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Protein

Aristolochene synthase

Gene

ARI1

Organism
Penicillium roqueforti
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 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

Mg2+By similarityNote: Binds 3 Mg2+ 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
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16547.
BRENDAi4.2.3.9. 4638.
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
Complete GO annotation...

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 – 6815Combined sources
Helixi74 – 8310Combined sources
Helixi85 – 928Combined sources
Turni98 – 1003Combined sources
Helixi101 – 12020Combined sources
Helixi123 – 13715Combined sources
Helixi148 – 18033Combined sources
Turni181 – 1833Combined sources
Helixi193 – 2019Combined sources
Helixi204 – 21714Combined sources
Helixi223 – 2275Combined sources
Helixi230 – 24819Combined sources
Turni249 – 2524Combined sources
Helixi269 – 2779Combined sources
Helixi281 – 30727Combined sources
Helixi315 – 33622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Phylogenomic databases

PhylomeDBiQ03471.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR005630. Terpene_synthase_metal-bd.
[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

        10         20         30         40         50
MATSTETISS LAQPFVHLEN PINSPLVKET IRPRNDTTIT PPPTQWSYLC
60 70 80 90 100
HPRVKEVQDE VDGYFLENWK FPSFKAVRTF LDAKFSEVTC LYFPLALDDR
110 120 130 140 150
IHFACRLLTV LFLIDDVLEH MSFADGEAYN NRLIPISRGD VLPDRTKPEE
160 170 180 190 200
FILYDLWESM RAHDAELANE VLEPTFVFMR AQTDRARLSI HELGHYLEYR
210 220 230 240 250
EKDVGKALLS ALMRFSMGLR LSADELQDMK ALEANCAKQL SVVNDIYSYD
260 270 280 290 300
KEEEASRTGH KEGAFLCSAV KVLAEESKLG IPATKRVLWS MTREWETVHD
310 320 330 340
EIVAEKIASP DGCSEAAKAY MKGLEYQMSG NEQWSKTTRR YN
Length:342
Mass (Da):39,192
Last modified:September 30, 1993 - v1
Checksum:iACFBD63F4FF9BB03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05193 Genomic DNA. Translation: AAA33694.1.
PIRiA45462.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05193 Genomic DNA. Translation: AAA33694.1.
PIRiA45462.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

PhylomeDBiQ03471.

Enzyme and pathway databases

UniPathwayiUPA00177; UER00582.
BioCyciMetaCyc:MONOMER-16547.
BRENDAi4.2.3.9. 4638.

Miscellaneous databases

EvolutionaryTraceiQ03471.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR005630. Terpene_synthase_metal-bd.
[Graphical view]
PfamiPF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

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(1992) [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(2003) [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(1999) [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: September 30, 1993
Last sequence update: September 30, 1993
Last modified: March 31, 2015
This is version 91 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

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.