ID   COMT1_ZINEL             Reviewed;         354 AA.
AC   Q43239;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   20-JAN-2009, entry version 50.
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   Zinnia elegans (Zinnia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae; Zinnia.
OX   NCBI_TaxID=34245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Peter Pan;
RX   MEDLINE=95334486; PubMed=7610157; DOI=10.1104/pp.108.2.459;
RA   Ye Z.-H., Varner J.E.;
RT   "Differential expression of two O-methyltransferases in lignin
RT   biosynthesis in Zinnia elegans.";
RL   Plant Physiol. 108:459-467(1995).
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; U19911; AAA86718.1; -; mRNA.
DR   HSSP; P28002; 1KYZ.
DR   BRENDA; 2.1.1.68; 228834.
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    354       Caffeic acid 3-O-methyltransferase.
FT                                /FTId=PRO_0000063214.
FT   REGION      121    127       Substrate binding (By similarity).
FT   REGION      153    171       Substrate binding (By similarity).
FT   ACT_SITE    260    260       Proton acceptor (By similarity).
FT   BINDING     199    199       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     222    222       S-adenosyl-L-methionine (By similarity).
FT   BINDING     242    242       S-adenosyl-L-methionine (By similarity).
FT   BINDING     243    243       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     256    256       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   354 AA;  38612 MW;  7CA613A57D2EC4D9 CRC64;
     MGSNQDDQAF LFAMQLASAS VLPMVLKTAI ELDLLETIAK AGPHGSVSSS ELVAQLPKVN
     NPEAPVMIDR ICSLLASYSV LTCTLKETAD GCAERFYGLA PVCKFLIKND AGVSLAPLLL
     MNQDKVLMES WYYLKDPVLD GGIPFNKAYG MSAFEYHGKD QRFNKVFNSG MFNHSTMTMK
     KIVELYNGFS GLKTLVDVGG GTGASLNMIT SKHKSLKGIN FDLPHVIADA TTYQGIEHVG
     GDMFESVPKG DAIFMKWILH DWSDAHCLQV LKNCYKSLPE NGKVIVAECI LPEAPDTTPA
     TQNVIHIDVI MLAHNPGGKE RTEKEFEALA KGAGFKGFNK AACALNTWVM EFCK
//