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   20-JAN-2009, entry version 40.
DE   RecName: Full=Caffeic acid 3-O-methyltransferase;
DE            EC=2.1.1.68;
DE   AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase;
DE            Short=CAOMT;
DE            Short=COMT;
GN   Name=COMT;
OS   Capsicum annuum (Bell pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae;
OC   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-methyltrasferase
RT   cDNA from Capsicum annuum.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid
CC       and of 5-hydroxyferulic acid to sinapic acid. The resulting
CC       products may subsequently be converted to the corresponding
CC       alcohols that are incorporated into lignins.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3,4-dihydroxy-trans-
CC       cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-
CC       cinnamate.
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: Fruit. Not expressed in leaf.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during fruit development
CC       but decreases during ripening.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type 2
CC       family. COMT subfamily.
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DR   EMBL; U83789; AAC17455.1; -; mRNA.
DR   EMBL; AF212316; AAG43822.1; -; mRNA.
DR   PIR; T12259; T12259.
DR   HSSP; P28002; 1KYZ.
DR   SMR; Q9FQY8; 11-359.
DR   BRENDA; 2.1.1.68; 1261.
DR   GO; GO:0047763; F:caffeate O-methyltransferase activity; IEA:EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016461; O-MeTrfase_COMT_euk.
DR   InterPro; IPR001077; O_MeTrfase_2.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
PE   2: Evidence at transcript level;
KW   Lignin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    359       Caffeic acid 3-O-methyltransferase.
FT                                /FTId=PRO_0000063196.
FT   REGION      126    132       Substrate binding (By similarity).
FT   REGION      158    176       Substrate binding (By similarity).
FT   ACT_SITE    265    265       Proton acceptor (By similarity).
FT   BINDING     204    204       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     227    227       S-adenosyl-L-methionine (By similarity).
FT   BINDING     247    247       S-adenosyl-L-methionine (By similarity).
FT   BINDING     248    248       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     261    261       S-adenosyl-L-methionine (By similarity).
FT   CONFLICT     71     71       V -> I (in Ref. 2; AAG43822).
FT   CONFLICT    246    246       R -> G (in Ref. 2; AAG43822).
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
//