CVMT1_OCIBA
ID CVMT1_OCIBA Reviewed; 356 AA.
AC Q93WU3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Chavicol O-methyltransferase;
DE EC=2.1.1.146;
DE AltName: Full=(Iso)eugenol O-methyltransferase CVOMT1;
DE AltName: Full=S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase CVOMT1;
GN Name=CVOMT1;
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 PHE-260.
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 chavicol to methylchavicol. Can
CC also convert eugenol to methyleugenol 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=6 uM for chavicol {ECO:0000269|PubMed:11884690};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AF435007; AAL30423.1; -; mRNA.
DR AlphaFoldDB; Q93WU3; -.
DR SMR; Q93WU3; -.
DR KEGG; ag:AAL30423; -.
DR SABIO-RK; Q93WU3; -.
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..356
FT /note="Chavicol O-methyltransferase"
FT /id="PRO_0000204434"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 245
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 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT MUTAGEN 260
FT /note="F->S: Induces a substrate preference for eugenol."
FT /evidence="ECO:0000269|PubMed:11884690"
SQ SEQUENCE 356 AA; 39916 MW; 2E57FD896895E4ED CRC64;
MALQNMDISL STEQLLQAQA HVWNHMYAFA NSMSLKCAIQ LGIPDILHKH DHPMTLSQLL
KAIPINKEKS QSFQRLMRAL VNSNFFIEEN SNNQEVCYWL TPASRLLLKG APLTVAPLVQ
VVLDPTFTNP WHYMSEWFKH ENHATQFEAA NGCTFWEKLA NKPSMGRFFD EAMSCDSRLV
AHVLTKDYKH VIDGIRTLVD VGGGNGTMAK AIVEAVPTMK CTVLDLPHVV AGLESTDKLS
YIGGDMFQSI PSADAILLKF IIHDWDDEEG LKILKRCKDA VGIGGKVIII DVVVGVNHDV
DEVLEDQLHF DMAMMSYFNA KERTMNEWEK LISAAGFTSY KLTPAFGVRS LIEAYP
