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Protein

Quercetin 2,3-dioxygenase

Gene

qdoI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Catalytic activityi

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

Cofactori

Fe2+1 PublicationNote: Binds 2 Fe2+ ions per subunit.1 Publication

Kineticsi

  1. KM=3.8 µM for quercetin1 Publication
  1. Vmax=2 µmol/min/mg enzyme1 Publication

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 bindingi62Iron 11
Metal bindingi64Iron 11
Metal bindingi69Iron 11
Metal bindingi103Iron 11
Metal bindingi234Iron 21
Metal bindingi236Iron 21
Metal bindingi241Iron 21
Metal bindingi275Iron 21

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU39980-MONOMER.
BRENDAi1.13.11.24. 658.
SABIO-RKP42106.
UniPathwayiUPA00724.

Names & Taxonomyi

Protein namesi
Recommended name:
Quercetin 2,3-dioxygenase (EC:1.13.11.24)
Short name:
Quercetinase
Alternative name(s):
Flavonol 2,4-dioxygenase
Gene namesi
Name:qdoI
Synonyms:yxaG
Ordered Locus Names:BSU39980
ORF Names:S14G
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000971351 – 337Quercetin 2,3-dioxygenaseAdd BLAST337

Proteomic databases

PaxDbiP42106.
PRIDEiP42106.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021561.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi16 – 18Combined sources3
Beta strandi23 – 28Combined sources6
Beta strandi31 – 37Combined sources7
Helixi39 – 42Combined sources4
Beta strandi44 – 53Combined sources10
Beta strandi58 – 63Combined sources6
Beta strandi69 – 76Combined sources8
Beta strandi78 – 82Combined sources5
Beta strandi85 – 89Combined sources5
Beta strandi94 – 97Combined sources4
Beta strandi103 – 107Combined sources5
Beta strandi112 – 119Combined sources8
Helixi125 – 130Combined sources6
Beta strandi131 – 133Combined sources3
Helixi153 – 155Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi195 – 200Combined sources6
Beta strandi203 – 209Combined sources7
Helixi211 – 213Combined sources3
Turni214 – 216Combined sources3
Beta strandi219 – 225Combined sources7
Beta strandi240 – 248Combined sources9
Beta strandi250 – 254Combined sources5
Beta strandi257 – 261Combined sources5
Beta strandi266 – 269Combined sources4
Beta strandi275 – 279Combined sources5
Beta strandi281 – 293Combined sources13
Turni294 – 296Combined sources3
Helixi297 – 302Combined sources6
Beta strandi303 – 305Combined sources3
Beta strandi308 – 310Combined sources3
Helixi320 – 325Combined sources6
Helixi327 – 329Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y3TX-ray2.40A/B1-337[»]
2H0VX-ray2.60A/B1-337[»]
ProteinModelPortaliP42106.
SMRiP42106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42106.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 148Cupin 1Add BLAST148
Regioni177 – 333Cupin 2Add BLAST157

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1917. LUCA.
HOGENOMiHOG000087868.
InParanoidiP42106.
KOiK07155.
OMAiDFLHVPA.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P42106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLCTHSLP KEKMPYLLRS GEGERYLFGR QVATVMANGR STGDLFEIVL
60 70 80 90 100
LSGGKGDAFP LHVHKDTHEG ILVLDGKLEL TLDGERYLLI SGDYANIPAG
110 120 130 140 150
TPHSYRMQSH RTRLVSYTMK GNVAHLYSVI GNPYDHAEHP PYASEEVSNE
160 170 180 190 200
RFAEAAAVAD IVFLDEAKPA CSAKLAELTE LPDGAVPYVL ESGEGDRLLT
210 220 230 240 250
GDQLHRIVAA QKNTDGQFIV VSSEGPKGDR IVDHYHEYHT ETFYCLEGQM
260 270 280 290 300
TMWTDGQEIQ LNPGDFLHVP ANTVHSYRLD SHYTKMVGVL VPGLFEPFFR
310 320 330
TLGDPYEGHI FPCEPQALRF DRILQNIEAL DLKVMKP
Length:337
Mass (Da):37,600
Last modified:July 28, 2009 - v2
Checksum:iA91148E6272AE64C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160D → T in BAA21586 (PubMed:7584049).Curated1
Sequence conflicti314E → K in BAA21586 (PubMed:7584049).Curated1

Mass spectrometryi

Molecular mass is 38658 Da from positions 1 - 337. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21586.1.
AL009126 Genomic DNA. Translation: CAB16035.2.
PIRiF70071.
RefSeqiNP_391878.2. NC_000964.3.
WP_003243000.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16035; CAB16035; BSU39980.
GeneIDi937689.
KEGGibsu:BSU39980.
PATRICi18980064. VBIBacSub10457_4194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21586.1.
AL009126 Genomic DNA. Translation: CAB16035.2.
PIRiF70071.
RefSeqiNP_391878.2. NC_000964.3.
WP_003243000.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y3TX-ray2.40A/B1-337[»]
2H0VX-ray2.60A/B1-337[»]
ProteinModelPortaliP42106.
SMRiP42106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021561.

Proteomic databases

PaxDbiP42106.
PRIDEiP42106.

Protocols and materials databases

DNASUi937689.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16035; CAB16035; BSU39980.
GeneIDi937689.
KEGGibsu:BSU39980.
PATRICi18980064. VBIBacSub10457_4194.

Phylogenomic databases

eggNOGiCOG1917. LUCA.
HOGENOMiHOG000087868.
InParanoidiP42106.
KOiK07155.
OMAiDFLHVPA.

Enzyme and pathway databases

UniPathwayiUPA00724.
BioCyciBSUB:BSU39980-MONOMER.
BRENDAi1.13.11.24. 658.
SABIO-RKP42106.

Miscellaneous databases

EvolutionaryTraceiP42106.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQDOI_BACSU
AccessioniPrimary (citable) accession number: P42106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.