COMT1_AMMMJ
ID COMT1_AMMMJ Reviewed; 365 AA.
AC Q6T1F5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Caffeic acid 3-O-methyltransferase {ECO:0000303|PubMed:15009205};
DE Short=CAOMT {ECO:0000250|UniProtKB:P28002};
DE Short=COMT {ECO:0000303|PubMed:15009205};
DE EC=2.1.1.68;
DE AltName: Full=S-adenosysl-L-methionine:caffeic acid 3-O-methyltransferase {ECO:0000250|UniProtKB:P28002};
GN Name=COMT {ECO:0000303|PubMed:15009205};
OS Ammi majus (Bishop's weed).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Ammi.
OX NCBI_TaxID=48026;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR24097.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15009205; DOI=10.1111/j.1432-1033.2004.03995.x;
RA Hehmann M., Lukacin R., Ekiert H., Matern U.;
RT "Furanocoumarin biosynthesis in Ammi majus L. Cloning of bergaptol O-
RT methyltransferase.";
RL Eur. J. Biochem. 271:932-940(2004).
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:0000305}.
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:0000269|PubMed:15009205};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), and to a lesser extent by
CC Ni(2+), Mn(2+), Co(2+), Fe(3+) and Zn(2+). Unaffected by Fe(2+) and
CC Mg(2+). {ECO:0000269|PubMed:15009205}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=122 uM for caffeate {ECO:0000269|PubMed:15009205};
CC KM=2 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:15009205};
CC KM=29 uM for 5-hydroxyferulate {ECO:0000269|PubMed:15009205};
CC KM=42 uM for caffeic acid methyl ester {ECO:0000269|PubMed:15009205};
CC KM=219 uM for caffeoyl coenzyme A {ECO:0000269|PubMed:15009205};
CC KM=2.2 mM for 3-(3,4-dihydroxyphenyl)propionate
CC {ECO:0000269|PubMed:15009205};
CC KM=133 uM for esculetin {ECO:0000269|PubMed:15009205};
CC KM=103 uM for daphnetin {ECO:0000269|PubMed:15009205};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15009205};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius.
CC {ECO:0000269|PubMed:15009205};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000250|UniProtKB:P28002}.
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}.
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DR EMBL; AY443007; AAR24097.1; -; mRNA.
DR AlphaFoldDB; Q6T1F5; -.
DR SMR; Q6T1F5; -.
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 Lignin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..365
FT /note="Caffeic acid 3-O-methyltransferase"
FT /id="PRO_0000401109"
FT REGION 164..182
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 132..138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P28002"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P28002,
FT ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 365 AA; 40152 MW; 54C4DB02E6CAD0D0 CRC64;
MNTTTELIPP TFQVNDDEEE ACMFAMQLAS ASVLPMVLKS AIELNLLESI AKAGPGAYVS
PSQLAAALPS SQPDTPVMLD RILRLLASYS VLNCKLRDLP DARVERLYGL APVCKFLTKN
SDGVSMAPLL LMNQDKILME SWYHLKDAVL DGGIPFNKAY GMTAFEYHGK DPRFNKVFNQ
GMSNHSTITM KKILQTYDGF GGLKTVVDVG GGTGATLNMI ISKYPNLKGI NFDLPHVVED
APSYAGVEHV GGDMFVSVPK GDAIFMKWIC HDWSDAHCLA FLKNCYKALP KDGKVILAEC
ILPEAPDSKL TTKNVILIDV IMLAHNPGGK ERTEKEFEAF GKQAGFKSFN KACCAYNTWV
IEYYK
