CAMT1_TOBAC
ID CAMT1_TOBAC Reviewed; 239 AA.
AC O24144;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN;
RX PubMed=9484483; DOI=10.1023/a:1005969825070;
RA Martz F., Maury S., Pincon G., Legrand M.;
RT "cDNA cloning, substrate specificity and expression study of tobacco
RT caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme.";
RL Plant Mol. Biol. 36:427-437(1998).
RN [2]
RP MUTAGENESIS OF 1-MET--LEU-16; GLU-40; GLU-43; LYS-47; ASP-58; GLN-61;
RP 186-ASN--ALA-191; 198-ARG-LYS-199; ARG-202 AND ARG-220.
RX PubMed=11459845; DOI=10.1074/jbc.m104977200;
RA Hoffmann L., Maury S., Bergdoll M., Thion L., Erard M., Legrand M.;
RT "Identification of the enzymatic active site of tobacco caffeoyl-coenzyme A
RT O-methyltransferase by site-directed mutagenesis.";
RL J. Biol. Chem. 276:36831-36838(2001).
RN [3]
RP TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND INDUCTION.
RX PubMed=10482677; DOI=10.1104/pp.121.1.215;
RA Maury S., Geoffroy P., Legrand M.;
RT "Tobacco O-methyltransferases involved in phenylpropanoid metabolism. The
RT different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-
RT methyltransferase and caffeic acid/5-hydroxyferulic acid 3/5-O-
RT methyltransferase classes have distinct substrate specificities and
RT expression patterns.";
RL Plant Physiol. 121:215-224(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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- TISSUE SPECIFICITY: Mostly expressed in the bottom and middle parts of
CC the stems. {ECO:0000269|PubMed:10482677}.
CC -!- INDUCTION: By wounding and viral infection.
CC {ECO:0000269|PubMed:10482677}.
CC -!- MISCELLANEOUS: CoA moiety is essential to enzymatic activity since free
CC caffeic acid is not a substrate for the enzyme. The N-terminal amino
CC acid sequence of the protein seems to have a particular role in the
CC enzyme-caffeoyl-CoA interaction.
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; U38612; AAC49913.1; -; mRNA.
DR PIR; T03783; T03783.
DR RefSeq; NP_001312329.1; NM_001325400.1.
DR AlphaFoldDB; O24144; -.
DR SMR; O24144; -.
DR GeneID; 107785450; -.
DR KEGG; nta:107785450; -.
DR OMA; FLGRWCP; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000084051; Unplaced.
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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Lignin biosynthesis; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..239
FT /note="Caffeoyl-CoA O-methyltransferase 1"
FT /id="PRO_0000165697"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 79..80
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 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 181
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 182
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT MUTAGEN 1..16
FT /note="Missing: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 40
FT /note="E->Q: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 43
FT /note="E->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 47
FT /note="K->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 58
FT /note="D->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 61
FT /note="Q->S: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 186..191
FT /note="Missing: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 198..199
FT /note="RK->TT: No effect on activity; when associated with
FT T-202."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 202
FT /note="R->T: No effect on activity; when associated with
FT 198-TT-199."
FT /evidence="ECO:0000269|PubMed:11459845"
FT MUTAGEN 220
FT /note="R->T: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:11459845"
SQ SEQUENCE 239 AA; 26965 MW; 89839F5F9F544783 CRC64;
MATNGRHQEV GHKSLLQSDA LYQYILETSV YPREPEPMKE LREITAKHPW NLMTTSADEG
QFLSMLIKLI NAKNTMEIGV FTGYSLLATA MALPDDGKIL AMDINRENYE IGLPVIEKAG
LAHKIEFKEG PALPVLDQMI EDGKYHGSYD FIFVDADKDN YLNYHKRLID LVKIGGLIGY
DNTLWNGSVV APPDAPLRKY VRYYRDFVLE LNKALAADSR IEICQLPVGD GITLCRRIS
