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P13513 (TRI5_FUSSP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:
Trichodiene synthase

EC=4.2.3.6
Alternative name(s):
Sesquiterpene cyclase
Short name=TS
Gene names
Name:TRI5
Synonyms:TOX 5
OrganismFusarium sporotrichioides
Taxonomic identifier5514 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.

Catalytic activity

(2E,6E)-farnesyl diphosphate = trichodiene + diphosphate.

Pathway

Sesquiterpene biosynthesis; trichothecene biosynthesis.

Miscellaneous

Trichothecenes are sesquiterpenoid toxins that act by inhibiting protein biosynthesis.

Sequence similarities

Belongs to the trichodiene synthase family.

Ontologies

Keywords
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processsesquiterpenoid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiontrichodiene synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374Trichodiene synthase
PRO_0000221584

Secondary structure

.............................................. 374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13513 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 189E8FC1663C3763

FASTA37444,000
        10         20         30         40         50         60 
MENFPTEYFL NTTVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP RQQQLLKVDP 

        70         80         90        100        110        120 
KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD DSKDDPYPTM VNYFDDLQAG 

       130        140        150        160        170        180 
REQAHPWWAL VNEHFPNVLR HFGPFCSLNL IRSTLDFFEG CWIEQYNFGG FPGSHDYPQF 

       190        200        210        220        230        240 
LRRMNGLGHC VGASLWPKEQ FNERSLFLEI TSAIAQMENW MVWVNDLMSF YKEFDDERDQ 

       250        260        270        280        290        300 
ISLVKNYVVS DEISLHEALE KLTQDTLHSS KQMVAVFSDK DPQVMDTIEC FMHGYVTWHL 

       310        320        330        340        350        360 
CDRRYRLSEI YEKVKEEKTE DAQKFCKFYE QAANVGAVSP SEWAYPPVAQ LANVRSKDVK 

       370 
EVQKPFLSSI ELVE 

« Hide

References

[1]"Isolation and nucleotide sequence of a sesquiterpene cyclase gene from the trichothecene-producing fungus Fusarium sporotrichioides."
Hohn T.M., Beremand P.D.
Gene 79:131-138(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: NRRL 3299.
[2]"Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade."
Rynkiewicz M.J., Cane D.E., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 98:13543-13548(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF364179 Genomic DNA. Translation: AAD13657.1.
PIRSYFUTP. JU0064.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFAX-ray2.50A/B1-374[»]
1JFGX-ray2.50A/B1-374[»]
1KIYX-ray2.40A/B1-374[»]
1KIZX-ray2.60A/B1-374[»]
1YJ4X-ray2.30A/B1-374[»]
1YYQX-ray2.10A/B1-374[»]
1YYRX-ray2.50A/B1-374[»]
1YYSX-ray2.75A/B1-374[»]
1YYTX-ray2.90A/B1-374[»]
1YYUX-ray2.95A/B1-374[»]
2AEKX-ray2.90A/B1-374[»]
2AELX-ray2.50A/B1-374[»]
2AETX-ray2.75A/B1-374[»]
2PS4X-ray2.46A/B1-374[»]
2PS5X-ray2.10A/B1-374[»]
2PS6X-ray2.60A/B1-374[»]
2PS7X-ray2.35A/B1-374[»]
2PS8X-ray2.67A/B1-374[»]
2Q9YX-ray2.85A/B1-374[»]
2Q9ZX-ray2.95A/B1-374[»]
ProteinModelPortalP13513.
SMRP13513. Positions 1-354.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.2.3.6. 2364.
UniPathwayUPA00267.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR008949. Terpenoid_synth.
IPR010458. TRI5_ascomyc.
IPR024652. Trichodiene_synth.
[Graphical view]
PfamPF06330. TRI5. 1 hit.
[Graphical view]
PIRSFPIRSF001388. TRI5. 1 hit.
SUPFAMSSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP13513.

Entry information

Entry nameTRI5_FUSSP
AccessionPrimary (citable) accession number: P13513
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 14, 2014
This is version 74 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