CAMT2_POPTR
ID CAMT2_POPTR Reviewed; 247 AA.
AC O65922;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase 2;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase 2;
DE Short=CCoAMT-2;
DE Short=CCoAOMT-2;
GN Name=CCOAOMT2;
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;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Trichobel; TISSUE=Leaf;
RA Chen C., Ardiles-Diaz W., van Montagu M., Boerjan W.;
RT "A poplar gene for caffeoyl-coenzyme A 3-O-methyltransferase.";
RL (er) Plant Gene Register PGR99-085(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 -!- 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; AJ224895; CAA12199.1; -; mRNA.
DR EMBL; AJ224896; CAA12200.1; -; mRNA.
DR EMBL; AJ223620; CAA11495.1; -; Genomic_DNA.
DR RefSeq; XP_002298729.1; XM_002298693.2.
DR AlphaFoldDB; O65922; -.
DR SMR; O65922; -.
DR STRING; 3694.POPTR_0001s31220.1; -.
DR EnsemblPlants; PNT57516; PNT57516; POPTR_001G304800v3.
DR GeneID; 7492044; -.
DR Gramene; PNT57516; PNT57516; POPTR_001G304800v3.
DR KEGG; pop:7492044; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR OMA; KYVLYYR; -.
DR BRENDA; 2.1.1.104; 4982.
DR UniPathway; UPA00711; -.
DR ExpressionAtlas; O65922; 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 2"
FT /id="PRO_0000165694"
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; 27953 MW; DE70345B1ED45C21 CRC64;
MAANGEEQQT QAGRHQEVGH KSLLQSDALY QYILETSVYP REPECMKELR ELTAKHPWNI
MTTSADEGQF LNMLLKLINA KNTMEIGVFT GYSLLATALA IPEDGKILAM DINRENYELG
LPVIQKAGLE HKIEFKEGPA LPVLDQMIED GKYHGTYDFI FVDADKDNYI NYHKRLIELV
KVGGLIGYDN TLWNGSVVAP ADAPMRKYVR YYRDFVLELN KALAADPRIE ICMLPVGDGI
TLCRRIK
