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Q40577

- 5EAS_TOBAC

UniProt

Q40577 - 5EAS_TOBAC

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (29 Apr 2008)
      Previous versions | rss
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    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

    Binds 3 magnesium ions per subunit.

    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 1
    Metal bindingi301 – 3011Magnesium 2
    Metal bindingi305 – 3051Magnesium 1
    Metal bindingi305 – 3051Magnesium 2
    Metal bindingi444 – 4441Magnesium 3
    Metal bindingi448 – 4481Magnesium 3
    Metal bindingi452 – 4521Magnesium 3

    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

    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-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MASAAVANYE EEIVRPVADF SPSLWGDQFL SFSIKNQVAE KYAKEIEALK    50
    EQTRNMLLAT GMKLADTLNL IDTIERLGIS YHFEKEIDDI LDQIYNQNSN 100
    CNDLCTSALQ FRLLRQHGFN ISPEIFSKFQ DENGKFKESL ASDVLGLLNL 150
    YEASHVRTHA DDILEDALAF STIHLESAAP HLKSPLREQV THALEQCLHK 200
    GVPRVETRFF ISSIYDKEQS KNNVLLRFAK LDFNLLQMLH KQELAQVSRW 250
    WKDLDFVTTL PYARDRVVEC YFWALGVYFE PQYSQARVML VKTISMISIV 300
    DDTFDAYGTV KELEAYTDAI QRWDINEIDR LPDYMKISYK AILDLYKDYE 350
    KELSSAGRSH IVCHAIERMK EVVRNYNVES TWFIEGYTPP VSEYLSNALA 400
    TTTYYYLATT SYLGMKSATE QDFEWLSKNP KILEASVIIC RVIDDTATYE 450
    VEKSRGQIAT GIECCMRDYG ISTKEAMAKF QNMAETAWKD INEGLLRPTP 500
    VSTEFLTPIL NLARIVEVTY IHNLDGYTHP EKVLKPHIIN LLVDSIKI 548
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04680 Unassigned RNA. Translation: AAA19216.1.
    PIRiT03714.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04680 Unassigned RNA. Translation: AAA19216.1 .
    PIRi T03714.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 101 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