EOMT1_OCIBA
ID EOMT1_OCIBA Reviewed; 357 AA.
AC Q93WU2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Eugenol O-methyltransferase;
DE EC=2.1.1.146;
DE AltName: Full=(Iso)eugenol O-methyltransferase EOMT1;
DE AltName: Full=S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase EOMT1;
GN Name=EOMT1;
OS Ocimum basilicum (Sweet basil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC Ocimum.
OX NCBI_TaxID=39350;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF SER-261.
RC STRAIN=cv. EMX-1; TISSUE=Peltate glandular trichome;
RX PubMed=11884690; DOI=10.1105/tpc.010327;
RA Gang D.R., Lavid N., Zubieta C., Chen F., Beuerle T., Lewinsohn E.,
RA Noel J.P., Pichersky E.;
RT "Characterization of phenylpropene O-methyltransferases from sweet basil:
RT facile change of substrate specificity and convergent evolution within a
RT plant O-methyltransferase family.";
RL Plant Cell 14:505-519(2002).
CC -!- FUNCTION: Phenylpropene O-methyltransferase that catalyzes the
CC methylation of the para-4-hydroxyl of eugenol to methyleugenol. Can
CC also convert chavicol to methylchavicol but with less affinity.
CC {ECO:0000269|PubMed:11884690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + trans-isoeugenol = H(+) + S-
CC adenosyl-L-homocysteine + trans-isomethyleugenol;
CC Xref=Rhea:RHEA:17081, ChEBI:CHEBI:6877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:50545, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.146; Evidence={ECO:0000269|PubMed:11884690};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for t-Isoeugenol {ECO:0000269|PubMed:11884690};
CC KM=7 uM for chavicol {ECO:0000269|PubMed:11884690};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the peltate glandular
CC trichomes on the surface of the young basil leaves.
CC {ECO:0000269|PubMed:11884690}.
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; AF435008; AAL30424.1; -; mRNA.
DR AlphaFoldDB; Q93WU2; -.
DR SMR; Q93WU2; -.
DR KEGG; ag:AAL30424; -.
DR BRENDA; 2.1.1.146; 4385.
DR SABIO-RK; Q93WU2; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0050630; F:(iso)eugenol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0102719; F:S-adenosyl-L-methionine:eugenol-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..357
FT /note="Eugenol O-methyltransferase"
FT /id="PRO_0000204435"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT MUTAGEN 261
FT /note="S->F: Induces a substrate preference for chavicol."
FT /evidence="ECO:0000269|PubMed:11884690"
SQ SEQUENCE 357 AA; 40237 MW; FC050C48BF6D719C CRC64;
MALQKVDISL STEQLLQAQV HVWNHMYAFA NSMSLKCAIQ LGIPDILHKH GRPMTLSQLL
QSIPINKEKT QCFQRLMRAL VNSNFFIEEN NSNNQEVCYW LTPASCLLLK EAPLTVTPLV
QVVLDPTFTN PWHHMSEWFT HEKHATQFEA ANGCTFWEKL ANEPSKGRFF DEAMSCDSRL
IAHVFTKDYK HVIEGIRTLV DVGGGNGTMA KAIVEAMPTI KCTVIDLPHV VAGLESTDNL
NYIGGDMFQS IPSADAILLK SIIHDWDDVE GLKILKKCKD AVVMGGKVII IDVVVGVNHD
IDEVLEDQLH FDMAMMCYFN AKERTMSEWE KLIYDAGFKS YKLTPAFGVR SLIEAYP
