Q15GI4 (EGS1_OCIBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eugenol synthase 1
EC=1.1.1.318

Gene names

Name:

EGS1

Organism

Ocimum basilicum (Sweet basil)

Taxonomic identifier

39350 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Lamiaceae › Nepetoideae › Ocimeae › Ocimum

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the synthesis of the phenylpropene eugenol from coniferyl acetate. Phenylpropenes are produced by plants as defense compounds with antimicrobial and antianimal properties, or as floral attractants of pollinators. Eugenol is a characteristic aromatic constituent of spices. Ref.1
Catalytic activity	Eugenol + acetic acid + NADP+ = coniferyl acetate + NADPH. Ref.1 Eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH. Ref.1
Enzyme regulation	Inhibited by zinc and copper ions. Repressed by 4-bromo-cinnamyl acetate. Ref.1
Pathway	Aromatic compound metabolism; phenylpropanoid biosynthesis.
Tissue specificity	Trichome glands. Ref.1
Sequence similarities	Belongs to the NmrA-type oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=5.1 mM for coniferyl acetate (at pH 6.5 and 28 degrees Celsius) Ref.1 KM=131 µM for NADPH (at pH 6.5 and 28 degrees Celsius) Vmax=19.9 nmol/sec/mg enzyme (at pH 6.5 and 28 degrees Celsius) pH dependence: Optimum pH is 6.5.

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	phenylpropanoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 314

314

Eugenol synthase 1

PRO_0000314576

Secondary structure

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314

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Turn

14 – 16

3

Helix

20 – 29

10

Beta strand

34 – 38

5

Helix

45 – 53

9

Beta strand

57 – 60

4

Helix

66 – 73

8

Beta strand

77 – 81

5

Helix

85 – 87

3

Turn

88 – 90

3

Helix

91 – 101

11

Beta strand

106 – 108

3

Turn

116 – 118

3

Helix

123 – 141

19

Beta strand

146 – 150

5

Helix

155 – 163

9

Beta strand

170 – 175

6

Beta strand

181 – 185

5

Helix

187 – 197

11

Helix

201 – 203

3

Beta strand

206 – 209

4

Helix

213 – 215

3

Beta strand

216 – 218

3

Helix

219 – 230

12

Beta strand

235 – 239

5

Helix

241 – 250

10

Turn

253 – 255

3

Helix

256 – 266

11

Turn

270 – 272

3

Helix

283 – 285

3

Helix

295 – 304

10

Sequences

	Sequence		Length	Mass (Da)
	Q15GI4 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: B221B0E8E733213B	FASTA	314	35,607
	10 20 30 40 50 60 MEENGMKSKI LIFGGTGYIG NHMVKGSLKL GHPTYVFTRP NSSKTTLLDE FQSLGAIIVK 70 80 90 100 110 120 GELDEHEKLV ELMKKVDVVI SALAFPQILD QFKILEAIKV AGNIKRFLPS DFGVEEDRIN 130 140 150 160 170 180 ALPPFEALIE RKRMIRRAIE EANIPYTYVS ANCFASYFIN YLLRPYDPKD EITVYGTGEA 190 200 210 220 230 240 KFAMNYEQDI GLYTIKVATD PRALNRVVIY RPSTNIITQL ELISRWEKKI GKKFKKIHVP 250 260 270 280 290 300 EEEIVALTKE LPEPENIPIA ILHCLFIDGA TMSYDFKEND VEASTLYPEL KFTTIDELLD 310 IFVHDPPPPA SAAF

References

[1]

"Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester." Koeduka T., Fridman E., Gang D.R., Vassao D.G., Jackson B.L., Kish C.M., Orlova I., Spassova S.M., Lewis N.G., Noel J.P., Baiga T.J., Dudareva N., Pichersky E. Proc. Natl. Acad. Sci. U.S.A. 103:10128-10133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, CATALYTIC ACTIVITY. Strain: cv. SW. Tissue: Trichome gland.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ372812 mRNA. Translation: ABD17321.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QW8	X-ray	1.60	A/B	1-314	[»]
2QX7	X-ray	1.75	A/B	1-314	[»]
2QYS	X-ray	1.80	A/B	1-314	[»]
2QZZ	X-ray	1.60	A/B	1-314	[»]
2R2G	X-ray	1.80	A/B	1-314	[»]
2R6J	X-ray	1.50	A/B	1-314	[»]
3C3X	X-ray	2.15	A/B	1-314	[»]

ProteinModelPortal

Q15GI4.

SMR

Q15GI4. Positions 5-314.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13834.

SABIO-RK

Q15GI4.

UniPathway

UPA00711.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR016040. NAD(P)-bd_dom.
IPR008030. NmrA.
[Graphical view]

Pfam

PF05368. NmrA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q15GI4.

Entry information

Entry name

EGS1_OCIBA

Accession

Primary (citable) accession number: Q15GI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 25, 2006
Last modified:	March 6, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program