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COMT1_SACOF
ID   COMT1_SACOF             Reviewed;         362 AA.
AC   O82054;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Saccharum officinarum (Sugarcane).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum;
OC   Saccharum officinarum complex.
OX   NCBI_TaxID=4547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Jaronu 60-5; TISSUE=Root;
RA   Selman-Housein G., Lopez M., Hernandez D., Civardi L., Miranda F.,
RA   Rigau J., Puigdomenech P.;
RT   "Molecular cloning of cDNAs coding for three sugarcane enzymes involved in
RT   lignification.";
RL   Plant Sci. 143:163-171(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; AJ231133; CAA13175.1; -; mRNA.
DR   AlphaFoldDB; O82054; -.
DR   SMR; O82054; -.
DR   BRENDA; 2.1.1.68; 5522.
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; IPR022657; De-COase2_CS.
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; PS00879; ODR_DC_2_2; 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..362
FT                   /note="Caffeic acid 3-O-methyltransferase"
FT                   /id="PRO_0000063213"
FT   REGION          161..179
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         129..135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         230
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         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         264
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   362 AA;  39578 MW;  1A5C6755444E2F49 CRC64;
     MGSTAEDVAA VADEEACMYA MQLASASILP MTLKNALELG LLEVLQAEAP AGKALAPEEV
     VARLPVAPTN PDAADMVDRM LRLLASYDVV KCQMEDKDGK YERRYSAAPV GKWLTPNEDG
     VSMAALTLMN QDKVLMESWY YLKDAVLDGG IPFNKAYGMT AFEYHGTDPR FNRVFNEGMK
     NHSVIITKKL LEFYTGFEGV STLVDVGGGI GATLHAITSH HPQIKGINFD LPHVISEAPP
     FPGVQHVGGD MFKSVPAGDA ILMKWILHDW SDAHCATLLK NCYDALPENG KVIIVECVLP
     VNTEAVPKAQ GVFHVDMIML AHNPGGRERY EREFHDLAKG AGFSGFKATY IYANAWAIEF
     IK
 
 
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