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Q7SIC2

- QDOI_ASPJA

UniProt

Q7SIC2 - QDOI_ASPJA

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Protein

Quercetin 2,3-dioxygenase

Gene
N/A
Organism
Aspergillus japonicus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Binds 1 copper ion per subunit.

Enzyme regulationi

Inhibited by diethyldithiocarbamate and kojic acid.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Copper
Binding sitei66 – 661Substrate
Metal bindingi68 – 681Copper
Metal bindingi73 – 731Copper
Binding sitei73 – 731Substrate
Metal bindingi112 – 1121Copper

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. quercetin 2,3-dioxygenase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16751.
UniPathwayiUPA00724.

Names & Taxonomyi

Protein namesi
Recommended name:
Quercetin 2,3-dioxygenase (EC:1.13.11.24)
Alternative name(s):
2,3QD
Flavonol 2,4-dioxygenase
Quercetinase
OrganismiAspergillus japonicus
Taxonomic identifieri34381 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731E → Q: 1000-fold decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Quercetin 2,3-dioxygenasePRO_0000097134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)
Glycosylationi109 – 1091N-linked (GlcNAc...)
Glycosylationi142 – 1421N-linked (GlcNAc...)
Glycosylationi191 – 1911N-linked (GlcNAc...)
Glycosylationi248 – 2481N-linked (GlcNAc...)

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Beta strandi17 – 193
Beta strandi28 – 303
Beta strandi33 – 397
Helixi41 – 444
Beta strandi49 – 557
Beta strandi72 – 8716
Beta strandi94 – 996
Beta strandi103 – 1064
Beta strandi111 – 1166
Beta strandi121 – 13010
Helixi134 – 1396
Beta strandi140 – 1423
Beta strandi162 – 1643
Helixi166 – 1694
Helixi170 – 1756
Beta strandi193 – 1986
Beta strandi200 – 2034
Beta strandi215 – 2173
Turni219 – 2213
Beta strandi224 – 2274
Beta strandi233 – 2397
Helixi241 – 2444
Helixi245 – 2473
Beta strandi249 – 2568
Beta strandi274 – 2818
Beta strandi283 – 2875
Beta strandi293 – 2953
Beta strandi300 – 3034
Beta strandi309 – 32921
Helixi330 – 3378
Beta strandi338 – 3414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ7SIC2.
SMRiQ7SIC2. Positions 3-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIC2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 145145Cupin 1Add
BLAST
Regioni146 – 20560LinkerAdd
BLAST
Regioni206 – 350145Cupin 2Add
BLAST

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7SIC2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
DTSSLIVEDA PDHVRPYVIR HYSHARAVTV DTQLYRFYVT GPSSGYAFTL
60 70 80 90 100
MGTNAPHSDA LGVLPHIHQK HYENFYCNKG SFQLWAQSGN ETQQTRVLSS
110 120 130 140 150
GDYGSVPRNV THTFQIQDPD TEMTGVIVPG GFEDLFYYLG TNATDTTHTP
160 170 180 190 200
YIPSSSDSSS TTGPDSSTIS TLQSFDVYAE LSFTPRTDTV NGTAPANTVW
210 220 230 240 250
HTGANALAST AGDPYFIANG WGPKYLNSQY GYQIVAPFVT ATQAQDTNYT
260 270 280 290 300
LSTISMSTTP STVTVPTWSF PGACAFQVQE GRVVVQIGDY AATELGSGDV
310 320 330 340 350
AFIPGGVEFK YYSEAYFSKV LFVSSGSDGL DQNLVNGGEE WSSVSFPADW
Length:350
Mass (Da):37,935
Last modified:December 15, 2003 - v1
Checksum:i7F33C372D0DFA5D9
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GQG X-ray 1.70 A/B/C/D 1-350 [» ]
1GQH X-ray 2.15 A/B/C/D 1-350 [» ]
1H1I X-ray 1.75 A/B/C/D 1-350 [» ]
1H1M X-ray 1.90 A/B/C/D 1-350 [» ]
1JUH X-ray 1.60 A/B/C/D 1-350 [» ]
ProteinModelPortali Q7SIC2.
SMRi Q7SIC2. Positions 3-350.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00724 .
BioCyci MetaCyc:MONOMER-16751.

Miscellaneous databases

EvolutionaryTracei Q7SIC2.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiQDOI_ASPJA
AccessioniPrimary (citable) accession number: Q7SIC2
Secondary accession number(s): Q7SIE5, Q7SIE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 15, 2003
Last modified: October 1, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3