ID   COMT1_ZINVI             Reviewed;         354 AA.
AC   Q43239;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Caffeic acid 3-O-methyltransferase;
DE            Short=CAOMT;
DE            Short=COMT;
DE            EC=2.1.1.68;
DE   AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase;
OS   Zinnia violacea (Garden zinnia) (Zinnia elegans).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Zinnia.
OX   NCBI_TaxID=34245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Peter Pan;
RX   PubMed=7610157; DOI=10.1104/pp.108.2.459;
RA   Ye Z.-H., Varner J.E.;
RT   "Differential expression of two O-methyltransferases in lignin biosynthesis
RT   in Zinnia elegans.";
RL   Plant Physiol. 108:459-467(1995).
CC   -!- FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid and
CC       of 5-hydroxyferulic acid to sinapic acid. The resulting products may
CC       subsequently be converted to the corresponding alcohols that are
CC       incorporated into lignins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeate + S-adenosyl-L-methionine = (E)-ferulate + H(+) +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:20225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29749, ChEBI:CHEBI:57770, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.68;
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; U19911; AAA86718.1; -; mRNA.
DR   AlphaFoldDB; Q43239; -.
DR   SMR; Q43239; -.
DR   UniPathway; UPA00711; -.
DR   GO; GO:0047763; F:caffeate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   2: Evidence at transcript level;
KW   Lignin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..354
FT                   /note="Caffeic acid 3-O-methyltransferase"
FT                   /id="PRO_0000063214"
FT   REGION          153..171
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         121..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         222
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         242
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   354 AA;  38612 MW;  7CA613A57D2EC4D9 CRC64;
     MGSNQDDQAF LFAMQLASAS VLPMVLKTAI ELDLLETIAK AGPHGSVSSS ELVAQLPKVN
     NPEAPVMIDR ICSLLASYSV LTCTLKETAD GCAERFYGLA PVCKFLIKND AGVSLAPLLL
     MNQDKVLMES WYYLKDPVLD GGIPFNKAYG MSAFEYHGKD QRFNKVFNSG MFNHSTMTMK
     KIVELYNGFS GLKTLVDVGG GTGASLNMIT SKHKSLKGIN FDLPHVIADA TTYQGIEHVG
     GDMFESVPKG DAIFMKWILH DWSDAHCLQV LKNCYKSLPE NGKVIVAECI LPEAPDTTPA
     TQNVIHIDVI MLAHNPGGKE RTEKEFEALA KGAGFKGFNK AACALNTWVM EFCK