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Q7SIC2

- QDOI_ASPJA

UniProt

Q7SIC2 - QDOI_ASPJA

Protein

Quercetin 2,3-dioxygenase

Gene
N/A
Organism
Aspergillus japonicus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    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

    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

    DTSSLIVEDA PDHVRPYVIR HYSHARAVTV DTQLYRFYVT GPSSGYAFTL    50
    MGTNAPHSDA LGVLPHIHQK HYENFYCNKG SFQLWAQSGN ETQQTRVLSS 100
    GDYGSVPRNV THTFQIQDPD TEMTGVIVPG GFEDLFYYLG TNATDTTHTP 150
    YIPSSSDSSS TTGPDSSTIS TLQSFDVYAE LSFTPRTDTV NGTAPANTVW 200
    HTGANALAST AGDPYFIANG WGPKYLNSQY GYQIVAPFVT ATQAQDTNYT 250
    LSTISMSTTP STVTVPTWSF PGACAFQVQE GRVVVQIGDY AATELGSGDV 300
    AFIPGGVEFK YYSEAYFSKV LFVSSGSDGL DQNLVNGGEE WSSVSFPADW 350
    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