COMT1_MAIZE
ID COMT1_MAIZE Reviewed; 364 AA.
AC Q06509;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
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;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1463825; DOI=10.1007/bf00027157;
RA Collazo P., Montoliu L., Puigdomenech P., Rigau J.;
RT "Structure and expression of the lignin O-methyltransferase gene from Zea
RT mays L.";
RL Plant Mol. Biol. 20:857-867(1992).
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 -!- 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}.
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DR EMBL; M73235; AAB03364.1; -; Genomic_DNA.
DR PIR; S28612; S28612.
DR AlphaFoldDB; Q06509; -.
DR SMR; Q06509; -.
DR STRING; 4577.AC196475.3_FGP004; -.
DR PaxDb; Q06509; -.
DR PRIDE; Q06509; -.
DR MaizeGDB; 26027; -.
DR eggNOG; KOG3178; Eukaryota.
DR BRENDA; 2.1.1.68; 6752.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q06509; baseline and differential.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0047763; F:caffeate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030744; F:luteolin O-methyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0051555; P:flavonol biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR022657; De-COase2_CS.
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 3: Inferred from homology;
KW Lignin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..364
FT /note="Caffeic acid 3-O-methyltransferase"
FT /id="PRO_0000063203"
FT REGION 163..181
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 131..137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 364 AA; 39567 MW; 089E8A6A4DDAF56A CRC64;
MGSTAGDVAA VVDEEACMYA MQLASSSILP MTLKNAIELG LLEVLQKEAG GGKAALAPEE
VVARMPAAPS DPAAAAAMVD RMLRLLASYD VVRCQMEDRD GRYERRYSAA PVCKWLTPNE
DGVSMAALAL MNQDKVLMES WYYLKDAVLD GGIPFNKAYG MTAFEYHGTD ARFNRVFNEG
MKNHSVIITK KLLDFYTGFE GVSTLVDVGG GVGATLHAIT SRHPHISGVN FDLPHVISEA
PPFPGVRHVG GDMFASVPAG DAILMKWILH DWSDAHCATL LKNCYDALPE NGKVIVVECV
LPVNTEATPK AQGVFHVDMI MLAHNPGGKE RYEREFRELA KGAGFSGFKA TYIYANAWAI
EFIK
