COMT1_POPTM
ID COMT1_POPTM Reviewed; 365 AA.
AC Q00763; Q43094;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Caffeic acid 3-O-methyltransferase 1;
DE Short=CAOMT-1;
DE Short=COMT-1;
DE EC=2.1.1.68;
DE AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase 1;
GN Name=OMT1;
OS Populus tremuloides (Quaking aspen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 165-184; 335-346 AND
RP 349-359.
RC TISSUE=Xylem;
RX PubMed=1932694; DOI=10.1007/bf00028736;
RA Bugos R.C., Chiang V.L.C., Campbell W.H.;
RT "cDNA cloning, sequence analysis and seasonal expression of lignin-
RT bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of
RT aspen.";
RL Plant Mol. Biol. 17:1203-1215(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7770534; DOI=10.1104/pp.107.4.1459;
RA Tsai C.-J., Podila G.K., Chiang V.L.C.;
RT "Nucleotide sequence of a Populus tremuloides gene encoding bispecific
RT caffeic acid/5-hydroxyferulic acid O-methyltransferase.";
RL Plant Physiol. 107:1459-1459(1995).
RN [3]
RP SEQUENCE REVISION.
RA Tsai C.-J., Mielke M.R., Podila G.K., Chiang V.L.C.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 165-184; 335-346 AND 349-359.
RC TISSUE=Xylem;
RX PubMed=1368360; DOI=10.1016/0031-9422(92)83093-e;
RA Bugos R.C., Chiang V.L., Campbell W.H.;
RT "Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-
RT methyltransferase from aspen.";
RL Phytochemistry 31:1495-1498(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 -!- TISSUE SPECIFICITY: Xylem.
CC -!- PTM: The N-terminus is blocked.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62096; CAA44006.1; -; mRNA.
DR EMBL; U13171; AAB61731.1; -; Genomic_DNA.
DR PIR; S18568; S18568.
DR AlphaFoldDB; Q00763; -.
DR SMR; Q00763; -.
DR UniPathway; UPA00711; -.
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:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; 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 1: Evidence at protein level;
KW Direct protein sequencing; Lignin biosynthesis; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..365
FT /note="Caffeic acid 3-O-methyltransferase 1"
FT /id="PRO_0000063209"
FT REGION 162..180
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 130..136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 251
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 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 365 AA; 39805 MW; A6CECDEA4E0007CD CRC64;
MGSTGETQMT PTQVSDEEAH LFAMQLASAS VLPMILKTAI ELDLLEIMAK AGPGAFLSTS
EIASHLPTKN PDAPVMLDRI LRLLASYSIL TCSLKDLPDG KVERLYGLAP VCKFLTKNED
GVSVSPLCLM NQDKVLMESW YYLKDAILDG GIPFNKAYGM TAFEYHGTDP RFNKVFNKGM
SDHSTITMKK ILETYKGFEG LTSLVDVGGG TGAVVNTIVS KYPSIKGINF DLPHVIEDAP
SYPGVEHVGG DMFVSVPKAD AVFMKWICHD WSDAHCLKFL KNCYDALPEN GKVILVECIL
PVAPDTSLAT KGVVHVDVIM LAHNPGGKER TEKEFEGLAK GAGFQGFEVM CCAFNTHVIE
FRKKA
