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Protein

Quercetin 2,3-dioxygenase

Gene
N/A
Organism
Aspergillus japonicus
Status
Reviewed-Annotation score: 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

Cu cationNote: Binds 1 copper ion per subunit.

Enzyme regulationi

Inhibited by diethyldithiocarbamate and kojic acid.

Pathwayi: quercetin degradation

This protein is involved in the pathway quercetin degradation, which is part of Flavonoid metabolism.
View all proteins of this organism that are known to be involved in the pathway quercetin degradation and in Flavonoid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi66Copper1
Binding sitei66Substrate1
Metal bindingi68Copper1
Metal bindingi73Copper1
Binding sitei73Substrate1
Metal bindingi112Copper1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16751.
BRENDAi1.13.11.24. 513.
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)DescriptionActionsGraphical viewLength
Mutagenesisi73E → Q: 1000-fold decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000971341 – 350Quercetin 2,3-dioxygenaseAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi90N-linked (GlcNAc...)1
Glycosylationi109N-linked (GlcNAc...)1
Glycosylationi142N-linked (GlcNAc...)1
Glycosylationi191N-linked (GlcNAc...)1
Glycosylationi248N-linked (GlcNAc...)1

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

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi17 – 19Combined sources3
Beta strandi28 – 30Combined sources3
Beta strandi33 – 39Combined sources7
Helixi41 – 44Combined sources4
Beta strandi49 – 55Combined sources7
Beta strandi72 – 87Combined sources16
Beta strandi94 – 99Combined sources6
Beta strandi103 – 106Combined sources4
Beta strandi111 – 116Combined sources6
Beta strandi121 – 130Combined sources10
Helixi134 – 139Combined sources6
Beta strandi140 – 142Combined sources3
Beta strandi162 – 164Combined sources3
Helixi166 – 169Combined sources4
Helixi170 – 175Combined sources6
Beta strandi193 – 198Combined sources6
Beta strandi200 – 203Combined sources4
Beta strandi215 – 217Combined sources3
Turni219 – 221Combined sources3
Beta strandi224 – 227Combined sources4
Beta strandi233 – 239Combined sources7
Helixi241 – 244Combined sources4
Helixi245 – 247Combined sources3
Beta strandi249 – 256Combined sources8
Beta strandi274 – 281Combined sources8
Beta strandi283 – 287Combined sources5
Beta strandi293 – 295Combined sources3
Beta strandi300 – 303Combined sources4
Beta strandi309 – 329Combined sources21
Helixi330 – 337Combined sources8
Beta strandi338 – 341Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIC2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 145Cupin 1Add BLAST145
Regioni146 – 205LinkerAdd BLAST60
Regioni206 – 350Cupin 2Add BLAST145

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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00724.
BioCyciMetaCyc:MONOMER-16751.
BRENDAi1.13.11.24. 513.

Miscellaneous databases

EvolutionaryTraceiQ7SIC2.

Family and domain databases

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

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: November 2, 2016
This is version 57 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.