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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)DescriptionActionsGraphical viewLength
Binding sitei187S-adenosyl-L-methionine1 Publication1
Binding sitei234S-adenosyl-L-methionine1 Publication1
Binding sitei268S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Active sitei272Proton acceptorPROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
Mutagenesisi95 – 96YT → CS: No effect on substrate preference. 1 Publication2
Mutagenesisi102S → D: No effect on substrate preference. 1 Publication1
Mutagenesisi130 – 131FL → 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 Publication2
Mutagenesisi133 – 135TAT → 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 Publication3
Mutagenesisi140L → M: No effect on substrate preference; when associated with S-142 and Y-144. 1 Publication1
Mutagenesisi142P → S: No effect on substrate preference; when associated with M-140 and Y-144. 1 Publication1
Mutagenesisi144F → Y: No effect on substrate preference; when associated with M-140 and S-142. 1 Publication1
Mutagenesisi164 – 165NE → 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 Publication2
Mutagenesisi173H → P: No effect on substrate preference. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002489701 – 21 Publication2
ChainiPRO_00000632183 – 368(Iso)eugenol O-methyltransferaseAdd BLAST366

Proteomic databases

PRIDEiO04385.

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

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 30Combined sources14
Helixi33 – 43Combined sources11
Helixi46 – 53Combined sources8
Beta strandi56 – 58Combined sources3
Helixi62 – 66Combined sources5
Helixi76 – 89Combined sources14
Beta strandi92 – 98Combined sources7
Beta strandi101 – 104Combined sources4
Beta strandi106 – 111Combined sources6
Helixi113 – 117Combined sources5
Helixi128 – 134Combined sources7
Helixi137 – 140Combined sources4
Helixi141 – 145Combined sources5
Helixi146 – 152Combined sources7
Helixi156 – 161Combined sources6
Helixi165 – 169Combined sources5
Helixi173 – 197Combined sources25
Turni200 – 203Combined sources4
Beta strandi205 – 210Combined sources6
Helixi216 – 224Combined sources9
Beta strandi229 – 234Combined sources6
Helixi236 – 239Combined sources4
Beta strandi248 – 252Combined sources5
Turni255 – 257Combined sources3
Beta strandi263 – 269Combined sources7
Helixi271 – 273Combined sources3
Helixi276 – 289Combined sources14
Beta strandi295 – 300Combined sources6
Helixi311 – 326Combined sources16
Beta strandi327 – 329Combined sources3
Helixi335 – 344Combined sources10
Beta strandi349 – 356Combined sources8
Beta strandi359 – 366Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni211 – 212S-adenosyl-L-methionine binding1 Publication2
Regioni254 – 255S-adenosyl-L-methionine binding1 Publication2

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO04385.

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: November 2, 2016
This is version 82 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.