ID COMT1_COFCA Reviewed; 350 AA.
AC Q8LL87; A0A068U9K4; Q8LL88;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Caffeic acid 3-O-methyltransferase {ECO:0000305};
DE Short=CAOMT {ECO:0000305};
DE EC=2.1.1.68 {ECO:0000305};
DE AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase {ECO:0000305};
GN Name=COMT {ECO:0000303|Ref.1};
GN ORFNames=GSCOC_T00019870001 {ECO:0000312|EMBL:CDP04982.1};
OS Coffea canephora (Robusta coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; 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 Coffea
RT canephora fruit.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH200-94;
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
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. {ECO:0000250|UniProtKB:P28002}.
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 Evidence={ECO:0000250|UniProtKB:P28002};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20226;
CC Evidence={ECO:0000250|UniProtKB:P28002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-5-hydroxyferulate + S-adenosyl-L-methionine = (E)-sinapate
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60952,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30023, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:144381;
CC Evidence={ECO:0000250|UniProtKB:P28002};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60953;
CC Evidence={ECO:0000250|UniProtKB:P28002};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28002}.
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, ECO:0000305}.
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DR EMBL; AF454631; AAN03726.1; -; mRNA.
DR EMBL; AF454632; AAN03727.1; -; mRNA.
DR EMBL; HG739099; CDP04982.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8LL87; -.
DR SMR; Q8LL87; -.
DR STRING; 49390.Q8LL87; -.
DR EnsemblPlants; CDP04982; CDP04982; GSCOC_T00019870001.
DR Gramene; CDP04982; CDP04982; GSCOC_T00019870001.
DR InParanoid; Q8LL87; -.
DR OMA; ENRRGPI; -.
DR PhylomeDB; Q8LL87; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000295252; Chromosome 2.
DR GO; GO:0047763; F:caffeate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016461; COMT-like.
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:SF199; FLAVONE 3'-O-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR11746; O-METHYLTRANSFERASE; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Lignin biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..350
FT /note="Caffeic acid 3-O-methyltransferase"
FT /id="PRO_0000063200"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT ACT_SITE 284
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT ACT_SITE 316
FT /evidence="ECO:0000250|UniProtKB:F1DBB3"
FT BINDING 118
FT /ligand="(E)-ferulate"
FT /ligand_id="ChEBI:CHEBI:29749"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 195
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 218
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 238
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 239
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 251
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 252
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 257
FT /ligand="(E)-5-hydroxyferulate"
FT /ligand_id="ChEBI:CHEBI:144381"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT CONFLICT 230
FT /note="S -> P (in Ref. 1; AAN03726)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="K -> R (in Ref. 1; AAN03726)"
FT /evidence="ECO:0000305"
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
//
