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Q7SIC2 (QDOI_ASPJA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Quercetin 2,3-dioxygenase

EC=1.13.11.24
Alternative name(s):
2,3QD
Flavonol 2,4-dioxygenase
Quercetinase
OrganismAspergillus japonicus
Taxonomic identifier34381 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.

Catalytic activity

Quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+.

Cofactor

Binds 1 copper ion per subunit.

Enzyme regulation

Inhibited by diethyldithiocarbamate and kojic acid.

Pathway

Flavonoid metabolism; quercetin degradation.

Subunit structure

Homodimer.

Post-translational modification

The N-linked glycan at Asn-191 consists of Man(5)-GlcNAc2.

Ontologies

Keywords
   DomainRepeat
   LigandCopper
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quercetin 2,3-dioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Quercetin 2,3-dioxygenase
PRO_0000097134

Regions

Region1 – 145145Cupin 1
Region146 – 20560Linker
Region206 – 350145Cupin 2

Sites

Metal binding661Copper
Metal binding681Copper
Metal binding731Copper
Metal binding1121Copper
Binding site661Substrate
Binding site731Substrate

Amino acid modifications

Glycosylation901N-linked (GlcNAc...)
Glycosylation1091N-linked (GlcNAc...)
Glycosylation1421N-linked (GlcNAc...)
Glycosylation1911N-linked (GlcNAc...)
Glycosylation2481N-linked (GlcNAc...)

Experimental info

Mutagenesis731E → Q: 1000-fold decrease in activity. Ref.3

Secondary structure

............................................................ 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7SIC2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 7F33C372D0DFA5D9

FASTA35037,935
        10         20         30         40         50         60 
DTSSLIVEDA PDHVRPYVIR HYSHARAVTV DTQLYRFYVT GPSSGYAFTL MGTNAPHSDA 

        70         80         90        100        110        120 
LGVLPHIHQK HYENFYCNKG SFQLWAQSGN ETQQTRVLSS GDYGSVPRNV THTFQIQDPD 

       130        140        150        160        170        180 
TEMTGVIVPG GFEDLFYYLG TNATDTTHTP YIPSSSDSSS TTGPDSSTIS TLQSFDVYAE 

       190        200        210        220        230        240 
LSFTPRTDTV NGTAPANTVW HTGANALAST AGDPYFIANG WGPKYLNSQY GYQIVAPFVT 

       250        260        270        280        290        300 
ATQAQDTNYT LSTISMSTTP STVTVPTWSF PGACAFQVQE GRVVVQIGDY AATELGSGDV 

       310        320        330        340        350 
AFIPGGVEFK YYSEAYFSKV LFVSSGSDGL DQNLVNGGEE WSSVSFPADW 

« Hide

References

[1]"Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights."
Steiner R.A., Kooter I.M., Dijkstra B.W.
Biochemistry 41:7955-7962(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DIETHYLDITHIOCARBAMATE AND KOJIC ACID.
[2]"Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase."
Steiner R.A., Kalk K.H., Dijkstra B.W.
Proc. Natl. Acad. Sci. U.S.A. 99:16625-16630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KAEMPFEROL AND QUERCETIN.
[3]"Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus."
Fusetti F., Schroeter K.H., Steiner R.A., van Noort P.I., Pijning T., Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W.
Structure 10:259-268(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), MUTAGENESIS OF GLU-73.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQGX-ray1.70A/B/C/D1-350[»]
1GQHX-ray2.15A/B/C/D1-350[»]
1H1IX-ray1.75A/B/C/D1-350[»]
1H1MX-ray1.90A/B/C/D1-350[»]
1JUHX-ray1.60A/B/C/D1-350[»]
ProteinModelPortalQ7SIC2.
SMRQ7SIC2. Positions 3-350.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16751.
UniPathwayUPA00724.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ7SIC2.

Entry information

Entry nameQDOI_ASPJA
AccessionPrimary (citable) accession number: Q7SIC2
Secondary accession number(s): Q7SIE5, Q7SIE7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 15, 2003
Last modified: November 13, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways