Reviewed, UniProtKB/Swiss-Prot Q96330 (FLS1_ARATH)

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
Ordered Locus Names:	At5g08640
ORF Names:	MAH20.20

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	A dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate + CO2 + H2O. A flavanone + 2-oxoglutarate + O2 = a dihydroflavonol + succinate + CO2.
Cofactor	Binds 1 ascorbate molecule per subunit. Binds 1 iron ion per subunit.
Pathway	Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family.

Ontologies

Keywords
Biological process	Flavonoid biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	flavonoid biosynthetic process Inferred from direct assay. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm 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. Source: TAIR iron 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
Sites
	Metal binding	221	1	Iron By similarity
	Metal binding	223	1	Iron By similarity
	Metal binding	277	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96330-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 3283E3AFE603D2A9	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

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: 9112784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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: 9770503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 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: 9405937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. AY058068 mRNA. Translation: AAL24176.1. BT000494 mRNA. Translation: AAN18063.1. AY086328 mRNA. Translation: AAM64397.1.
IPI	IPI00532962.
RefSeq	NP_196481.1.
UniGene	At.8771
3D structure databases
HSSP	HSSP built from PDB template 1GP6 based on UniProtKB Q96323.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96330. 3 interactions.
Proteomic databases
PRIDE	Q96330.
ProMEX	Q96330.
Genome annotation databases
GeneID	830765.
GenomeReviews	Gene locus AT5G08640 in contig BA000015_GR.
KEGG	ath:AT5G08640.
NMPDR	fig|3702.1.peg.23017.
Organism-specific databases
TAIR	At5g08640.
Phylogenomic databases
OMA	Q96330. REVNEEY.
Enzyme and pathway databases
BRENDA	1.14.11.23. 302. 1.14.11.9. 302.
Gene expression databases
ArrayExpress	Q96330.
GermOnline	AT5G08640. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_Oase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FLS1_ARATH

Accession

Primary (citable) accession number: Q96330
Secondary accession number(s): O04730 , O04731, O04732, O04830, O04831, O04832

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)