COMT1_CAPAN
ID COMT1_CAPAN Reviewed; 359 AA.
AC Q9FQY8; P93088;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 81.
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 annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pericarp;
RA Lee B.-H., Choi D., Lee K.-W.;
RT "Isolation and characterization of o-diphenol-O-methyltransferase cDNA
RT clone in hot pepper (Capsicum annuum L.).";
RL J. Plant Biol. 41:9-14(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chungyang; TISSUE=Root;
RA Kim K.-W., Lee S.-W.;
RT "Isolation and characterization of caffeic acid O-methyltransferase cDNA
RT from Capsicum annuum.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Fruit. Not expressed in leaf.
CC -!- DEVELOPMENTAL STAGE: Expression increases during fruit development but
CC decreases during ripening.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U83789; AAC17455.1; -; mRNA.
DR EMBL; AF212316; AAG43822.1; -; mRNA.
DR PIR; T12259; T12259.
DR RefSeq; NP_001311774.1; NM_001324845.1.
DR AlphaFoldDB; Q9FQY8; -.
DR SMR; Q9FQY8; -.
DR GeneID; 107862991; -.
DR KEGG; cann:107862991; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000189700; Genome assembly.
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_0000063196"
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"
FT CONFLICT 71
FT /note="V -> I (in Ref. 2; AAG43822)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="R -> G (in Ref. 2; AAG43822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39433 MW; 70599AED75CE1730 CRC64;
MDSTNQNLTQ TEDEAFLFAM QLASASVLPM VLKSALELDL LEIMAKAGPG AAISPSELAA
QLPTKNPEAP VMLDRMLRLL ATYSVLNCTL RTLPDGRVER LYSLAPVCKL LTKNADGVSV
APLLLMNQDK VLMESWYHLT DAVLDGGVPF NKAYGMTAFE YHGTDPRFNK VFNRGMSDHS
TMTMKKILED YKGFEGLNSI VDVGGGTGAT VNMIVSKYPS IKGINFDLSH VIEDAPAYPG
VEHVGRDMFV SVPKADAIFM KWICHDWSDE HCLKFLKNCY EALPANGKVL VAECILPETP
DTSAATKNAV HVDIVMLAHN PGGKERTEKE FEALAKGAGF TGFRRACCAY QTWVMEFHK
