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Q03471

- ARIS_PENRO

UniProt

Q03471 - ARIS_PENRO

Protein

Aristolochene synthase

Gene

ARI1

Organism
Penicillium roqueforti
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalyzes the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene. Produces germacrene A as an enzyme-bound intermediate that is not released by the enzyme, but is further cyclized to produce aristolochene. Aristolochene is the likely parent compound for a number of sesquiterpenoid toxins produced by filamentous fungi.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Kineticsi

    1. KM=0.6 µM for (2E,6E)-farnesyl diphosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi115 – 1151Magnesium 1By similarity
    Metal bindingi115 – 1151Magnesium 2By similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Metal bindingi244 – 2441Magnesium 3By similarity
    Metal bindingi248 – 2481Magnesium 3By similarity
    Binding sitei251 – 2511SubstrateBy similarity
    Metal bindingi252 – 2521Magnesium 3By similarity

    GO - Molecular functioni

    1. aristolochene synthase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16547.
    BRENDAi4.2.3.9. 8737.
    UniPathwayiUPA00177; UER00582.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aristolochene synthase (EC:4.2.3.9)
    Short name:
    AS
    Alternative name(s):
    Sesquiterpene cyclase
    Gene namesi
    Name:ARI1
    OrganismiPenicillium roqueforti
    Taxonomic identifieri5082 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921Y → F: Causes 100-fold reduction in kcat but a 50-fold decrease in KM, resulting in a 2-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi115 – 1151D → N: Abolishes catalytic activity. 1 Publication
    Mutagenesisi244 – 2441N → L: Abolishes catalytic activity. 1 Publication
    Mutagenesisi248 – 2481S → A: Abolishes catalytic activity; when associated with D-252. 1 Publication
    Mutagenesisi252 – 2521E → D: Abolishes catalytic activity; when associated with A-248. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Aristolochene synthasePRO_0000064677Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    Secondary structure

    1
    342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi54 – 6815
    Helixi74 – 8310
    Helixi85 – 928
    Turni98 – 1003
    Helixi101 – 12020
    Helixi123 – 13715
    Helixi148 – 18033
    Turni181 – 1833
    Helixi193 – 2019
    Helixi204 – 21714
    Helixi223 – 2275
    Helixi230 – 24819
    Turni249 – 2524
    Helixi269 – 2779
    Helixi281 – 30727
    Helixi315 – 33622

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DGPX-ray2.80A/B40-339[»]
    1DI1X-ray2.50A/B40-339[»]
    1F1Kmodel-A1-342[»]
    1F1Lmodel-A1-342[»]
    1F1Nmodel-A1-342[»]
    1F1Pmodel-A1-342[»]
    ProteinModelPortaliQ03471.
    SMRiQ03471. Positions 40-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03471.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 3412Substrate-bindingBy similarity

    Sequence similaritiesi

    Belongs to the terpene synthase family.Curated

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR005630. Terpene_synthase_metal-bd.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q03471-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSTETISS LAQPFVHLEN PINSPLVKET IRPRNDTTIT PPPTQWSYLC    50
    HPRVKEVQDE VDGYFLENWK FPSFKAVRTF LDAKFSEVTC LYFPLALDDR 100
    IHFACRLLTV LFLIDDVLEH MSFADGEAYN NRLIPISRGD VLPDRTKPEE 150
    FILYDLWESM RAHDAELANE VLEPTFVFMR AQTDRARLSI HELGHYLEYR 200
    EKDVGKALLS ALMRFSMGLR LSADELQDMK ALEANCAKQL SVVNDIYSYD 250
    KEEEASRTGH KEGAFLCSAV KVLAEESKLG IPATKRVLWS MTREWETVHD 300
    EIVAEKIASP DGCSEAAKAY MKGLEYQMSG NEQWSKTTRR YN 342
    Length:342
    Mass (Da):39,192
    Last modified:October 1, 1993 - v1
    Checksum:iACFBD63F4FF9BB03
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05193 Genomic DNA. Translation: AAA33694.1.
    PIRiA45462.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05193 Genomic DNA. Translation: AAA33694.1 .
    PIRi A45462.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DGP X-ray 2.80 A/B 40-339 [» ]
    1DI1 X-ray 2.50 A/B 40-339 [» ]
    1F1K model - A 1-342 [» ]
    1F1L model - A 1-342 [» ]
    1F1N model - A 1-342 [» ]
    1F1P model - A 1-342 [» ]
    ProteinModelPortali Q03471.
    SMRi Q03471. Positions 40-339.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00177 ; UER00582 .
    BioCyci MetaCyc:MONOMER-16547.
    BRENDAi 4.2.3.9. 8737.

    Miscellaneous databases

    EvolutionaryTracei Q03471.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR005630. Terpene_synthase_metal-bd.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF03936. Terpene_synth_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti."
      Proctor R.H., Hohn T.M.
      J. Biol. Chem. 268:4543-4548(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 56-70; 76-84; 245-251 AND 323-336, FUNCTION, CATALYTIC ACTIVITY.
      Strain: ATCC 10110 / CBS 221.30 / NBRC 5459 / NRRL 849.
    2. "Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis."
      Felicetti B., Cane D.E.
      J. Am. Chem. Soc. 126:7212-7221(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-92; ASP-115; ASN-244; SER-248 AND GLU-252.
    3. "Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti."
      Caruthers J.M., Kang I., Rynkiewicz M.J., Cane D.E., Christianson D.W.
      J. Biol. Chem. 275:25533-25539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiARIS_PENRO
    AccessioniPrimary (citable) accession number: Q03471
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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