ID   COMT1_CAPCH             Reviewed;         359 AA.
AC   O81646;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=COMT;
OS   Capsicum chinense (Scotch bonnet) (Bonnet pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=80379;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Habanero;
RA   Curry J., Mendoza M., O'Connell M.;
RT   "Nucleotide sequence of a caffeic acid 3-O-methyltransferase gene from
RT   Habanero Chile.";
RL   (er) Plant Gene Register PGR98-170(1998).
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; AF081214; AAC78475.1; -; mRNA.
DR   AlphaFoldDB; O81646; -.
DR   SMR; O81646; -.
DR   BioCyc; MetaCyc:MON-13528; -.
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..359
FT                   /note="Caffeic acid 3-O-methyltransferase"
FT                   /id="PRO_0000063197"
FT   REGION          158..176
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         126..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         247
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   359 AA;  39636 MW;  4A836904EF6D7119 CRC64;
     MGSINQSLTQ TEDEAFVFAM QLASASVLPM VLKATVELDL LEIMAKSGPG AFISPSELAA
     QLPTKNPEAP VMLDRMFRLL ATYSVLNCTL RTLPDGRVER LYSLAPVCKF LTKNGDGVSI
     APILLMNQDK VLMESWYHLT DAVLDGGVPF NKAYGMTTFE YHGTDPRFNK VFNCGMSDHT
     TLSMKKILED YTGFEGLNSI VDVGGGTGAT VNMIVSKYPS IKGINFDLPH VIRDAPSYPG
     VEQVGGDMFV SVPKADAIFM KWICHDWSDD HCIKLLKNCY EALPANGKVI IVECILPEAP
     DTSAATKSKV HGDIIMLAHN PGGKERTEKD FEALANWGWF SRFRKVCCAY HTWVMEFNK