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Q40577

- 5EAS_TOBAC

UniProt

Q40577 - 5EAS_TOBAC

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Protein

5-epi-aristolochene synthase

Gene

EAS3

more
Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

(2E,6E)-farnesyl diphosphate = (+)-5-epiaristolochene + diphosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg(2+) ions per subunit.1 Publication

Kineticsi

  1. KM=2.3 µM for 2-trans,6-trans-farnesyl diphosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi301 – 3011Magnesium 11 Publication
Metal bindingi301 – 3011Magnesium 21 Publication
Metal bindingi305 – 3051Magnesium 11 Publication
Metal bindingi305 – 3051Magnesium 21 Publication
Metal bindingi444 – 4441Magnesium 31 Publication
Metal bindingi448 – 4481Magnesium 31 Publication
Metal bindingi452 – 4521Magnesium 31 Publication

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. terpene synthase activity Source: InterPro

GO - Biological processi

  1. terpenoid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:EAS-MONOMER.
BRENDAi4.2.3.9. 3645.
UniPathwayiUPA00213.

Names & Taxonomyi

Protein namesi
Recommended name:
5-epi-aristolochene synthase (EC:4.2.3.61)
Short name:
EAS
Gene namesi
Name:EAS3
AND
Name:EAS4
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi520 – 5201Y → F: Loss of production of aristolochene, and accumulation of the intermediate germacrene A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5485485-epi-aristolochene synthasePRO_0000186438Add
BLAST

Expressioni

Inductioni

By fungal elicitor.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 296Combined sources
Helixi36 – 5722Combined sources
Helixi64 – 7613Combined sources
Helixi80 – 823Combined sources
Helixi84 – 9714Combined sources
Helixi104 – 11613Combined sources
Helixi123 – 1297Combined sources
Beta strandi134 – 1363Combined sources
Helixi138 – 1425Combined sources
Helixi144 – 15411Combined sources
Helixi162 – 1643Combined sources
Helixi167 – 17812Combined sources
Helixi179 – 1813Combined sources
Helixi186 – 19510Combined sources
Helixi203 – 21311Combined sources
Helixi215 – 2173Combined sources
Helixi223 – 25230Combined sources
Turni253 – 2553Combined sources
Helixi256 – 2594Combined sources
Helixi267 – 27711Combined sources
Helixi281 – 2833Combined sources
Helixi284 – 30522Combined sources
Helixi310 – 32213Combined sources
Helixi325 – 3306Combined sources
Helixi333 – 35422Combined sources
Turni355 – 3573Combined sources
Helixi359 – 3613Combined sources
Helixi362 – 38524Combined sources
Helixi391 – 3988Combined sources
Helixi400 – 4023Combined sources
Helixi404 – 41310Combined sources
Helixi420 – 4278Combined sources
Helixi431 – 44717Combined sources
Helixi449 – 4546Combined sources
Helixi461 – 4699Combined sources
Helixi473 – 49422Combined sources
Beta strandi496 – 4983Combined sources
Helixi503 – 5053Combined sources
Helixi507 – 51913Combined sources
Turni520 – 5223Combined sources
Turni523 – 5253Combined sources
Turni526 – 5283Combined sources
Helixi531 – 54212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ40577.
SMRiQ40577. Positions 21-548.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ40577.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3055DDXXD motif

Domaini

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

Sequence similaritiesi

Belongs to the terpene synthase family.Curated

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

Q40577-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASAAVANYE EEIVRPVADF SPSLWGDQFL SFSIKNQVAE KYAKEIEALK
60 70 80 90 100
EQTRNMLLAT GMKLADTLNL IDTIERLGIS YHFEKEIDDI LDQIYNQNSN
110 120 130 140 150
CNDLCTSALQ FRLLRQHGFN ISPEIFSKFQ DENGKFKESL ASDVLGLLNL
160 170 180 190 200
YEASHVRTHA DDILEDALAF STIHLESAAP HLKSPLREQV THALEQCLHK
210 220 230 240 250
GVPRVETRFF ISSIYDKEQS KNNVLLRFAK LDFNLLQMLH KQELAQVSRW
260 270 280 290 300
WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV
310 320 330 340 350
DDTFDAYGTV KELEAYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE
360 370 380 390 400
KELSSAGRSH IVCHAIERMK EVVRNYNVES TWFIEGYTPP VSEYLSNALA
410 420 430 440 450
TTTYYYLATT SYLGMKSATE QDFEWLSKNP KILEASVIIC RVIDDTATYE
460 470 480 490 500
VEKSRGQIAT GIECCMRDYG ISTKEAMAKF QNMAETAWKD INEGLLRPTP
510 520 530 540
VSTEFLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIIN LLVDSIKI
Length:548
Mass (Da):62,987
Last modified:April 29, 2008 - v3
Checksum:i9FE25FF361A68BF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351K → D in AAA19216. (PubMed:1438319)Curated
Sequence conflicti42 – 421Y → YIY AA sequence (PubMed:1438319)Curated
Sequence conflicti44 – 441K → Q in AAA19216. (PubMed:1438319)Curated
Sequence conflicti55 – 551N → S in AAA19216. (PubMed:1438319)Curated
Sequence conflicti62 – 621M → R in AAA19216. (PubMed:1438319)Curated
Sequence conflicti73 – 731T → I in AAA19216. (PubMed:1438319)Curated
Sequence conflicti89 – 891D → E in AAA19216. (PubMed:1438319)Curated
Sequence conflicti388 – 3881T → M in AAA19216. (PubMed:1438319)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04680 Unassigned RNA. Translation: AAA19216.1.
PIRiT03714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04680 Unassigned RNA. Translation: AAA19216.1 .
PIRi T03714.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HX9 X-ray 3.50 A 1-548 [» ]
1HXA X-ray 2.32 A 1-548 [» ]
1HXC X-ray 2.25 A 1-548 [» ]
1HXG X-ray 2.90 A 1-548 [» ]
3LZ9 X-ray 2.28 A 1-548 [» ]
3M00 X-ray 2.10 A 1-548 [» ]
3M01 X-ray 2.60 A 1-548 [» ]
3M02 X-ray 2.50 A 1-548 [» ]
4DI5 X-ray 2.30 A 14-548 [» ]
5EAS X-ray 2.25 A 1-548 [» ]
5EAT X-ray 2.80 A 1-548 [» ]
5EAU X-ray 2.15 A 1-548 [» ]
ProteinModelPortali Q40577.
SMRi Q40577. Positions 21-548.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00213 .
BioCyci MetaCyc:EAS-MONOMER.
BRENDAi 4.2.3.9. 3645.

Miscellaneous databases

EvolutionaryTracei Q40577.

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProi IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry namei5EAS_TOBAC
AccessioniPrimary (citable) accession number: Q40577
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 29, 2008
Last modified: November 26, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

PubMed:1438319 indicates the presence of at least two genes coding for the same protein.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

External Data

Dasty 3