IEMT_CLABR
ID IEMT_CLABR Reviewed; 368 AA.
AC O04385;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=(Iso)eugenol O-methyltransferase;
DE EC=2.1.1.146;
DE AltName: Full=S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase;
DE Short=IEMT;
DE Flags: Precursor;
GN Name=IEMT1;
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], PROTEIN SEQUENCE OF 3-13; 79-99 AND 255-268,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Flower;
RX PubMed=9159948; DOI=10.1104/pp.114.1.213;
RA Wang J., Dudareva N., Bhakta S., Raguso R.A., Pichersky E.;
RT "Floral scent production in Clarkia breweri (Onagraceae). II. Localization
RT and developmental modulation of the enzyme S-adenosyl-L-
RT methionine:(iso)eugenol O-methyltransferase and phenylpropanoid emission.";
RL Plant Physiol. 114:213-221(1997).
RN [2]
RP MUTAGENESIS OF 95-TYR-THR-96; SER-102; 130-PHE-LEU-131; 133-THR--THR-135;
RP LEU-140; PRO-142; PHE-144; 164-ASN-GLU-165 AND HIS-173.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=22851762; DOI=10.1105/tpc.112.101287;
RA Zhang K., Bhuiya M.W., Pazo J.R., Miao Y., Kim H., Ralph J., Liu C.J.;
RT "An engineered monolignol 4-O-methyltransferase depresses lignin
RT biosynthesis and confers novel metabolic capability in Arabidopsis.";
RL Plant Cell 24:3135-3152(2012).
CC -!- FUNCTION: Catalyzes the methylation of the para-4-hydroxyl of both
CC eugenol and (iso)eugenol to methyleugenol and isomethyleugenol,
CC respectively. The resulting products are part of a complex mixture of
CC low-molecular-weight volatile compounds emitted by the flowers to
CC attract pollinators.
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;
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in petals, style and stamens, but not in
CC stigma, sepals, leaves or stem tissues. {ECO:0000269|PubMed:9159948}.
CC -!- DEVELOPMENTAL STAGE: Expressed during flower development with a peak
CC just before anthesis. {ECO:0000269|PubMed:9159948}.
CC -!- MISCELLANEOUS: (iso)eugenol O-methyltransferase (IEMT) not only has
CC distinct substrate specificity from Caffeic acid 3-O-methyltransferases
CC (COMT), a highly homologous enzyme, but it also methylates the hydroxyl
CC group at the para position rather than at the meta position as COMT
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; U86760; AAC01533.1; -; mRNA.
DR PDB; 3REO; X-ray; 1.90 A; A/B/C/D=1-368.
DR PDB; 3TKY; X-ray; 2.47 A; A/B/C/D=1-368.
DR PDB; 5CVJ; X-ray; 1.80 A; A/B/C/D=1-368.
DR PDB; 5CVU; X-ray; 1.80 A; A/B/C/D=1-368.
DR PDB; 5CVV; X-ray; 1.73 A; A/B=1-368.
DR PDBsum; 3REO; -.
DR PDBsum; 3TKY; -.
DR PDBsum; 5CVJ; -.
DR PDBsum; 5CVU; -.
DR PDBsum; 5CVV; -.
DR AlphaFoldDB; O04385; -.
DR SMR; O04385; -.
DR KEGG; ag:AAC01533; -.
DR BRENDA; 2.1.1.146; 1437.
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 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 3D-structure; Direct protein sequencing; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:9159948"
FT /id="PRO_0000248970"
FT CHAIN 3..368
FT /note="(Iso)eugenol O-methyltransferase"
FT /id="PRO_0000063218"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22851762"
FT BINDING 211..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22851762"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22851762"
FT BINDING 254..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22851762"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22851762"
FT MUTAGEN 95..96
FT /note="YT->CS: No effect on substrate preference."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 102
FT /note="S->D: No effect on substrate preference."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 130..131
FT /note="FL->LC: No effect on substrate preference. Decreases
FT substrate discrimination; when associated with 164-TA-165.
FT Substrate preference changed; when associated with 133-MNQ-
FT 135 or 133-MNQ-135 and 164-TA-165."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 133..135
FT /note="TAT->MNQ: Decreases substrate discrimination.
FT Substrate preference changed; when associated with 130-LC-
FT 131 or 164-TA-165 or 130-LC-131 and 164-TA-165."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 140
FT /note="L->M: No effect on substrate preference; when
FT associated with S-142 and Y-144."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 142
FT /note="P->S: No effect on substrate preference; when
FT associated with M-140 and Y-144."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 144
FT /note="F->Y: No effect on substrate preference; when
FT associated with M-140 and S-142."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 164..165
FT /note="NE->TA: Decreases substrate discrimination.
FT Decreases substrate discrimination; when associated with
FT 130-LC-131. Substrate preference changed; when associated
FT with 133-MNQ-135 or 130-LC-131 and 133-MNQ-135."
FT /evidence="ECO:0000269|PubMed:10415125"
FT MUTAGEN 173
FT /note="H->P: No effect on substrate preference."
FT /evidence="ECO:0000269|PubMed:10415125"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 173..197
FT /evidence="ECO:0007829|PDB:5CVV"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:5CVV"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5CVV"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:5CVV"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:5CVV"
SQ SEQUENCE 368 AA; 39993 MW; 3963BA8FEFD2BC3B CRC64;
MGSTGNAEIQ IIPTHSSDEE ANLFAMQLAS AAVLPMALKA AIELDVLEIM AKSVPPSGYI
SPAEIAAQLP TTNPEAPVML DRVLRLLASY SVVTYTLREL PSGKVERLYG LAPVCKFLTK
NEDGVSLAPF LLTATDKVLL EPWFYLKDAI LEGGIPFNKA YGMNEFDYHG TDHRFNKVFN
KGMSSNSTIT MKKILEMYNG FEGLTTIVDV GGGTGAVASM IVAKYPSINA INFDLPHVIQ
DAPAFSGVEH LGGDMFDGVP KGDAIFIKWI CHDWSDEHCL KLLKNCYAAL PDHGKVIVAE
YILPPSPDPS IATKVVIHTD ALMLAYNPGG KERTEKEFQA LAMASGFRGF KVASCAFNTY
VMEFLKTA
