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Q03471 (ARIS_PENRO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aristolochene synthase

Short name=AS
EC=4.2.3.9
Alternative name(s):
Sesquiterpene cyclase
Gene names
Name:ARI1
OrganismPenicillium roqueforti
Taxonomic identifier5082 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

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

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Sesquiterpene biosynthesis; aristolochene biosynthesis; aristolochene from farnesyl diphosphate: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the terpene synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.6 µM for (2E,6E)-farnesyl diphosphate Ref.2

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaristolochene synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Aristolochene synthase
PRO_0000064677

Regions

Region340 – 3412Substrate-binding By similarity

Sites

Metal binding1151Magnesium 1 By similarity
Metal binding1151Magnesium 2 By similarity
Metal binding2441Magnesium 3 By similarity
Metal binding2481Magnesium 3 By similarity
Metal binding2521Magnesium 3 By similarity
Binding site2001Substrate By similarity
Binding site2511Substrate By similarity

Experimental info

Mutagenesis921Y → F: Causes 100-fold reduction in kcat but a 50-fold decrease in KM, resulting in a 2-fold decrease in catalytic efficiency. Ref.2
Mutagenesis1151D → N: Abolishes catalytic activity. Ref.2
Mutagenesis2441N → L: Abolishes catalytic activity. Ref.2
Mutagenesis2481S → A: Abolishes catalytic activity; when associated with D-252. Ref.2
Mutagenesis2521E → D: Abolishes catalytic activity; when associated with A-248. Ref.2

Secondary structure

.............................. 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03471 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: ACFBD63F4FF9BB03

FASTA34239,192
        10         20         30         40         50         60 
MATSTETISS LAQPFVHLEN PINSPLVKET IRPRNDTTIT PPPTQWSYLC HPRVKEVQDE 

        70         80         90        100        110        120 
VDGYFLENWK FPSFKAVRTF LDAKFSEVTC LYFPLALDDR IHFACRLLTV LFLIDDVLEH 

       130        140        150        160        170        180 
MSFADGEAYN NRLIPISRGD VLPDRTKPEE FILYDLWESM RAHDAELANE VLEPTFVFMR 

       190        200        210        220        230        240 
AQTDRARLSI HELGHYLEYR EKDVGKALLS ALMRFSMGLR LSADELQDMK ALEANCAKQL 

       250        260        270        280        290        300 
SVVNDIYSYD KEEEASRTGH KEGAFLCSAV KVLAEESKLG IPATKRVLWS MTREWETVHD 

       310        320        330        340 
EIVAEKIASP DGCSEAAKAY MKGLEYQMSG NEQWSKTTRR YN 

« Hide

References

[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05193 Genomic DNA. Translation: AAA33694.1.
PIRA45462.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ03471.
SMRQ03471. Positions 40-339.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16547.
BRENDA4.2.3.9. 8737.
UniPathwayUPA00177; UER00582.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR005630. Terpene_synthase_metal-bd.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ03471.

Entry information

Entry nameARIS_PENRO
AccessionPrimary (citable) accession number: Q03471
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways