TRI5

Functionⁱ

Trichodiene synthase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:2817906).

The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:3800398, PubMed:7873527, PubMed:8823172).

Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333).

TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519).

Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042).

During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042).

More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533).

Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973).

TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973).

A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041).

A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated by the acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533).

A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047).

Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755).

12 Publications

Miscellaneous

Trichothecenes are sesquiterpenoid toxins that act by inhibiting protein biosynthesis.Curated

Catalytic activityⁱ

(2E,6E)-farnesyl diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
diphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
trichodiene
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
5 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides."
  Hohn T.M., Vanmiddlesworth F.
  Arch. Biochem. Biophys. 251:756-761(1986) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, PATHWAY.
- Ref.8
  "Trichodiene synthase. Identification of active site residues by site-directed mutagenesis."
  Cane D.E., Shim J.H., Xue Q., Fitzsimons B.C., Hohn T.M.
  Biochemistry 34:2480-2488(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-146; CYS-190; ARG-304 AND TYR-305.
- Ref.11
  "Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis."
  Cane D.E., Xue Q., Fitzsimons B.C.
  Biochemistry 35:12369-12376(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, DOMAIN, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-100; ASP-101 AND ASP-104.
- Ref.22
  "Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase."
  Vedula L.S., Cane D.E., Christianson D.W.
  Biochemistry 44:12719-12727(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, MUTAGENESIS OF ARG-304, CATALYTIC ACTIVITY.
- Ref.24
  "Exploring biosynthetic diversity with trichodiene synthase."
  Vedula L.S., Zhao Y., Coates R.M., Koyama T., Cane D.E., Christianson D.W.
  Arch. Biochem. Biophys. 466:260-266(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND INHIBITOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
EC:
4.2.3.6
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
5 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides."
  Hohn T.M., Vanmiddlesworth F.
  Arch. Biochem. Biophys. 251:756-761(1986) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, PATHWAY.
- Ref.8
  "Trichodiene synthase. Identification of active site residues by site-directed mutagenesis."
  Cane D.E., Shim J.H., Xue Q., Fitzsimons B.C., Hohn T.M.
  Biochemistry 34:2480-2488(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-146; CYS-190; ARG-304 AND TYR-305.
- Ref.11
  "Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis."
  Cane D.E., Xue Q., Fitzsimons B.C.
  Biochemistry 35:12369-12376(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, DOMAIN, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-100; ASP-101 AND ASP-104.
- Ref.22
  "Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase."
  Vedula L.S., Cane D.E., Christianson D.W.
  Biochemistry 44:12719-12727(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, MUTAGENESIS OF ARG-304, CATALYTIC ACTIVITY.
- Ref.24
  "Exploring biosynthetic diversity with trichodiene synthase."
  Vedula L.S., Zhao Y., Coates R.M., Koyama T., Cane D.E., Christianson D.W.
  Arch. Biochem. Biophys. 466:260-266(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND INHIBITOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
(2E,6E)-farnesyl diphosphate
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=
diphosphate
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+
trichodiene
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Cofactorⁱ

Mg²⁺6 Publications, Mn²⁺1 PublicationNote: Some of the cofactor binding sites show unusual localization within the protein.Curated

Activity regulationⁱ

Benzyl triethylammonium cation (BTAC) acts as a competitive inhibitor of trichodiene synthase reaction in the presence of pyrophosphate (PPi) (PubMed:17678871).1 Publication

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 6.75-7.75.1 Publication

Pathwayⁱ: trichothecene biosynthesis

This protein is involved in the pathway trichothecene biosynthesis, which is part of Sesquiterpene biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway trichothecene biosynthesis and in Sesquiterpene biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	100	Magnesium 1Combined sources1 Publication	1
Metal bindingⁱ	164	Magnesium 1Combined sources1 Publication	1
Metal bindingⁱ	225	Magnesium 2Combined sources3 Publications	1
Metal bindingⁱ	229	Magnesium 2Combined sources3 Publications	1
Metal bindingⁱ	233	Magnesium 2Combined sources3 Publications	1
Metal bindingⁱ	239	Magnesium 3Combined sources2 Publications	1
Metal bindingⁱ	241	Magnesium 3; via carbonyl oxygenCombined sources2 Publications	1
Binding siteⁱ	295	(4s)-7-azabisabolene; inhibitorCombined sources1 Publication	1

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
trichodiene synthase activity Source: UniProtKB-EC

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

sesquiterpenoid biosynthetic process Source: InterPro

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	4.2.3.6, 2364
UniPathwayⁱ	UPA00267

