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Caffeoyl-CoA O-methyltransferase 1 (EC 2.1.1.104) (Trans-caffeoyl-CoA 3-O-methyltransferase 1) (CCoAMT-1) (CCoAOMT-1)

 CAMT1_TOBAC             Reviewed;         239 AA.
O24144;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 77.
RecName: Full=Caffeoyl-CoA O-methyltransferase 1;
EC=2.1.1.104;
AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase 1;
Short=CCoAMT-1;
Short=CCoAOMT-1;
Name=CCOAOMT1;
Nicotiana tabacum (Common tobacco).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae;
Nicotianoideae; Nicotianeae; Nicotiana.
NCBI_TaxID=4097;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Samsun NN;
PubMed=9484483; DOI=10.1023/A:1005969825070;
Martz F., Maury S., Pincon G., Legrand M.;
"cDNA cloning, substrate specificity and expression study of tobacco
caffeoyl-CoA 3-O-methyltransferase, a lignin biosynthetic enzyme.";
Plant Mol. Biol. 36:427-437(1998).
[2]
MUTAGENESIS OF 1-MET--LEU-16; GLU-40; GLU-43; LYS-47; ASP-58; GLN-61;
186-ASN--ALA-191; 198-ARG-LYS-199; ARG-202 AND ARG-220.
PubMed=11459845; DOI=10.1074/jbc.M104977200;
Hoffmann L., Maury S., Bergdoll M., Thion L., Erard M., Legrand M.;
"Identification of the enzymatic active site of tobacco caffeoyl-
coenzyme A O-methyltransferase by site-directed mutagenesis.";
J. Biol. Chem. 276:36831-36838(2001).
[3]
TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND INDUCTION.
PubMed=10482677; DOI=10.1104/pp.121.1.215;
Maury S., Geoffroy P., Legrand M.;
"Tobacco O-methyltransferases involved in phenylpropanoid metabolism.
The different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-
methyltransferase and caffeic acid/5-hydroxyferulic acid 3/5-O-
methyltransferase classes have distinct substrate specificities and
expression patterns.";
Plant Physiol. 121:215-224(1999).
-!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis
of feruloylated polysaccharides. Involved in the reinforcement of
the plant cell wall. Also involved in the responding to wounding
or pathogen challenge by the increased formation of cell wall-
bound ferulic acid polymers.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + caffeoyl-CoA = S-
adenosyl-L-homocysteine + feruloyl-CoA.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) ion per subunit.;
-!- PATHWAY: Aromatic compound metabolism; phenylpropanoid
biosynthesis.
-!- SUBUNIT: Monomer.
-!- TISSUE SPECIFICITY: Mostly expressed in the bottom and middle
parts of the stems. {ECO:0000269|PubMed:10482677}.
-!- INDUCTION: By wounding and viral infection.
{ECO:0000269|PubMed:10482677}.
-!- MISCELLANEOUS: CoA moiety is essential to enzymatic activity since
free caffeic acid is not a substrate for the enzyme. The N-
terminal amino acid sequence of the protein seems to have a
particular role in the enzyme-caffeoyl-CoA interaction.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Cation-dependent O-
methyltransferase family. CCoAMT subfamily. {ECO:0000255|PROSITE-
ProRule:PRU01019}.
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EMBL; U38612; AAC49913.1; -; mRNA.
PIR; T03783; T03783.
RefSeq; NP_001312329.1; NM_001325400.1.
UniGene; Nta.3623; -.
ProteinModelPortal; O24144; -.
SMR; O24144; -.
PRIDE; O24144; -.
GeneID; 107785450; -.
KEGG; nta:107785450; -.
KO; K00588; -.
UniPathway; UPA00711; -.
Proteomes; UP000084051; Genome assembly.
GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR002935; O-MeTrfase_3.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01596; Methyltransf_3; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51682; SAM_OMT_I; 1.
1: Evidence at protein level;
Complete proteome; Lignin biosynthesis; Magnesium; Metal-binding;
Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 239 Caffeoyl-CoA O-methyltransferase 1.
/FTId=PRO_0000165697.
REGION 79 80 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
METAL 155 155 Divalent metal cation.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
METAL 181 181 Divalent metal cation.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
METAL 182 182 Divalent metal cation.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 13 13 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:Q40313}.
BINDING 55 55 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01019}.
BINDING 77 77 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 85 85 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 103 103 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 132 132 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01019}.
BINDING 155 155 Substrate.
{ECO:0000250|UniProtKB:Q40313}.
BINDING 157 157 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01019}.
BINDING 186 186 Substrate.
{ECO:0000250|UniProtKB:Q40313}.
MUTAGEN 1 16 Missing: Total loss of activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 40 40 E->Q: No effect on activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 43 43 E->S: No effect on activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 47 47 K->A: No effect on activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 58 58 D->A: Decrease of activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 61 61 Q->S: Decrease of activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 186 191 Missing: Total loss of activity.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 198 199 RK->TT: No effect on activity; when
associated with T-202.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 202 202 R->T: No effect on activity; when
associated with 198-TT-199.
{ECO:0000269|PubMed:11459845}.
MUTAGEN 220 220 R->T: Total loss of activity.
{ECO:0000269|PubMed:11459845}.
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


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