CAMT5_TOBAC
ID CAMT5_TOBAC Reviewed; 240 AA.
AC O04899; O22546;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase 5;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase 5;
DE Short=CCoAMT-5;
DE Short=CCoAOMT-5;
GN Name=CCOAOMT5;
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.
RC STRAIN=cv. Samsun NN;
RA Busam G., Grimmig B., Kneusel R.E., Matern U.;
RT "Isolation of tobacco cDNAs encoding caffeoyl-CoA 3-O-methyltransferase.";
RL (er) Plant Gene Register PGR97-039(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Samsun NN; TISSUE=Stem;
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: Expression steadily increases from the bottom to
CC the top of the plant. {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}.
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; Z82982; CAB05369.1; -; Transcribed_RNA.
DR EMBL; AF022775; AAB80931.1; -; mRNA.
DR PIR; T04084; T04084.
DR RefSeq; NP_001311999.1; NM_001325070.1.
DR AlphaFoldDB; O04899; -.
DR SMR; O04899; -.
DR STRING; 4097.O04899; -.
DR GeneID; 107770611; -.
DR KEGG; nta:107770611; -.
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..240
FT /note="Caffeoyl-CoA O-methyltransferase 5"
FT /id="PRO_0000165701"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 80..81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 183
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT CONFLICT 218
FT /note="A -> V (in Ref. 2; AAB80931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27142 MW; 468F3A375CDFA8D0 CRC64;
MAENGIKHQE VGHKSLLQSD ALYQYILETS VYPREPESMK ELREVTAKHP WNLMTTSADE
GQFLNMLLKL INAKNTMEIG VYTGYSLLAT ALAIPDDGKI LAMDINRENY EIGLPIIEKA
GVAHKIEFRE GPALPVLDQL VEDKKNHGTY DFIFVDADKD NYINYHKRII DLVKVGGLIG
YDNTLWNGSV VAPPDAPMRK YVRYYRDFVL ELNKALAADP RIEICMLPVG DGITLCRRIT
