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Reviewed, UniProtKB/Swiss-Prot Q9ZWQ9 (FLS_CITUN)

Last modified November 4, 2008. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Flavonol synthase/flavanone 3-hydroxylase
    EC=1.14.11.23
    EC=1.14.11.9
Alternative name(s):
    CitFLS
      Short name=FLS
Gene names
Name: FLS
OrganismCitrus unshiu (Satsuma orange)
Taxonomic identifier55188 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IISapindalesRutaceaeCitrus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

Catalytic activity

A dihydroflavonol + 2-oxoglutarate + O(2) = a flavonol + succinate + CO(2) + H(2)O.

A flavanone + 2-oxoglutarate + O(2) = a dihydroflavonol + succinate + CO(2).

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 ascorbate molecule per subunit By similarity.

Pathway

Secondary metabolite biosynthesis; flavonoid biosynthesis.

Subcellular location

CytoplasmBy similarity.

Tissue specificity

In the juice sacs/segment epidermis (edible part) at the early developmental stage.

Developmental stage

Increases in the peel during fruit maturation.

Sequence similarities

Belongs to the iron/ascorbate-dependent oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Flavonol synthase/flavanone 3-hydroxylase
PRO_0000067292

Sites

Metal binding2211Iron By similarity
Metal binding2231Iron By similarity
Metal binding2771Iron By similarity

Experimental info

Mutagenesis681G → A: Reduces activity 95%
Mutagenesis681G → P: Results in complete loss of activity
Mutagenesis2071P → G: No effect
Mutagenesis2611G → A: Reduces activity 95%
Mutagenesis2611G → P: Results in complete loss of activity

Sequences

Sequence LengthMass (Da)Tools
Q9ZWQ9-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 157E1AFA4C47564B

FASTA33537,899
        10         20         30         40         50         60 
MEVERVQAIA SLSHSNGTIP AEFIRPEKEQ PASTTYHGPA PEIPTIDLDD PVQDRLVRSI 

        70         80         90        100        110        120 
AEASREWGIF QVTNHGIPSD LICKLQAVGK EFFELPQEEK EVYSRPADAK DVQGYGTKLQ 

       130        140        150        160        170        180 
KEVEGKKSWV DHLFHRVWPP SSINYRFWPK NPPSYRAVNE EYAKYMREVV DKLFTYLSLG 

       190        200        210        220        230        240 
LGVEGGVLKE AAGGDDIEYM LKINYYPPCP RPDLALGVVA HTDLSALTVL VPNEVPGLQV 

       250        260        270        280        290        300 
FKDDRWIDAK YIPNALVIHI GDQIEILSNG KYKAVLHRTT VNKDKTRMSW PVFLEPPADT 

       310        320        330 
VVGPLPQLVD DENPPKYKAK KFKDYSYCKL NKLPQ 

« Hide

References

[1]"Flavonol synthase gene expression during citrus fruit development."
Moriguchi T., Kita M., Ogawa K., Tomono Y., Endo T., Omura M.
Physiol. Plantarum 114:251-258(2002) [PubMed: 11903972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Satsuma Mandarin.
[2]"Functional expression and mutational analysis of flavonol synthase from Citrus unshiu."
Wellmann F., Lukacin R., Moriguchi T., Britsch L., Schiltz E., Matern U.
Eur. J. Biochem. 269:4134-4142(2002) [PubMed: 12180990] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-14, CHARACTERIZATION, MUTAGENESIS OF GLY-68 AND GLY-261.
[3]"Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase."
Lukacin R., Wellmann F., Britsch L., Martens S., Matern U.
Phytochemistry 62:287-292(2003) [PubMed: 12620339] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

AB011796 mRNA. Translation: BAA36554.1.

3D structure databases

HSSPHSSP built from PDB template 1GP6 based on UniProtKB Q96323.
ModBaseSearch...

Family and domain databases

InterProIPR005123. 2OG-FeII_Oase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFLS_CITUN
AccessionPrimary (citable) accession number: Q9ZWQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: May 1, 1999
Last modified: November 4, 2008
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents