ID   COMT3_POPKI             Reviewed;         364 AA.
AC   Q43047;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   20-JAN-2009, entry version 51.
DE   RecName: Full=Caffeic acid 3-O-methyltransferase 3;
DE            EC=2.1.1.68;
DE   AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase 1;
DE   AltName: Full=CAOMT-3;
DE            Short=COMT-3;
GN   Name=HOMT3;
OS   Populus kitakamiensis (Aspen) (Populus sieboldii x Populus
OS   grandidentata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=34292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hayakawa T., Nanto K., Kawai S., Katayama Y., Morohoshi N.;
RT   "Molecular cloning and tissue-specific expression of two genes that
RT   encode caffeic acid O-methyltransferases from Populus kitakamiensis.";
RL   Plant Sci. 113:157-165(1996).
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; D49711; BAA08559.1; -; Genomic_DNA.
DR   HSSP; P28002; 1KYZ.
DR   SMR; Q43047; 5-363.
DR   BRENDA; 2.1.1.68; 280164.
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   3: Inferred from homology;
KW   Lignin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    364       Caffeic acid 3-O-methyltransferase 3.
FT                                /FTId=PRO_0000063208.
FT   REGION      129    135       Substrate binding (By similarity).
FT   REGION      161    179       Substrate binding (By similarity).
FT   ACT_SITE    268    268       Proton acceptor (By similarity).
FT   BINDING     207    207       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     230    230       S-adenosyl-L-methionine (By similarity).
FT   BINDING     250    250       S-adenosyl-L-methionine (By similarity).
FT   BINDING     251    251       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     264    264       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   364 AA;  39576 MW;  6322956A988EE6C1 CRC64;
     MGSTGETQMS PAQILDEEAN FAMQLISSSV LPMVLKTAIE LDLLEIMAKA GPGALLSPSD
     IASHLPTKNP DAPVMLDRIL RLLASYSILI CSLRDLPDGK VERLYGLASV CKFLTKNEDG
     VSVSPLCLMN QDKVLMESWY HLKDAILEGG IPFNKAYGMT AFEYHGTDPR FNKVFNKGMS
     DHSKMAMKKI LESYKGFEGL ASLVDVGGGT GAVVSTIVSK YPSIKGINFD LPHVIADAPA
     FPGVENVGGD MFVSVPKADA VFMKWICHDW SDEHCLRLLK NCYDALPENG KVILVECILP
     VAPDTSLATK GVMHVDAIML AHNPGGKERT DKEFEGLARG AGFKGFEVMC CAFNTHVIEF
     RKQA
//