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Protein

Aristolochene synthase

Gene

Ari1

Organism
Aspergillus terreus
Status
Reviewed-Annotation score: Annotation score: 5 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+Note: Binds 3 Mg2+ ions per monomer.

Kineticsi

  1. KM=13.5 nM for (2E,6E)-farnesyl diphosphate2 Publications
  1. Vmax=23.6 nmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 8.0.2 Publications

Pathwayi: aristolochene biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes aristolochene from farnesyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Aristolochene synthase (Ari1)
This subpathway is part of the pathway aristolochene biosynthesis, which is itself part of Sesquiterpene biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes aristolochene from farnesyl diphosphate, the pathway aristolochene biosynthesis and in Sesquiterpene biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Magnesium 12 Publications
Metal bindingi90 – 901Magnesium 22 Publications
Binding sitei175 – 1751Substrate1 Publication
Metal bindingi219 – 2191Magnesium 32 Publications
Metal bindingi223 – 2231Magnesium 32 Publications
Binding sitei226 – 2261Substrate1 Publication
Metal bindingi227 – 2271Magnesium 32 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.3.9. 536.
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
OrganismiAspergillus terreus
Taxonomic identifieri33178 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271E → Q: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Aristolochene synthasePRO_0000418550Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
320
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 4315Combined sources
Helixi49 – 5810Combined sources
Helixi60 – 678Combined sources
Turni73 – 753Combined sources
Helixi76 – 9217Combined sources
Helixi93 – 953Combined sources
Helixi98 – 11215Combined sources
Helixi123 – 13816Combined sources
Helixi140 – 1445Combined sources
Helixi147 – 15711Combined sources
Helixi160 – 1634Combined sources
Helixi168 – 17811Combined sources
Helixi181 – 19212Combined sources
Helixi198 – 2036Combined sources
Helixi205 – 23329Combined sources
Turni236 – 2394Combined sources
Helixi244 – 2529Combined sources
Helixi256 – 28328Combined sources
Turni284 – 2863Combined sources
Helixi289 – 31123Combined sources
Helixi313 – 3164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4OX-ray2.20A/B/C/D1-320[»]
2OA6X-ray2.15A/B/C/D1-320[»]
3BNXX-ray2.10A/B/C/D1-320[»]
3BNYX-ray1.89A/B/C/D1-320[»]
3CKEX-ray2.40A/B/C/D1-320[»]
4KUXX-ray1.90A/B/C/D14-320[»]
4KVDX-ray2.40A/B/C/D14-320[»]
4KVIX-ray2.15A/B/C/D14-320[»]
4KVWX-ray2.10A/B/C/D14-320[»]
4KVYX-ray1.95A/B/C/D14-320[»]
4KWDX-ray1.86A/B/C/D14-320[»]
ProteinModelPortaliQ9UR08.
SMRiQ9UR08. Positions 13-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UR08.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni314 – 3152Substrate-binding

Sequence similaritiesi

Belongs to the terpene synthase family.Curated

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UR08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKPNGTNGA SSSLEPPPST FQPLCHPLVE EVSKEVDGYF LQHWNFPNEK
60 70 80 90 100
ARKKFVAAGF SRVTCLYFPK ALDDRIHFAC RLLTVLFLID DLLEYMSFEE
110 120 130 140 150
GSAYNEKLIP ISRGDVLPDR SIPVEYIIYD LWESMRAHDR EMADEILEPV
160 170 180 190 200
FLFMRAQTDR TRARPMGLGG YLEYRERDVG KELLAALMRF SMGLKLSPSE
210 220 230 240 250
LQRVREIDAN CSKHLSVVND IYSYEKELYT SKTAHSEGGI LCTSVQILAQ
260 270 280 290 300
EADVTAEAAK RVLFVMCREW ELRHQLLVAR LSAEGLETPG LAAYVEGLEY
310 320
QMSGNELWSQ TTLRYSVVVD
Length:320
Mass (Da):36,481
Last modified:May 1, 2000 - v1
Checksum:i73190707711ADC2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198359 mRNA. Translation: AAF13263.1.
AF198360 Genomic DNA. Translation: AAF13264.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198359 mRNA. Translation: AAF13263.1.
AF198360 Genomic DNA. Translation: AAF13264.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E4OX-ray2.20A/B/C/D1-320[»]
2OA6X-ray2.15A/B/C/D1-320[»]
3BNXX-ray2.10A/B/C/D1-320[»]
3BNYX-ray1.89A/B/C/D1-320[»]
3CKEX-ray2.40A/B/C/D1-320[»]
4KUXX-ray1.90A/B/C/D14-320[»]
4KVDX-ray2.40A/B/C/D14-320[»]
4KVIX-ray2.15A/B/C/D14-320[»]
4KVWX-ray2.10A/B/C/D14-320[»]
4KVYX-ray1.95A/B/C/D14-320[»]
4KWDX-ray1.86A/B/C/D14-320[»]
ProteinModelPortaliQ9UR08.
SMRiQ9UR08. Positions 13-318.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00177; UER00582.
BRENDAi4.2.3.9. 536.

Miscellaneous databases

EvolutionaryTraceiQ9UR08.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase."
    Cane D.E., Kang I.
    Arch. Biochem. Biophys. 376:354-364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 35-48; 183-195 AND 215-226, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 20516 / NRRL 11156.
  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 GLU-227.
  3. "X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate."
    Shishova E.Y., Di Costanzo L., Cane D.E., Christianson D.W.
    Biochemistry 46:1941-1951(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT.
  4. "X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis."
    Shishova E.Y., Yu F., Miller D.J., Faraldos J.A., Zhao Y., Coates R.M., Allemann R.K., Cane D.E., Christianson D.W.
    J. Biol. Chem. 283:15431-15439(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; SUBSTRATE ANALOGS AND MAGNESIUM.

Entry informationi

Entry nameiARIS_ASPTE
AccessioniPrimary (citable) accession number: Q9UR08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 58 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

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 one 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.