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Reviewed, UniProtKB/Swiss-Prot P42106 (QDOI_BACSU)

Last modified May 5, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Quercetin 2,3-dioxygenase
      Short name=Quercetinase
    EC=1.13.11.24
Alternative name(s):
    Flavonol 2,4-dioxygenase
Gene names
Name: qdoI
Synonyms: yxaG
Ordered Locus Names: BSU39980
ORF Names: S14G
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. Ref.3

Catalytic activity

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

Cofactor

Binds 2 Fe2+ ions per subunit. Ref.4

Pathway

Flavonoid metabolism; quercetin degradation.

Subunit structure

Homodimer.

Biophysicochemical properties

Kinetic parameters:

KM=3.8 µM for quercetin

Vmax=2 µmol/min/mg enzyme

Mass spectrometry

Molecular mass is 38658 Da from positions 1 - 337. Determined by MALDI. Ref.3

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Ontologies

Keywords
   DomainRepeat
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quercetin 2,3-dioxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Quercetin 2,3-dioxygenase
PRO_0000097135

Regions

Region1 – 148148Cupin 1
Region177 – 333157Cupin 2

Sites

Metal binding621Iron 1
Metal binding641Iron 1
Metal binding691Iron 1
Metal binding1031Iron 1
Metal binding2341Iron 2
Metal binding2361Iron 2
Metal binding2411Iron 2
Metal binding2751Iron 2

Secondary structure

1 ................................................................ 337
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P42106-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F9F3255C9D8C215A

FASTA33737,585
        10         20         30         40         50         60 
MKTLCTHSLP KEKMPYLLRS GEGERYLFGR QVATVMANGR STGDLFEIVL LSGGKGDAFP 

        70         80         90        100        110        120 
LHVHKDTHEG ILVLDGKLEL TLDGERYLLI SGDYANIPAG TPHSYRMQSH RTRLVSYTMK 

       130        140        150        160        170        180 
GNVAHLYSVI GNPYDHAEHP PYASEEVSNE RFAEAAAVAT IVFLDEAKPA CSAKLAELTE 

       190        200        210        220        230        240 
LPDGAVPYVL ESGEGDRLLT GDQLHRIVAA QKNTDGQFIV VSSEGPKGDR IVDHYHEYHT 

       250        260        270        280        290        300 
ETFYCLEGQM TMWTDGQEIQ LNPGDFLHVP ANTVHSYRLD SHYTKMVGVL VPGLFEPFFR 

       310        320        330 
TLGDPYEGHI FPCKPQALRF DRILQNIEAL DLKVMKP

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons."
Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.
DNA Res. 2:61-69(1995) [PubMed: 7584049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BGSC1A1.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase."
Bowater L., Fairhurst S.A., Just V.J., Bornemann S.
FEBS Lett. 557:45-48(2004) [PubMed: 14741339] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
Strain: 168.
[4]"Evidence for a new metal in a known active site: purification and characterization of an iron-containing quercetin 2,3-dioxygenase from Bacillus subtilis."
Barney B.M., Schaab M.R., LoBrutto R., Francisco W.A.
Protein Expr. Purif. 35:131-141(2004) [PubMed: 15039076] [Abstract]
Cited for: CHARACTERIZATION, COFACTOR.
[5]"The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)."
Gopal B., Madan L.L., Betz S.F., Kossiakoff A.A.
Biochemistry 44:193-201(2005) [PubMed: 15628860] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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Cross-references

Sequence databases

AB005554 Genomic DNA. Translation: BAA21586.1.
Z99124 Genomic DNA. Translation: CAB16035.1.
PIRF70071.
RefSeqNP_391878.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1Y3TX-ray2.40A/B1-337[»]
2H0VX-ray2.60A/B1-337[»]
ModBaseSearch...

Genome annotation databases

GeneID937689.
GenomeReviewsGene locus BSU39980 in contig AL009126_GR.
KEGGbsu:BSU39980.
NMPDRfig|224308.1.peg.4004.

Organism-specific databases

SubtiListBG11109. qdoI. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP42106.
OMAP42106. HAPAGTI.

Enzyme and pathway databases

BioCycBSUB224308:BSU3995-MON.
BRENDA1.13.11.24. 150.

Family and domain databases

InterProIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
PfamPF07883. Cupin_2. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameQDOI_BACSU
AccessionPrimary (citable) accession number: P42106
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 5, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents