ID   COMT2_OCIBA             Reviewed;         361 AA.
AC   Q9XGV9;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Caffeic acid 3-O-methyltransferase 2;
DE            Short=CAOMT-2;
DE            Short=COMT-2;
DE            EC=2.1.1.68;
DE   AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase 2;
GN   Name=COMT2;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. EMX-1;
RA   Wang J., Dudareva N., Kish C.M., Simon J.E., Lewinsohn E., Pichersky E.;
RT   "Nucleotide sequences of two cDNAs encoding caffeic acid O-
RT   methyltransferases from sweet basil (Ocimum basilicum).";
RL   (er) Plant Gene Register PGR99-105(1999).
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; AF154918; AAD38190.1; -; mRNA.
DR   AlphaFoldDB; Q9XGV9; -.
DR   SMR; Q9XGV9; -.
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..361
FT                   /note="Caffeic acid 3-O-methyltransferase 2"
FT                   /id="PRO_0000063206"
FT   REGION          160..178
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         128..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         250
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   361 AA;  39613 MW;  4B8CA0825E6B65D0 CRC64;
     MSSTANNPQI NSDEEENFLF AMQLASASVL PMVLKSAIEL DLLELIKKAG AGAFVSPAEL
     AAQLLTTNAE AHVMLDRILR LLTSYAILEC RLKTLPDGGV QRLYGLAPVC KFLTKNEDGV
     SMAPLALMNQ DKVLMESWYH LKDAVLDGGI PFNKAYGMTA FEYHGTDPRF NKVFNQGMSN
     HSTITMKKIL ETYTGFDGLK TVVDVGGGTG ATLNMIISKY PSIKGINFDL PHVVEDAPSY
     PGVEHVGGDM FVSVPKGDAI FMKWICHDWS DAHCVKFLKK CYEALPENGK VILAECVLPE
     APDTGLATKN VVHIDVIMLA HNPGGKERTE KEFQVLAKAS GFKQFNKVCC AYNSWIMELL
     K