P13513 (TRI5_FUSSP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trichodiene synthase
EC=4.2.3.6

Alternative name(s):
Sesquiterpene cyclase
Short name=TS

Gene names

Name:	TRI5
Synonyms:	TOX 5

Organism

Fusarium sporotrichioides

Taxonomic identifier

5514 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	sesquiterpenoid biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	trichodiene synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 374

374

Trichodiene synthase

PRO_0000221584

Secondary structure

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374

Helix Strand Turn

Details...

Helix

6 – 19

14

Helix

29 – 47

19

Helix

50 – 55

6

Helix

60 – 77

18

Helix

83 – 99

17

Helix

107 – 110

4

Helix

113 – 119

7

Helix

126 – 139

14

Helix

144 – 164

21

Turn

165 – 167

3

Helix

177 – 186

10

Helix

188 – 193

6

Turn

198 – 200

3

Turn

203 – 206

4

Helix

207 – 233

27

Helix

243 – 251

9

Helix

255 – 277

23

Beta strand

278 – 280

3

Helix

282 – 301

20

Helix

303 – 305

3

Helix

308 – 314

7

Helix

320 – 336

17

Helix

340 – 342

3

Helix

348 – 353

6

Sequences

	Sequence		Length	Mass (Da)
	P13513 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 189E8FC1663C3763	FASTA	374	44,000
	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

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.

PIR

SYFUTP. JU0064.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JFA	X-ray	2.50	A/B	1-374	[»]
1JFG	X-ray	2.50	A/B	1-374	[»]
1KIY	X-ray	2.40	A/B	1-374	[»]
1KIZ	X-ray	2.60	A/B	1-374	[»]
1YJ4	X-ray	2.30	A/B	1-374	[»]
1YYQ	X-ray	2.10	A/B	1-374	[»]
1YYR	X-ray	2.50	A/B	1-374	[»]
1YYS	X-ray	2.75	A/B	1-374	[»]
1YYT	X-ray	2.90	A/B	1-374	[»]
1YYU	X-ray	2.95	A/B	1-374	[»]
2AEK	X-ray	2.90	A/B	1-374	[»]
2AEL	X-ray	2.50	A/B	1-374	[»]
2AET	X-ray	2.75	A/B	1-374	[»]
2PS4	X-ray	2.46	A/B	1-374	[»]
2PS5	X-ray	2.10	A/B	1-374	[»]
2PS6	X-ray	2.60	A/B	1-374	[»]
2PS7	X-ray	2.35	A/B	1-374	[»]
2PS8	X-ray	2.67	A/B	1-374	[»]
2Q9Y	X-ray	2.85	A/B	1-374	[»]
2Q9Z	X-ray	2.95	A/B	1-374	[»]

ProteinModelPortal

P13513.

SMR

P13513. Positions 1-354.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

4.2.3.6. 2364.

UniPathway

UPA00267.

Family and domain databases

Gene3D

1.10.600.10. 1 hit.

InterPro

IPR008949. Terpenoid_synth.
IPR010458. TRI5_ascomyc.
IPR024652. Trichodiene_synth.
[Graphical view]

Pfam

PF06330. TRI5. 1 hit.
[Graphical view]

PIRSF

PIRSF001388. TRI5. 1 hit.

SUPFAM

SSF48576. Terpenoid_synth. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P13513.

Entry information

Entry name

TRI5_FUSSP

Accession

Primary (citable) accession number: P13513

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program