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Trichodiene synthase1 Publication (EC:4.2.3.65 Publications) Alternative name(s): Core trichothecene cluster (CTC) protein 51 Publication Sesquiterpene cyclase TRI51 Publication Short name: TS1 Publication
Gene namesⁱ	Name:TRI51 Publication Synonyms:TOX 5
Organismⁱ	Fusarium sporotrichioides
Taxonomic identifierⁱ	5514 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Fusarium › Fusarium sambucinum species complex

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	100	D → E: Does not significantly perturb the overall structure of trichodiene synthase but leads to an increased KM, a reduction in kcat, as well as to the production of anomalous sesquiterpene products in addition to trichodiene when incubated with farnesyl diphosphate. 2 Publications	1
Mutagenesisⁱ	101	D → E: Leads to an increased KM for Mg(2+), a reduction in kcat, as well as to the production of anomalous sesquiterpene products in addition to trichodiene when incubated with farnesyl diphosphate. 1 Publication	1
Mutagenesisⁱ	104	D → E: Does not significantly affect the KM and kcat for farnesyl diphosphate. 1 Publication	1
Mutagenesisⁱ	146	C → F: Leads to the loss of activity. 1 Publication	1
Mutagenesisⁱ	190	C → F: Increases the KM for farnesyl diphosphate by about 1.3-fold and reduces the kcat by about 2000-fold. 1 Publication	1
Mutagenesisⁱ	225	N → D: Increases the KM for farnesyl diphosphate by about 6-fold and reduces the kcat by about 28-fold. Leads to complete loss of activity; when associated with S-229. 1 Publication	1
Mutagenesisⁱ	229	S → T: Increases the KM for farnesyl diphosphate by about 77-fold and reduces the kcat by about 9-fold. Leads to complete loss of activity; when associated with D-225. 1 Publication	1
Mutagenesisⁱ	295	Y → F: Does not affect the catalytic activity. 1 Publication	1
Mutagenesisⁱ	304	R → K: Does not cause large changes in the overall structure but increases the KM for farnesyl diphosphate by about 25-fold, reduces the kcat by about 200-fold, and leads to conversion of farnesyl diphosphate not only to trichodiene but to at least 2 additional C(15)H(24) hydrocarbons. 2 Publications	1
Mutagenesisⁱ	305	Y → F: Does not cause large changes in the overall structure but increases the KM for farnesyl diphosphate by about 7-fold. 2 Publications	1
Mutagenesisⁱ	305	Y → T: Increases the KM for farnesyl diphosphate by about 80-fold, reduces the kcat by about 120-fold, and leads to the conversion of farneyl diphosphate to an approximately equal mixture of trichodiene and an unidentified sesquiterpene hydrocarbon. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000221584	1 – 374	Trichodiene synthaseAdd BLAST		374

Expressionⁱ

Inductionⁱ

Expression is positively regulated by the trichothecene cluster-specific transcription activator TRI10 (PubMed:12732543). Expression is induced between 18h and 21h growth on GYEP medium (PubMed:16347944). The initial detection of trichothecenes occurs several hours after the initial detection of TRI5 (PubMed:16347944). The initiation of trichothecene biosynthesis occurs with a high concentration of glucose remaining in the culture medium (PubMed:16347944).2 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 19	Combined sources	14
Helixⁱ	29 – 47	Combined sources	19
Helixⁱ	50 – 55	Combined sources	6
Helixⁱ	60 – 77	Combined sources	18
Helixⁱ	83 – 99	Combined sources	17
Helixⁱ	107 – 110	Combined sources	4
Helixⁱ	113 – 119	Combined sources	7
Helixⁱ	126 – 139	Combined sources	14
Helixⁱ	144 – 164	Combined sources	21
Turnⁱ	165 – 167	Combined sources	3
Helixⁱ	177 – 186	Combined sources	10
Helixⁱ	188 – 193	Combined sources	6
Turnⁱ	198 – 200	Combined sources	3
Turnⁱ	203 – 206	Combined sources	4
Helixⁱ	207 – 233	Combined sources	27
Helixⁱ	243 – 251	Combined sources	9
Helixⁱ	255 – 277	Combined sources	23
Beta strandⁱ	278 – 280	Combined sources	3
Helixⁱ	282 – 301	Combined sources	20
Helixⁱ	303 – 305	Combined sources	3
Helixⁱ	308 – 314	Combined sources	7
Helixⁱ	320 – 336	Combined sources	17
Helixⁱ	340 – 342	Combined sources	3
Helixⁱ	348 – 353	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P13513
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P13513

EvolutionaryTraceⁱ

P13513

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	100 – 104	Aspartate-rich domain1 Publication		5

