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Protein

(Iso)eugenol O-methyltransferase

Gene

IEMT1

Organism
Clarkia breweri (Fairy fans) (Eucharidium breweri)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the methylation of the para-4-hydroxyl of both eugenol and (iso)eugenol to methyleugenol and isomethyleugenol, respectively. The resulting products are part of a complex mixture of low-molecular-weight volatile compounds emitted by the flowers to attract pollinators.

Catalytic activityi

S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + isomethyleugenol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871S-adenosyl-L-methionine1 Publication
Binding sitei234 – 2341S-adenosyl-L-methionine1 Publication
Binding sitei268 – 2681S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
Active sitei272 – 2721Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.146. 1437.

Names & Taxonomyi

Protein namesi
Recommended name:
(Iso)eugenol O-methyltransferase (EC:2.1.1.146)
Alternative name(s):
S-adenosysl-L-methionine:(Iso)eugenol O-methyltransferase
Short name:
IEMT
Gene namesi
Name:IEMT1
OrganismiClarkia breweri (Fairy fans) (Eucharidium breweri)
Taxonomic identifieri36903 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMyrtalesOnagraceaeOnagroideaeOnagreaeClarkia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 962YT → CS: No effect on substrate preference. 1 Publication
Mutagenesisi102 – 1021S → D: No effect on substrate preference. 1 Publication
Mutagenesisi130 – 1312FL → LC: No effect on substrate preference. Decreases substrate discrimination; when associated with 164-TA-165. Substrate preference changed; when associated with 133-MNQ-135 or 133-MNQ-135 and 164-TA-165. 1 Publication
Mutagenesisi133 – 1353TAT → MNQ: Decreases substrate discrimination. Substrate preference changed; when associated with 130-LC-131 or 164-TA-165 or 130-LC-131 and 164-TA-165. 1 Publication
Mutagenesisi140 – 1401L → M: No effect on substrate preference; when associated with S-142 and Y-144. 1 Publication
Mutagenesisi142 – 1421P → S: No effect on substrate preference; when associated with M-140 and Y-144. 1 Publication
Mutagenesisi144 – 1441F → Y: No effect on substrate preference; when associated with M-140 and S-142. 1 Publication
Mutagenesisi164 – 1652NE → TA: Decreases substrate discrimination. Decreases substrate discrimination; when associated with 130-LC-131. Substrate preference changed; when associated with 133-MNQ-135 or 130-LC-131 and 133-MNQ-135. 1 Publication
Mutagenesisi173 – 1731H → P: No effect on substrate preference. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 221 PublicationPRO_0000248970
Chaini3 – 368366(Iso)eugenol O-methyltransferasePRO_0000063218Add
BLAST

Expressioni

Tissue specificityi

Expressed in petals, style and stamens, but not in stigma, sepals, leaves or stem tissues.1 Publication

Developmental stagei

Expressed during flower development with a peak just before anthesis.1 Publication

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 3014Combined sources
Helixi33 – 4311Combined sources
Helixi46 – 538Combined sources
Beta strandi56 – 583Combined sources
Helixi62 – 665Combined sources
Helixi76 – 8914Combined sources
Beta strandi92 – 987Combined sources
Beta strandi101 – 1044Combined sources
Beta strandi106 – 1116Combined sources
Helixi113 – 1175Combined sources
Helixi128 – 1347Combined sources
Helixi137 – 1404Combined sources
Helixi141 – 1455Combined sources
Helixi146 – 1527Combined sources
Helixi156 – 1616Combined sources
Helixi165 – 1695Combined sources
Helixi173 – 19725Combined sources
Turni200 – 2034Combined sources
Beta strandi205 – 2106Combined sources
Helixi216 – 2249Combined sources
Beta strandi229 – 2346Combined sources
Helixi236 – 2394Combined sources
Beta strandi248 – 2525Combined sources
Turni255 – 2573Combined sources
Beta strandi263 – 2697Combined sources
Helixi271 – 2733Combined sources
Helixi276 – 28914Combined sources
Beta strandi295 – 3006Combined sources
Helixi311 – 32616Combined sources
Beta strandi327 – 3293Combined sources
Helixi335 – 34410Combined sources
Beta strandi349 – 3568Combined sources
Beta strandi359 – 3668Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3REOX-ray1.90A/B/C/D1-368[»]
3TKYX-ray2.47A/B/C/D1-368[»]
5CVJX-ray1.80A/B/C/D1-368[»]
5CVUX-ray1.80A/B/C/D1-368[»]
5CVVX-ray1.73A/B1-368[»]
ProteinModelPortaliO04385.
SMRiO04385. Positions 7-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 2122S-adenosyl-L-methionine binding1 Publication
Regioni254 – 2552S-adenosyl-L-methionine binding1 Publication

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.PROSITE-ProRule annotation

Phylogenomic databases

KOiK17057.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSTGNAEIQ IIPTHSSDEE ANLFAMQLAS AAVLPMALKA AIELDVLEIM
60 70 80 90 100
AKSVPPSGYI SPAEIAAQLP TTNPEAPVML DRVLRLLASY SVVTYTLREL
110 120 130 140 150
PSGKVERLYG LAPVCKFLTK NEDGVSLAPF LLTATDKVLL EPWFYLKDAI
160 170 180 190 200
LEGGIPFNKA YGMNEFDYHG TDHRFNKVFN KGMSSNSTIT MKKILEMYNG
210 220 230 240 250
FEGLTTIVDV GGGTGAVASM IVAKYPSINA INFDLPHVIQ DAPAFSGVEH
260 270 280 290 300
LGGDMFDGVP KGDAIFIKWI CHDWSDEHCL KLLKNCYAAL PDHGKVIVAE
310 320 330 340 350
YILPPSPDPS IATKVVIHTD ALMLAYNPGG KERTEKEFQA LAMASGFRGF
360
KVASCAFNTY VMEFLKTA
Length:368
Mass (Da):39,993
Last modified:June 1, 1998 - v2
Checksum:i3963BA8FEFD2BC3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86760 mRNA. Translation: AAC01533.1.

Genome annotation databases

KEGGiag:AAC01533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86760 mRNA. Translation: AAC01533.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3REOX-ray1.90A/B/C/D1-368[»]
3TKYX-ray2.47A/B/C/D1-368[»]
5CVJX-ray1.80A/B/C/D1-368[»]
5CVUX-ray1.80A/B/C/D1-368[»]
5CVVX-ray1.73A/B1-368[»]
ProteinModelPortaliO04385.
SMRiO04385. Positions 7-366.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC01533.

Phylogenomic databases

KOiK17057.

Enzyme and pathway databases

BRENDAi2.1.1.146. 1437.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR012967. Plant_MeTrfase_dimerisation.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08100. Dimerisation. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIEMT_CLABR
AccessioniPrimary (citable) accession number: O04385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: June 1, 1998
Last modified: April 13, 2016
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

(iso)eugenol O-methyltransferase (IEMT) not only has distinct substrate specificity from Caffeic acid 3-O-methyltransferases (COMT), a highly homologous enzyme, but it also methylates the hydroxyl group at the para position rather than at the meta position as COMT does.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.