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Protein

5-epi-aristolochene synthase

Gene

EAS3

more
Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: 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 Mg2+ 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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:EAS-MONOMER.
    BRENDAi4.2.3.61. 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

    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.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [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.
    PIRiT03714.

    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...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00213.
    BioCyciMetaCyc:EAS-MONOMER.
    BRENDAi4.2.3.61. 3645.

    Miscellaneous databases

    EvolutionaryTraceiQ40577.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF48576. SSF48576. 1 hit.
    ProtoNetiSearch...

    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: April 1, 2015
    This is version 105 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

    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 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.