Sequence similaritiesⁱ

Belongs to the trichodiene synthase family.Curated

Family and domain databases

Gene3Dⁱ	1.10.600.10, 1 hit
InterProⁱ	View protein in InterPro IPR008949, Isoprenoid_synthase_dom_sf IPR010458, TRI5_ascomyc IPR024652, Trichodiene_synth
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06330, TRI5, 1 hit
PIRSFⁱ	PIRSF001388, TRI5, 1 hit
SFLDⁱ	SFLDG01021, Trichodiene_Synthase_Like, 1 hit
SUPFAMⁱ	SSF48576, SSF48576, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P13513-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MENFPTEYFL NTTVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP 
        60         70         80         90        100
RQQQLLKVDP KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD 
       110        120        130        140        150
DSKDDPYPTM VNYFDDLQAG REQAHPWWAL VNEHFPNVLR HFGPFCSLNL 
       160        170        180        190        200
IRSTLDFFEG CWIEQYNFGG FPGSHDYPQF LRRMNGLGHC VGASLWPKEQ 
       210        220        230        240        250
FNERSLFLEI TSAIAQMENW MVWVNDLMSF YKEFDDERDQ ISLVKNYVVS 
       260        270        280        290        300
DEISLHEALE KLTQDTLHSS KQMVAVFSDK DPQVMDTIEC FMHGYVTWHL 
       310        320        330        340        350
CDRRYRLSEI YEKVKEEKTE DAQKFCKFYE QAANVGAVSP SEWAYPPVAQ 
       360        370 
LANVRSKDVK EVQKPFLSSI ELVE

Length:374

Mass (Da):44,000

Last modified:January 1, 1990 - v1

Checksum:ⁱ189E8FC1663C3763

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF364179 Genomic DNA Translation: AAD13657.1 AF359360 Genomic DNA Translation: AAK33074.1 AY032745 mRNA Translation: AAK77935.1
PIRⁱ	JU0064, SYFUTP

Genome annotation databases

KEGGⁱ	ag:AAD13657

KEGGⁱ

ag:AAD13657

Protein	Similar proteins		Species	Score	Length	Source
P13513	Trichodiene synthase (Fragment)		FUSLA		111	UniRef100_P13513
Trichodiene synthase (Fragment)		Fusarium sibiricum		111
Trichodiene synthase (Fragment)		FUSSP		111
Trichodiene synthase (Fragment)		Fusarium sp. RBG6915		230
Trichodiene synthase (Fragment)		Fusarium sp. RBG6914		230
+14

Protein	Similar proteins		Species	Score	Length	Source
P13513	Trichodiene synthase		GIBPU		383	UniRef90_P13513
Trichodiene synthase		FUSPO		377
Trichodiene synthase (Fragment)		FUSLA		111
Trichodiene synthase (Fragment)		Fusarium sibiricum		111
Trichodiene synthase (Fragment)		FUSSP		111
+50

Protein	Similar proteins		Species	Score	Length	Source
P13513	Trichodiene synthase		GIBPU		383	UniRef50_P13513
Trichodiene synthase		FUSPO		377
Trichodiene synthase		PARRD		385
Trichodiene synthase		FUSCO		375
Trichodiene synthase		FUSME		375
+176

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF364179 Genomic DNA Translation: AAD13657.1 AF359360 Genomic DNA Translation: AAK33074.1 AY032745 mRNA Translation: AAK77935.1
PIRⁱ	JU0064, SYFUTP

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
SMRⁱ	P13513
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Genome annotation databases

KEGGⁱ	ag:AAD13657

KEGGⁱ

ag:AAD13657

Enzyme and pathway databases

UniPathwayⁱ	UPA00267
BRENDAⁱ	4.2.3.6, 2364

Miscellaneous databases

EvolutionaryTraceⁱ	P13513

EvolutionaryTraceⁱ

P13513

Family and domain databases

Gene3Dⁱ	1.10.600.10, 1 hit
InterProⁱ	View protein in InterPro IPR008949, Isoprenoid_synthase_dom_sf IPR010458, TRI5_ascomyc IPR024652, Trichodiene_synth
Pfamⁱ	View protein in Pfam PF06330, TRI5, 1 hit
PIRSFⁱ	PIRSF001388, TRI5, 1 hit
SFLDⁱ	SFLDG01021, Trichodiene_Synthase_Like, 1 hit
SUPFAMⁱ	SSF48576, SSF48576, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TRI5_FUSSP
Accessionⁱ	P13513Primary (citable) accession number: P13513 Secondary accession number(s): Q7LP67
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
	Last sequence update:	January 1, 1990
	Last modified:	September 29, 2021
	This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

UniProtKB

UniParc

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Annotation systems

Supporting data

UniProtKB - P13513 (TRI5_FUSSP)

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Trichodiene synthase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: trichothecene biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Genome annotation databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: trichothecene biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