Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q96330 (FLS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. 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:
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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence 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:

KM=59 µM for dihydroquercetin. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Flavonol synthase/flavanone 3-hydroxylase
PRO_0000067291

Regions

Domain196 – 296101Fe2OG dioxygenase
Region204 – 20632-oxoglutarate binding By similarity
Region287 – 28932-oxoglutarate binding Probable

Sites

Metal binding2211Iron; catalytic Probable
Metal binding2231Iron; catalytic Probable
Metal binding2771Iron; catalytic Probable

Experimental info

Mutagenesis1321H → F: Slightly increases activity. Ref.11 Ref.12
Mutagenesis1321H → Y: Slightly decreases activity. Ref.11 Ref.12
Mutagenesis1341F → A: Reduces activity 7-fold. Ref.12
Mutagenesis1341F → L: Reduces activity 2-fold. Ref.12
Mutagenesis2021K → M: Reduces activity 25-fold. Ref.12
Mutagenesis2021K → R: Reduces activity 8-fold. Ref.12
Mutagenesis2211H → W: Loss of activity. Ref.12
Mutagenesis2231D → E: Loss of activity. Ref.12
Mutagenesis2771H → F: Loss of activity. Ref.12
Mutagenesis2871R → K: Loss of activity. Ref.12
Mutagenesis2891S → T: Reduces activity 2-fold. Ref.12
Mutagenesis2931F → A or L: Reduces activity 12-fold. Ref.12
Mutagenesis2951E → L: Reduces activity 15-fold. Ref.12
Mutagenesis2951E → Q: Reduces activity 2-fold. Ref.12
Mutagenesis3291K → N: Reduces activity 4-fold. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q96330 [UniParc].

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

FASTA33638,282
        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' 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. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.
IPIIPI00532962.
RefSeqNP_001190266.1. NM_001203337.1.
NP_196481.1. NM_120951.2.
UniGeneAt.8771.

3D structure databases

ProteinModelPortalQ96330.
SMRQ96330. Positions 3-330.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96330. 3 interactions.
STRING3702.AT5G08640.1-P.

Proteomic databases

PaxDbQ96330.
PRIDEQ96330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G08640.1; AT5G08640.1; AT5G08640.
AT5G08640.2; AT5G08640.2; AT5G08640.
GeneID830765.
KEGGath:AT5G08640.

Organism-specific databases

TAIRAt5g08640.

Phylogenomic databases

eggNOGCOG3491.
InParanoidQ96330.
KOK05278.
OMALHRTTVD.
PhylomeDBQ96330.
ProtClustDBPLN02704.

Enzyme and pathway databases

UniPathwayUPA00154.

Gene expression databases

ArrayExpressQ96330.
GenevestigatorQ96330.
GermOnlineAT5G08640. Arabidopsis thaliana.

Family and domain databases

InterProIPR026992. DIOX_N.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
PF14226. DIOX_N. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFLS1_ARATH
AccessionPrimary (citable) accession number: Q96330
Secondary accession number(s): O04730 expand/collapse secondary AC list , O04731, O04732, O04830, O04831, 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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