Flavonol synthase/flavanone 3-hydroxylase - Arabidopsis thaliana (Mouse-ear cress)

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Q96330 (FLS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Flavonol synthase/flavanone 3-hydroxylase
EC=1.14.11.23
EC=1.14.11.9

Alternative name(s):
FLS 1

Gene names

Name:	FLS1
Synonyms:	FLS
Ordered Locus Names:	At5g08640
ORF Names:	MAH20.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. In vitro catalyzes the oxidation of both enantiomers of naringenin to give both cis- and trans-dihydrokaempferol. Ref.2 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
Catalytic activity	A dihydroflavonol + 2-oxoglutarate + O₂ = a flavonol + succinate + CO₂ + H₂O. Ref.8 Ref.9 A flavanone + 2-oxoglutarate + O₂ = a dihydroflavonol + succinate + CO₂. Ref.8 Ref.9
Cofactor	Binds 1 ascorbate molecule per subunit By similarity. Binds 1 Fe²⁺ ion per subunit Probable.
Pathway	Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subcellular location	Cytoplasm. Nucleus Ref.17.
Tissue specificity	Expressed in young seedlings (at protein level). Expressed in roots, emerging leaves, shoot-root transition zone, trichomes, flowers and siliques. In cotyledons, expressed mostly on the adaxial side and only in guard cells on the abaxial side. Ref.7 Ref.10 Ref.13 Ref.17
Induction	By light, auxin and 1-aminocyclopropane-1-carboxylic acid (ACC). Ref.1 Ref.2 Ref.10 Ref.16
Disruption phenotype	Accumulation of anthocyanins and glycosylated forms of dihydroflavonols, and drastic reduction of kaempferol, quercitin and favonol glycosides. Ref.2 Ref.13 Ref.15
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.
Biophysicochemical properties	Kinetic parameters: K_M=59 µM for dihydroquercetin. Ref.12

Ontologies

Keywords
Biological process	Flavonoid biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to auxin stimulus Inferred from expression pattern Ref.16. Source: TAIR response to karrikin Inferred from expression pattern PubMed 20351290. Source: TAIR
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW flavonol synthase activity Inferred from direct assay Ref.8. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW naringenin 3-dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 336

336

Flavonol synthase/flavanone 3-hydroxylase

PRO_0000067291

Regions

Domain

196 – 296

101

Fe2OG dioxygenase

Region

204 – 206

2-oxoglutarate binding By similarity

Region

287 – 289

2-oxoglutarate binding Probable

Sites

Metal binding

221

Iron; catalytic Probable

Metal binding

223

Iron; catalytic Probable

Metal binding

277

Iron; catalytic Probable

Experimental info

Mutagenesis

132

H → F: Slightly increases activity. Ref.11 Ref.12

Mutagenesis

132

H → Y: Slightly decreases activity. Ref.11 Ref.12

Mutagenesis

134

F → A: Reduces activity 7-fold. Ref.12

Mutagenesis

134

F → L: Reduces activity 2-fold. Ref.12

Mutagenesis

202

K → M: Reduces activity 25-fold. Ref.12

Mutagenesis

202

K → R: Reduces activity 8-fold. Ref.12

Mutagenesis

221

H → W: Loss of activity. Ref.12

Mutagenesis

223

D → E: Loss of activity. Ref.12

Mutagenesis

277

H → F: Loss of activity. Ref.12

Mutagenesis

287

R → K: Loss of activity. Ref.12

Mutagenesis

289

S → T: Reduces activity 2-fold. Ref.12

Mutagenesis

293

F → A or L: Reduces activity 12-fold. Ref.12

Mutagenesis

295

E → L: Reduces activity 15-fold. Ref.12

Mutagenesis

295

E → Q: Reduces activity 2-fold. Ref.12

Mutagenesis

329

K → N: Reduces activity 4-fold. Ref.11

Sequences

Sequence

Length

Mass (Da)

Tools

Q96330 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 3283E3AFE603D2A9
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FASTA

336

38,282

        10         20         30         40         50         60 
MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV 

        70         80         90        100        110        120 
VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ 

       130        140        150        160        170        180 
KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG 

       190        200        210        220        230        240 
LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV 

       250        260        270        280        290        300 
FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK 

       310        320        330 
IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of flavonol synthase and leucoanthocyanidin dioxygenase genes in Arabidopsis. Further evidence for differential regulation of 'early' and 'late' genes." Pelletier M.K., Murrell J.R., Shirley B.W. Plant Physiol. 113:1437-1445(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY LIGHT. Strain: cv. Landsberg erecta.
[2]	"Knock-out mutants from an En-1 mutagenized Arabidopsis thaliana population generate phenylpropanoid biosynthesis phenotypes." Wisman E., Hartmann U., Sagasser M., Baumann E., Palme K., Hahlbrock K., Saedler H., Weisshaar B. Proc. Natl. Acad. Sci. U.S.A. 95:12432-12437(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INDUCTION BY LIGHT, DISRUPTION PHENOTYPE. Strain: cv. Columbia and cv. Landsberg erecta.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Disruption of specific flavonoid genes enhances the accumulation of flavonoid enzymes and end-products in Arabidopsis seedlings." Pelletier M.K., Burbulis I.E., Winkel-Shirley B. Plant Mol. Biol. 40:45-54(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"In vitro properties of a recombinant flavonol synthase from Arabidopsis thaliana." Prescott A.G., Stamford N.P., Wheeler G., Firmin J.L. Phytochemistry 60:589-593(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]	"Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans." Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J., Schofield C.J. FEBS Lett. 579:5170-5174(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[10]	"Differential combinatorial interactions of cis-acting elements recognized by R2R3-MYB, BZIP, and BHLH factors control light-responsive and tissue-specific activation of phenylpropanoid biosynthesis genes." Hartmann U., Sagasser M., Mehrtens F., Stracke R., Weisshaar B. Plant Mol. Biol. 57:155-171(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[11]	"Structural and mechanistic studies on anthocyanidin synthase catalysed oxidation of flavanone substrates: the effect of C-2 stereochemistry on product selectivity and mechanism." Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C., Schofield C.J. Org. Biomol. Chem. 3:3117-3126(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-132 AND LYS-329.
[12]	"Elucidation of active site residues of Arabidopsis thaliana flavonol synthase provides a molecular platform for engineering flavonols." Chua C.S., Biermann D., Goo K.S., Sim T.S. Phytochemistry 69:66-75(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-132; PHE-134; LYS-202; HIS-221; ASP-223; HIS-277; ARG-287; SER-289; PHE-293 AND GLU-295.
[13]	"Functional analysis of a predicted flavonol synthase gene family in Arabidopsis." Owens D.K., Alerding A.B., Crosby K.C., Bandara A.B., Westwood J.H., Winkel B.S. Plant Physiol. 147:1046-1061(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, DISRUPTION PHENOTYPE. Strain: cv. Wassilewskija.
[14]	"Arabidopsis thaliana expresses a second functional flavonol synthase." Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., Martens S. FEBS Lett. 583:1981-1986(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis thaliana support the in vivo involvement of leucoanthocyanidin dioxygenase." Stracke R., De Vos R.C., Bartelniewoehner L., Ishihara H., Sagasser M., Martens S., Weisshaar B. Planta 229:427-445(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: cv. No-0.
[16]	"Auxin and ethylene induce flavonol accumulation through distinct transcriptional networks." Lewis D.R., Ramirez M.V., Miller N.D., Vallabhaneni P., Ray W.K., Helm R.F., Winkel B.S., Muday G.K. Plant Physiol. 156:144-164(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[17]	"Flavonols accumulate asymmetrically and affect auxin transport in Arabidopsis." Kuhn B.M., Geisler M., Bigler L., Ringli C. Plant Physiol. 156:585-595(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[18]	"The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity." Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R. Plant Physiol. Biochem. 0:0-0(2013) Cited for: REVIEW, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U72631 Genomic DNA. Translation: AAB17393.1. U84258 Genomic DNA. Translation: AAC69362.1. U84259 mRNA. Translation: AAC69363.1. U84260 mRNA. Translation: AAB41504.1. AB006697 Genomic DNA. Translation: BAB10013.1. CP002688 Genomic DNA. Translation: AED91332.1. CP002688 Genomic DNA. Translation: AED91333.1. AY058068 mRNA. Translation: AAL24176.1. BT000494 mRNA. Translation: AAN18063.1. AY086328 mRNA. Translation: AAM64397.1.
IPI	IPI00532962.
RefSeq	NP_001190266.1. NM_001203337.1. NP_196481.1. NM_120951.2.
UniGene	At.8771.
3D structure databases
ProteinModelPortal	Q96330.
SMR	Q96330. Positions 3-330.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96330. 3 interactions.
STRING	3702.AT5G08640.1-P.
Proteomic databases
PaxDb	Q96330.
PRIDE	Q96330.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G08640.1; AT5G08640.1; AT5G08640. AT5G08640.2; AT5G08640.2; AT5G08640.
GeneID	830765.
KEGG	ath:AT5G08640.
Organism-specific databases
TAIR	At5g08640.
Phylogenomic databases
eggNOG	COG3491.
InParanoid	Q96330.
KO	K05278.
OMA	LHRTTVD.
PhylomeDB	Q96330.
ProtClustDB	PLN02704.
Enzyme and pathway databases
UniPathway	UPA00154.
Gene expression databases
ArrayExpress	Q96330.
Genevestigator	Q96330.
GermOnline	AT5G08640. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR026992. DIOX_N. IPR005123. Oxoglu/Fe-dep_dioxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. PF14226. DIOX_N. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FLS1_ARATH

Accession

Primary (citable) accession number: Q96330
Secondary accession number(s): O04730

O04832

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents