CHS2

Functionⁱ

The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.4 Publications

Catalytic activityⁱ

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO₂.PROSITE-ProRule annotation

Kineticsⁱ

K_M=
4.1 µM for malonyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
K_M=
4.5 µM for 4-coumaroyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
K_M=
2.2 µM for benzoyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
K_M=
4.1 µM for hexanoyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
K_M=
5.1 µM for phenylacetyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.
K_M=
5.2 µM for feruloyl-CoA
3 Publications
Manual assertion based on experiment inⁱ
- Ref.3
  "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."
  Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.
  Biochemistry 39:890-902(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH COENZYME A, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-164; PHE-215; HIS-303 AND ASN-336.
- Ref.4
  "Structure-guided programming of polyketide chain-length determination in chalcone synthase."
  Jez J.M., Bowman M.E., Noel J.P.
  Biochemistry 40:14829-14838(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-256.
- Ref.5
  "Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity."
  Jez J.M., Bowman M.E., Noel J.P.
  Proc. Natl. Acad. Sci. U.S.A. 99:5319-5324(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-215 AND PHE-265.

Pathwayⁱ: flavonoid biosynthesis

This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.
View all proteins of this organism that are known to be involved in the pathway flavonoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	164	Acyl-thioester intermediateCurated	1
Binding siteⁱ	197	Substrate1 Publication	1
Binding siteⁱ	308	Coenzyme A; via amide nitrogen2 Publications	1

GO - Molecular functionⁱ

naringenin-chalcone synthase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10653632

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chalcone biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 10653632
flavonoid biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Flavonoid biosynthesis

Enzyme and pathway databases

BRENDAⁱ	2.3.1.74 3078
SABIO-RKⁱ	P30074
UniPathwayⁱ	UPA00154

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Chalcone synthase 2 (EC:2.3.1.74) Alternative name(s): Naringenin-chalcone synthase 2
Gene namesⁱ	Name:CHS2
Organismⁱ	Medicago sativa (Alfalfa)
Taxonomic identifierⁱ	3879 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › fabids › Fabales › Fabaceae › Papilionoideae › 50 kb inversion clade › NPAAA clade › Hologalegina › IRL clade › Trifolieae › Medicago

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	164	C → A, D or S: Loss of activity. 1 Publication	1
Mutagenesisⁱ	215	F → S, W or Y: Drastically reduces catalytic efficiency. 2 Publications	1
Mutagenesisⁱ	256	G → A: Decreases catalytic efficiency 2-fold. 1 Publication	1
Mutagenesisⁱ	256	G → F or L: Drastically reduces catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	256	G → V: Decreases catalytic efficiency 7-fold. 1 Publication	1
Mutagenesisⁱ	265	F → V: Decreases catalytic efficiency 2-fold. 1 Publication	1
Mutagenesisⁱ	303	H → A, D, N or T: Drastically reduces catalytic efficiency. 1 Publication	1
Mutagenesisⁱ	303	H → Q: Decreases catalytic efficiency 13-fold. 1 Publication	1
Mutagenesisⁱ	336	N → A, D, H, K or Q: Drastically reduces catalytic efficiency. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000216007	1 – 389	Chalcone synthase 2Add BLAST		389

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 11	Combined sources	8
Beta strandⁱ	18 – 25	Combined sources	8
Beta strandⁱ	30 – 32	Combined sources	3
Helixⁱ	33 – 35	Combined sources	3
Helixⁱ	36 – 43	Combined sources	8
Helixⁱ	50 – 62	Combined sources	13
Beta strandⁱ	67 – 69	Combined sources	3
Helixⁱ	74 – 79	Combined sources	6
Helixⁱ	81 – 84	Combined sources	4
Beta strandⁱ	85 – 87	Combined sources	3
Helixⁱ	91 – 117	Combined sources	27
Helixⁱ	121 – 123	Combined sources	3
Beta strandⁱ	126 – 133	Combined sources	8
Beta strandⁱ	136 – 138	Combined sources	3
Helixⁱ	140 – 148	Combined sources	9
Beta strandⁱ	155 – 161	Combined sources	7
Helixⁱ	166 – 179	Combined sources	14
Beta strandⁱ	185 – 192	Combined sources	8
Helixⁱ	194 – 196	Combined sources	3
Helixⁱ	206 – 214	Combined sources	9
Beta strandⁱ	218 – 227	Combined sources	10
Turnⁱ	230 – 232	Combined sources	3
Beta strandⁱ	237 – 246	Combined sources	10
Beta strandⁱ	253 – 259	Combined sources	7
Beta strandⁱ	262 – 267	Combined sources	6
Helixⁱ	271 – 287	Combined sources	17
Helixⁱ	288 – 290	Combined sources	3
Beta strandⁱ	297 – 302	Combined sources	6
Helixⁱ	307 – 317	Combined sources	11
Helixⁱ	321 – 324	Combined sources	4
Helixⁱ	325 – 334	Combined sources	10
Helixⁱ	338 – 340	Combined sources	3
Helixⁱ	341 – 355	Combined sources	15
Turnⁱ	361 – 364	Combined sources	4
Beta strandⁱ	366 – 374	Combined sources	9
Turnⁱ	375 – 377	Combined sources	3
Beta strandⁱ	378 – 386	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	P30074
SMRⁱ	P30074
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P30074

EvolutionaryTraceⁱ

P30074

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	55 – 62	Coenzyme A binding		8
Regionⁱ	216 – 217	Substrate binding		2

Sequence similaritiesⁱ

Belongs to the chalcone/stilbene synthases family.Curated

Family and domain databases

Gene3Dⁱ	3.40.47.10, 2 hits
InterProⁱ	View protein in InterPro IPR012328 Chalcone/stilbene_synth_C IPR018088 Chalcone/stilbene_synthase_AS IPR001099 Chalcone/stilbene_synthase_N IPR011141 Polyketide_synthase_type-III IPR016039 Thiolase-like
PANTHERⁱ	PTHR11877 PTHR11877, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02797 Chal_sti_synt_C, 1 hit PF00195 Chal_sti_synt_N, 1 hit
PIRSFⁱ	PIRSF000451 PKS_III, 1 hit
SUPFAMⁱ	SSF53901 SSF53901, 2 hits
PROSITEⁱ	View protein in PROSITE PS00441 CHALCONE_SYNTH, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P30074-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT 
        60         70         80         90        100
ELKEKFQRMC DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV 
       110        120        130        140        150
EVPRLGKEAA VKAIKEWGQP KSKITHLIVC TTSGVDMPGA DYQLTKLLGL 
       160        170        180        190        200
RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN NKGARVLVVC SEVTAVTFRG 
       210        220        230        240        250
PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV WTAQTIAPDS 
       260        270        280        290        300
EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW 
       310        320        330        340        350
IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR 
       360        370        380 
KKSTQNGLKT TGEGLEWGVL FGFGPGLTIE TVVLRSVAI

Length:389

Mass (Da):42,706

Last modified:April 1, 1993 - v1

Checksum:ⁱE03422EE332A5408

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L02902 mRNA Translation: AAA02824.1
PIRⁱ	S35164

Protein	Similar proteins		Species	Score	Length	Source
P30074	Chalcone synthase		ONOVI		390	UniRef90_P30074
Chalcone synthase 1		CICAR		389
Chalcone synthase 8		MEDSA		389
Chalcone synthase 6		TRISU		389
Chalcone synthase 6		PEA		389
+189

Protein	Similar proteins		Species	Score	Length	Source
P30074	Chalcone synthase		ONOVI		390	UniRef50_P30074
Chalcone synthase 6		PEA		389
Chalcone synthase 1		TRISU		389
Chalcone synthase 1		MEDSA		389
Chalcone synthase 1		CICAR		389
+348

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L02902 mRNA Translation: AAA02824.1
PIRⁱ	S35164

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
	1BI5	X-ray	1.56	A	1-389	[»]
	1BQ6	X-ray	1.56	A	2-389	[»]
	1CGK	X-ray	1.84	A	1-389	[»]
	1CGZ	X-ray	1.70	A	1-389	[»]
	1CHW	X-ray	1.90	A/B	1-389	[»]
	1CML	X-ray	1.69	A	1-389	[»]
	1D6F	X-ray	1.69	A	1-389	[»]
	1D6H	X-ray	2.15	A	3-389	[»]
	1D6I	X-ray	2.00	A/B	2-389	[»]
	1I86	X-ray	1.50	A	1-389	[»]
	1I88	X-ray	1.45	A/B	1-389	[»]
	1I89	X-ray	1.86	A/B	1-389	[»]
	1I8B	X-ray	1.95	A/B	1-389	[»]
	1JWX	X-ray	1.63	A	1-389	[»]
	1U0V	X-ray	1.90	A/B	1-389	[»]
	1U0W	X-ray	2.00	A/B/C/D	1-389	[»]
ProteinModelPortalⁱ	P30074
SMRⁱ	P30074
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

UniPathwayⁱ	UPA00154
BRENDAⁱ	2.3.1.74 3078
SABIO-RKⁱ	P30074

Miscellaneous databases

EvolutionaryTraceⁱ	P30074

EvolutionaryTraceⁱ

P30074

Family and domain databases

Gene3Dⁱ	3.40.47.10, 2 hits
InterProⁱ	View protein in InterPro IPR012328 Chalcone/stilbene_synth_C IPR018088 Chalcone/stilbene_synthase_AS IPR001099 Chalcone/stilbene_synthase_N IPR011141 Polyketide_synthase_type-III IPR016039 Thiolase-like
PANTHERⁱ	PTHR11877 PTHR11877, 1 hit
Pfamⁱ	View protein in Pfam PF02797 Chal_sti_synt_C, 1 hit PF00195 Chal_sti_synt_N, 1 hit
PIRSFⁱ	PIRSF000451 PKS_III, 1 hit
SUPFAMⁱ	SSF53901 SSF53901, 2 hits
PROSITEⁱ	View protein in PROSITE PS00441 CHALCONE_SYNTH, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CHS2_MEDSA
Accessionⁱ	P30074Primary (citable) accession number: P30074
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
	Last sequence update:	April 1, 1993
	Last modified:	September 12, 2018
	This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Plant Protein Annotation Program

UniProtKB

UniParc

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Annotation systems

Supporting data

UniProtKB - P30074 (CHS2_MEDSA)

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Chalcone synthase 2

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

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: flavonoid 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 quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<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

<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

Protocols and materials 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

Kineticsⁱ

Pathwayⁱ: flavonoid biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