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UniProtKB/Swiss-Prot entry P42106


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name QDOI_BACSU
Primary accession number P42106
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 61)
Name and origin of the protein
Protein name Quercetin 2,3-dioxygenase
Synonyms Quercetinase
EC 1.13.11.24
Flavonol 2,4-dioxygenase
Gene name
Name: qdoI
Synonyms: yxaG
OrderedLocusNames: BSU39980
ORFNames: S14G
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / BGSC1A1;
DOI=10.1093/dnares/2.2.61; PubMed=7584049 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
"Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons.";
DNA Res. 2:61-69(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
STRAIN=168;
DOI=10.1016/S0014-5793(03)01439-X; PubMed=14741339 [NCBI, ExPASy, EBI, Israel, Japan]
Bowater L., Fairhurst S.A., Just V.J., Bornemann S.;
"Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase.";
FEBS Lett. 557:45-48(2004).
[4]
CHARACTERIZATION, AND COFACTOR.
DOI=10.1016/j.pep.2004.01.005; PubMed=15039076 [NCBI, ExPASy, EBI, Israel, Japan]
Barney B.M., Schaab M.R., LoBrutto R., Francisco W.A.;
"Evidence for a new metal in a known active site: purification and characterization of an iron-containing quercetin 2,3-dioxygenase from Bacillus subtilis.";
Protein Expr. Purif. 35:131-141(2004).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi0484421; PubMed=15628860 [NCBI, ExPASy, EBI, Israel, Japan]
Gopal B., Madan L.L., Betz S.F., Kossiakoff A.A.;
"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).";
Biochemistry 44:193-201(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB005554; BAA21586.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99124; CAB16035.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F70071; F70071.
RefSeq NP_391878.1; -.
3D structure databases
PDB
1Y3T; X-ray; 2.40 A; A/B=1-337.[ExPASy / RCSB / EBI]
2H0V; X-ray; 2.60 A; A/B=1-337.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1Y3T; -.
2H0V; -.
ModBase P42106.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3995-MON; -.
Organism-specific databases
SubtiList BG11109; qdoI. [Micado]
Family and domain databases
InterPro IPR013096; Cupin_2.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
Pfam PF07883; Cupin_2; 2.
Pfam graphical view of domain structure.
BLOCKS P42106.
Genome annotation databases
GeneID 937689; -.
GenomeReviews AL009126_GR; BSU39980.
KEGG bsu:BSU39980; -.
NMPDR fig|224308.1.peg.4004; -.
Phylogenomic databases
HOGENOM P42106; -.
Genome annotation databases
CMR P42106; BSU39980.
Other
ProtoNet P42106.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   337  337     Quercetin 2,3-dioxygenase. PRO_0000097135
REGION   1   148  148     Cupin 1. 
REGION   177   333  157     Cupin 2. 
METAL   62    62        Iron 1. 
METAL   64    64        Iron 1. 
METAL   69    69        Iron 1. 
METAL   103   103        Iron 1. 
METAL   234   234        Iron 2. 
METAL   236   236        Iron 2. 
METAL   241   241        Iron 2. 
METAL   275   275        Iron 2. 
STRAND   11    13  3      
STRAND   16    18  3      
STRAND   23    28  6      
STRAND   31    37  7      
HELIX   39    42  4      
STRAND   44    53  10      
STRAND   58    63  6      
STRAND   69    76  8      
STRAND   78    82  5      
STRAND   85    89  5      
STRAND   94    97  4      
STRAND   103   107  5      
STRAND   112   119  8      
HELIX   125   130  6      
STRAND   131   133  3      
HELIX   153   155  3      
STRAND   183   185  3      
STRAND   188   190  3      
STRAND   195   200  6      
STRAND   203   209  7      
HELIX   211   213  3      
TURN   214   216  3      
STRAND   219   225  7      
STRAND   240   248  9      
STRAND   250   254  5      
STRAND   257   261  5      
STRAND   266   269  4      
STRAND   275   279  5      
STRAND   281   293  13      
TURN   294   296  3      
HELIX   297   302  6      
STRAND   303   305  3      
STRAND   308   310  3      
HELIX   320   325  6      
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 37585 Da [This is the MW of the unprocessed precursor] CRC64: F9F3255C9D8C215A [This is a checksum on the sequence]
        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 

P42106 in FASTA format

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