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Q40577 (5EAS_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-epi-aristolochene synthase

Short name=EAS
EC=4.2.3.61
Gene names
Name:EAS3
AND
Name:EAS4
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic intermediate 5-epi-aristolochene, initial step in the conversion of FPP to the sesquiterpenoid antifungal phytoalexin capsidiol. Produces germacrene A as an enzyme-bound intermediate that is not released by the enzyme, but is further cyclized to produce the bicyclic 5-epi-aristolochene.

Catalytic activity

(2E,6E)-farnesyl diphosphate = (+)-5-epiaristolochene + diphosphate. Ref.3

Cofactor

Binds 3 magnesium ions per subunit.

Pathway

Secondary metabolite biosynthesis; terpenoid biosynthesis.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Induction

By fungal elicitor. Ref.1

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Miscellaneous

Ref.1 indicates the presence of at least two genes coding for the same protein.

Sequence similarities

Belongs to the terpene synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.3 µM for 2-trans,6-trans-farnesyl diphosphate Ref.3

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processterpenoid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

terpene synthase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5485485-epi-aristolochene synthase
PRO_0000186438

Regions

Motif301 – 3055DDXXD motif

Sites

Metal binding3011Magnesium 1
Metal binding3011Magnesium 2
Metal binding3051Magnesium 1
Metal binding3051Magnesium 2
Metal binding4441Magnesium 3
Metal binding4481Magnesium 3
Metal binding4521Magnesium 3

Experimental info

Mutagenesis5201Y → F: Loss of production of aristolochene, and accumulation of the intermediate germacrene A. Ref.3
Sequence conflict351K → D in AAA19216. Ref.1
Sequence conflict421Y → YIY AA sequence Ref.1
Sequence conflict441K → Q in AAA19216. Ref.1
Sequence conflict551N → S in AAA19216. Ref.1
Sequence conflict621M → R in AAA19216. Ref.1
Sequence conflict731T → I in AAA19216. Ref.1
Sequence conflict891D → E in AAA19216. Ref.1
Sequence conflict3881T → M in AAA19216. Ref.1

Secondary structure

.............................................................................. 548
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q40577 [UniParc].

Last modified April 29, 2008. Version 3.
Checksum: 9FE25FF361A68BF1

FASTA54862,987
        10         20         30         40         50         60 
MASAAVANYE EEIVRPVADF SPSLWGDQFL SFSIKNQVAE KYAKEIEALK EQTRNMLLAT 

        70         80         90        100        110        120 
GMKLADTLNL IDTIERLGIS YHFEKEIDDI LDQIYNQNSN CNDLCTSALQ FRLLRQHGFN 

       130        140        150        160        170        180 
ISPEIFSKFQ DENGKFKESL ASDVLGLLNL YEASHVRTHA DDILEDALAF STIHLESAAP 

       190        200        210        220        230        240 
HLKSPLREQV THALEQCLHK GVPRVETRFF ISSIYDKEQS KNNVLLRFAK LDFNLLQMLH 

       250        260        270        280        290        300 
KQELAQVSRW WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV 

       310        320        330        340        350        360 
DDTFDAYGTV KELEAYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE KELSSAGRSH 

       370        380        390        400        410        420 
IVCHAIERMK EVVRNYNVES TWFIEGYTPP VSEYLSNALA TTTYYYLATT SYLGMKSATE 

       430        440        450        460        470        480 
QDFEWLSKNP KILEASVIIC RVIDDTATYE VEKSRGQIAT GIECCMRDYG ISTKEAMAKF 

       490        500        510        520        530        540 
QNMAETAWKD INEGLLRPTP VSTEFLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIIN 


LLVDSIKI 

« Hide

References

[1]"Gene family for an elicitor-induced sesquiterpene cyclase in tobacco."
Facchini P.J., Chappell J.
Proc. Natl. Acad. Sci. U.S.A. 89:11088-11092(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 56-73, INDUCTION.
Strain: cv. NK 326.
[2]O'Maille P.E.
Unpublished observations (APR-2008)
Cited for: SEQUENCE REVISION TO 35.
[3]"Demonstration of germacrene A as an intermediate in 5-epi-aristolochene synthase catalysis."
Rising K.A., Starks C.M., Noel J.P., Chappell J.
J. Am. Chem. Soc. 122:1861-1866(2000)
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-520.
[4]"Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase."
Starks C.M., Back K., Chappell J., Noel J.P.
Science 277:1815-1820(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE, SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04680 Unassigned RNA. Translation: AAA19216.1.
PIRT03714.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HX9X-ray3.50A1-548[»]
1HXAX-ray2.32A1-548[»]
1HXCX-ray2.25A1-548[»]
1HXGX-ray2.90A1-548[»]
3LZ9X-ray2.28A1-548[»]
3M00X-ray2.10A1-548[»]
3M01X-ray2.60A1-548[»]
3M02X-ray2.50A1-548[»]
4DI5X-ray2.30A14-548[»]
5EASX-ray2.25A1-548[»]
5EATX-ray2.80A1-548[»]
5EAUX-ray2.15A1-548[»]
ProteinModelPortalQ40577.
SMRQ40577. Positions 21-548.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:EAS-MONOMER.
BRENDA4.2.3.9. 3645.
UniPathwayUPA00213.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ40577.

Entry information

Entry name5EAS_TOBAC
AccessionPrimary (citable) accession number: Q40577
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways