF IVSDAMTLLD DLLADGRYQG SYDFAFVDAD KTNYVNYHER LIELVKVGGI
IAYDNTLWGG TVALPESEVP DFMKNNWVCV TKLNEILGSD ARIDIAHLPV GDGITFCRRV
Y
