ID   COMT1_COFCA             Reviewed;         350 AA.
AC   Q8LL87; Q8LL88;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   20-JAN-2009, entry version 35.
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;
OS   Coffea canephora (Robusta coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Coffeeae;
OC   Coffea.
OX   NCBI_TaxID=49390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit, and Leaf;
RA   Campa C., Legal L., Khounlotham M., Noirot M., de Kochko A.;
RT   "Complete cDNA sequence of a caffeic acid O-methyltransferase from
RT   Coffea canephora fruit.";
RL   Submitted (DEC-2001) 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   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type 2
CC       family. COMT subfamily.
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DR   EMBL; AF454631; AAN03726.1; -; mRNA.
DR   EMBL; AF454632; AAN03727.1; -; mRNA.
DR   HSSP; P28002; 1KYZ.
DR   SMR; Q8LL87; 1-350.
DR   BRENDA; 2.1.1.68; 275282.
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    350       Caffeic acid 3-O-methyltransferase.
FT                                /FTId=PRO_0000063200.
FT   REGION      117    123       Substrate binding (By similarity).
FT   REGION      149    167       Substrate binding (By similarity).
FT   ACT_SITE    256    256       Proton acceptor (By similarity).
FT   BINDING     195    195       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     218    218       S-adenosyl-L-methionine (By similarity).
FT   BINDING     238    238       S-adenosyl-L-methionine (By similarity).
FT   BINDING     239    239       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     252    252       S-adenosyl-L-methionine (By similarity).
FT   CONFLICT    230    230       S -> P (in Ref. 1; AAN03726).
FT   CONFLICT    268    268       K -> R (in Ref. 1; AAN03726).
SQ   SEQUENCE   350 AA;  38258 MW;  D6AC10007BDF8E6B CRC64;
     MAEEEACLFA MSLASASVLP MVLKSAIELD LLELIAKAGP GAYVSPSELA AQLPTHNPEA
     PIMLDRILRL LATYSVLDCK LNNLADGGVE RLYGLAPVCK FLTKNADGVS MAPLLLMNQD
     KVLMESWYHL KDAVLDGGIP FNKAYGMTAF EYHGTDPRFN KVFNQGMSNH STITMKKILE
     VYRGFEGLKT VVDVGGGTGA TLNMIISKYP TIKGINFELP HVVEDAPSHS GVEHVGGDMF
     VSVPKGDAIF MKWICHDWSD DHCRKLLKNC YQALPDNGKV ILAECVLPEA PDTSLATQNV
     VHVDVVMLAH NPGGKERTEK EFEALAKGAG FKEFRKVCSA VNTWIMELCK
//