CAMT2_TOBAC
ID CAMT2_TOBAC Reviewed; 242 AA.
AC O24149;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 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; TISSUE=Leaf;
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 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. Methylates 5-hydroxyferulolyl-CoA more
CC efficiently than caffeoyl-CoA.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
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 -!- 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; U62734; AAC49914.1; -; mRNA.
DR PIR; T03796; T03796.
DR RefSeq; XP_016466601.1; XM_016611115.1.
DR AlphaFoldDB; O24149; -.
DR SMR; O24149; -.
DR GeneID; 107789329; -.
DR KEGG; nta:107789329; -.
DR OMA; AICAMTV; -.
DR OrthoDB; 1116724at2759; -.
DR BRENDA; 2.1.1.104; 3645.
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 2: Evidence at transcript level;
KW Lignin biosynthesis; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..242
FT /note="Caffeoyl-CoA O-methyltransferase 2"
FT /id="PRO_0000165698"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
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"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 242 AA; 27263 MW; A900B71449010671 CRC64;
MATNGENGRH QEVGHKSLLQ SDALYQYILE TSVYPREPEP MKELREITAK HPWNLMTTSA
DEGQFLSMLL KLINAKNTME IGVFTGYSLL ATAMALPDDG KILAMDINRE NYEIGLPIIE
KAGLAHKIVF REGPALPVLD QMIEDGKYHG SYDFIFVDAD KDNYLNYHKR LIDLVKVGGL
IGYDNTLWNG SVVAPPDAPL RKYVRYYRDF VLELNKALAA DSRIEICQLP VGDGITLCRR
IS
