CAMT1_POPTR
ID CAMT1_POPTR Reviewed; 247 AA.
AC O65862;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase 1;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase 1;
DE Short=CCoAMT-1;
DE Short=CCoAOMT-1;
GN Name=CCOAOMT1;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Trichobel; TISSUE=Xylem;
RA Meyermans H., Ardiles-Diaz W., van Montagu M., Boerjan W.;
RT "The cDNA cloning and expression study of caffeoyl-CoA 3-O-
RT methyltransferase in poplar.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Trichobel; TISSUE=Leaf;
RA Chen C., Meyermans H., Van Doorsselaere J., van Montagu M., Boerjan W.;
RT "A gene encoding caffeoyl coenzyme A 3-O-methyltransferase (CCoAOMT) from
RT Populus trichocarpa.";
RL (er) Plant Gene Register PGR98-104(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 65-247.
RC STRAIN=cv. Trichbobel; TISSUE=Xylem;
RX PubMed=10934215; DOI=10.1074/jbc.m006915200;
RA Meyermans H., Morreel K., Lapierre C., Pollet B., De Bruyn A., Busson R.,
RA Herdewijn P., Devreese B., Van Beeumen J., Marita J.M., Ralph J., Chen C.,
RA Burggraeve B., Van Montagu M., Messens E., Boerjan W.;
RT "Modifications in lignin and accumulation of phenolic glucosides in poplar
RT xylem upon down-regulation of caffeoyl-coenzyme A O-methyltransferase, an
RT enzyme involved in lignin biosynthesis.";
RL J. Biol. Chem. 275:36899-36909(2000).
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; AJ224894; CAA12198.1; -; mRNA.
DR EMBL; AJ223621; CAA11496.1; -; Genomic_DNA.
DR EMBL; AJ130841; CAA10217.1; -; mRNA.
DR RefSeq; XP_002313125.1; XM_002313089.2.
DR AlphaFoldDB; O65862; -.
DR SMR; O65862; -.
DR STRING; 3694.POPTR_0009s10270.1; -.
DR EnsemblPlants; PNT20575; PNT20575; POPTR_009G099800v3.
DR EnsemblPlants; PNT20577; PNT20577; POPTR_009G099800v3.
DR GeneID; 7457542; -.
DR Gramene; PNT20575; PNT20575; POPTR_009G099800v3.
DR Gramene; PNT20577; PNT20577; POPTR_009G099800v3.
DR KEGG; pop:7457542; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR BRENDA; 2.1.1.104; 4982.
DR UniPathway; UPA00711; -.
DR ExpressionAtlas; O65862; 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..247
FT /note="Caffeoyl-CoA O-methyltransferase 1"
FT /id="PRO_0000165693"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 87..88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 190
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 247 AA; 27807 MW; 9E2C633378E2074B CRC64;
MATNGEEQQS QAGRHQEVGH KSLLQSDALY QYILETSVYP REPECMKELR EVTAKHPWNI
MTTSADEGQF LNMLLKLVNA KNTMEIGVYT GYSLLATALA IPEDGKILAM DINRENYELG
LPVIQKAGVA HKIDFKEGPA LPVLDQMIED GKCHGSFDFI FVDADKDNYI NYHKRLIELV
KVGGLIGYDN TLWNGSVVAP PDAPMRKYVR YYRDFVLELN KALAADPRIE ICMLPVGDGI
TLCRRIQ
