ID   COMT1_EUCGU             Reviewed;         366 AA.
AC   P46484;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 82.
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;
GN   Name=OMT;
OS   Eucalyptus gunnii (Cider gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=3933;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Xylem;
RX   PubMed=8066135; DOI=10.1104/pp.105.2.749;
RA   Poeydomenge O., Boudet A.M., Grima-Pettenati J.;
RT   "A cDNA encoding S-adenosyl-L-methionine:caffeic acid 3-O-methyltransferase
RT   from Eucalyptus.";
RL   Plant Physiol. 105:749-750(1994).
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; X74814; CAA52814.1; -; mRNA.
DR   PIR; S40146; S40146.
DR   AlphaFoldDB; P46484; -.
DR   SMR; P46484; -.
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..366
FT                   /note="Caffeic acid 3-O-methyltransferase"
FT                   /id="PRO_0000063202"
FT   REGION          163..181
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         131..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   366 AA;  39914 MW;  6B2385C3085AFABA CRC64;
     MGSTGSETQM TPTQVSDEEA NLFAMQLASA SVLPMVLKAA IELDLLEIMA KAGPGAFLSP
     GEVAAQLPTQ NPEAPVMLDR IFRLLASYSV LTCTLRNLPD GKVERLYGLA PVCKFLVKNE
     DGVSIAALNL MNQDKILMES WYYLKDAVLE GGIPFNKAYG MTAFEYHGTD PRFNKIFNRG
     MSDHSTITMK KILETYKGFE GLETVVDVGG GTGAVLSMIV AKYPSMKGIN FDLPHVIEDA
     PPLPGVKHVG GDMFVSVPKG DAIFMKWICH DWSDDHCAKF LKNCYDALPN IGKVIVAECV
     LPVYPDTSLA TKNVIHIDCI MLAHNPGGKE RTQKEFETLA KGAGFQGFQV MCCAFGTHVM
     EFLKTA