COMT1_CLABR
ID COMT1_CLABR Reviewed; 370 AA.
AC O23760;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
DE Flags: Precursor;
GN Name=COMT;
OS Clarkia breweri (Fairy fans) (Eucharidium breweri).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX NCBI_TaxID=36903;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 3-13.
RA Wang J., Pichersky E.;
RT "Nucleotide sequence of S-adenosyl-L-methionine:caffeic acid 3-O-
RT methyltransferase from Clarkia breweri.";
RL (er) Plant Gene Register PGR97-104(1997).
RN [2]
RP MUTAGENESIS OF 132-LEU-CYS-133; 135-MET--GLN-137 AND 166-THR-ALA-167.
RX PubMed=10415125; DOI=10.1006/abbi.1999.1304;
RA Wang J., Pichersky E.;
RT "Identification of specific residues involved in substrate discrimination
RT in two plant O-methyltransferases.";
RL Arch. Biochem. Biophys. 368:172-180(1999).
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.
CC -!- MISCELLANEOUS: Caffeic acid 3-O-methyltransferase (COMT) not only has
CC distinct substrate specificity from (iso)eugenol O-methyltransferases
CC (IEMT), a highly homologous enzyme, but it also methylates the hydroxyl
CC group at the meta position rather than at the para position as IEMT
CC does.
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; AF006009; AAB71141.1; -; mRNA.
DR AlphaFoldDB; O23760; -.
DR SMR; O23760; -.
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 PROPEP 1..2
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000248968"
FT CHAIN 3..370
FT /note="Caffeic acid 3-O-methyltransferase"
FT /id="PRO_0000063199"
FT REGION 167..185
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 135..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT MUTAGEN 132..133
FT /note="LC->FL: Decreases substrate discrimination.
FT Substrate preference changed; when associated with 135-TAT-
FT 137 or 135-TAT-137 and 166-NE-167."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 135..137
FT /note="MNQ->TAT: Decreases substrate discrimination.
FT Substrate preference changed; when associated with 132-FL-
FT 133 or 166-NE-167 or 132-FL-133 and 166-NE-167."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 166..167
FT /note="TA->NE: No effect on substrate preference; substrate
FT preference changed; when associated with 135-TAT-137 or
FT 132-FL-133 and 135-TAT-137."
FT /evidence="ECO:0000269|PubMed:10415125"
SQ SEQUENCE 370 AA; 40262 MW; 8ADC2F626FCB87CA CRC64;
MGSTGNAETQ LTPTHVSDEE ANLFAMQLAS ASVLPMVLKA AIELDVLEIM AKSIPHGSGA
YISPAEIAAQ LPTTNPDAPV MLDRVLRLLA SYSVVTCSLR ELPDGKVERL YGLAPVCKFL
TKNEDGVSLA PLCLMNQDKV LMESWYYLKD AILDGGIPFN KAYGMTAFEY HGTDPRFNKV
FNRGMSDHST ITMKKIFEMY TGFEALNTIV DVGGGTGAVL SMIVAKYPSI KGINFDLPHV
IEDAPIYPGV EHVGGDMFVS VPKGDAIFMK WICHDWSDEH CLKFLKNCYA ALPEHGKVIV
AECILPLSPD PSLATKGVIH IDAIMLAHNP GGKERTEKEF EALAIGAGFK GFKVACCAFN
TYVMEFLKTA
