QDOI_BACSU
ID QDOI_BACSU Reviewed; 337 AA.
AC P42106;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Quercetin 2,3-dioxygenase;
DE Short=Quercetinase;
DE EC=1.13.11.24;
DE AltName: Full=Flavonol 2,4-dioxygenase;
GN Name=qdoI; Synonyms=yxaG; OrderedLocusNames=BSU39980; ORFNames=S14G;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT between the gnt and iol operons.";
RL DNA Res. 2:61-69(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 160 AND 314.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=14741339; DOI=10.1016/s0014-5793(03)01439-x;
RA Bowater L., Fairhurst S.A., Just V.J., Bornemann S.;
RT "Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-
RT dioxygenase.";
RL FEBS Lett. 557:45-48(2004).
RN [5]
RP CHARACTERIZATION, AND COFACTOR.
RX PubMed=15039076; DOI=10.1016/j.pep.2004.01.005;
RA Barney B.M., Schaab M.R., LoBrutto R., Francisco W.A.;
RT "Evidence for a new metal in a known active site: purification and
RT characterization of an iron-containing quercetin 2,3-dioxygenase from
RT Bacillus subtilis.";
RL Protein Expr. Purif. 35:131-141(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=15628860; DOI=10.1021/bi0484421;
RA Gopal B., Madan L.L., Betz S.F., Kossiakoff A.A.;
RT "The crystal structure of a quercetin 2,3-dioxygenase from Bacillus
RT subtilis suggests modulation of enzyme activity by a change in the metal
RT ion at the active site(s).";
RL Biochemistry 44:193-201(2005).
CC -!- FUNCTION: Performs the first step in the degradation of the flavonoid
CC quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage
CC of the O-heteroaromatic ring of the flavonol quercetin yielding the
CC depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon
CC monoxide. This involves the remarkable dioxygenolytic cleavage of two
CC carbon-carbon bonds. {ECO:0000269|PubMed:14741339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-
CC dihydroxybenzoate + CO; Xref=Rhea:RHEA:15381, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:57628, ChEBI:CHEBI:57694;
CC EC=1.13.11.24;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:15039076};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000269|PubMed:15039076};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for quercetin {ECO:0000269|PubMed:14741339};
CC Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:14741339};
CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC -!- SUBUNIT: Homodimer.
CC -!- MASS SPECTROMETRY: Mass=38658; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14741339};
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DR EMBL; AB005554; BAA21586.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16035.2; -; Genomic_DNA.
DR PIR; F70071; F70071.
DR RefSeq; NP_391878.2; NC_000964.3.
DR RefSeq; WP_003243000.1; NZ_JNCM01000034.1.
DR PDB; 1Y3T; X-ray; 2.40 A; A/B=1-337.
DR PDB; 2H0V; X-ray; 2.60 A; A/B=1-337.
DR PDBsum; 1Y3T; -.
DR PDBsum; 2H0V; -.
DR AlphaFoldDB; P42106; -.
DR SMR; P42106; -.
DR STRING; 224308.BSU39980; -.
DR PaxDb; P42106; -.
DR PRIDE; P42106; -.
DR DNASU; 937689; -.
DR EnsemblBacteria; CAB16035; CAB16035; BSU_39980.
DR GeneID; 937689; -.
DR KEGG; bsu:BSU39980; -.
DR PATRIC; fig|224308.179.peg.4324; -.
DR eggNOG; COG1917; Bacteria.
DR InParanoid; P42106; -.
DR OMA; DFLHVPA; -.
DR BioCyc; BSUB:BSU39980-MON; -.
DR BRENDA; 1.13.11.24; 658.
DR SABIO-RK; P42106; -.
DR UniPathway; UPA00724; -.
DR EvolutionaryTrace; P42106; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008127; F:quercetin 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..337
FT /note="Quercetin 2,3-dioxygenase"
FT /id="PRO_0000097135"
FT REGION 1..148
FT /note="Cupin 1"
FT REGION 177..333
FT /note="Cupin 2"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 103
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT CONFLICT 160
FT /note="D -> T (in Ref. 1; BAA21586)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="E -> K (in Ref. 1; BAA21586)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1Y3T"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 281..293
FT /evidence="ECO:0007829|PDB:1Y3T"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1Y3T"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:1Y3T"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2H0V"
SQ SEQUENCE 337 AA; 37600 MW; A91148E6272AE64C CRC64;
MKTLCTHSLP KEKMPYLLRS GEGERYLFGR QVATVMANGR STGDLFEIVL LSGGKGDAFP
LHVHKDTHEG ILVLDGKLEL TLDGERYLLI SGDYANIPAG TPHSYRMQSH RTRLVSYTMK
GNVAHLYSVI GNPYDHAEHP PYASEEVSNE RFAEAAAVAD IVFLDEAKPA CSAKLAELTE
LPDGAVPYVL ESGEGDRLLT GDQLHRIVAA QKNTDGQFIV VSSEGPKGDR IVDHYHEYHT
ETFYCLEGQM TMWTDGQEIQ LNPGDFLHVP ANTVHSYRLD SHYTKMVGVL VPGLFEPFFR
TLGDPYEGHI FPCEPQALRF DRILQNIEAL DLKVMKP
