ID   YHHW_ECO57              Reviewed;         231 AA.
AC   P58116;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Quercetin 2,3-dioxygenase;
DE            Short=Quercetinase;
DE            EC=1.13.11.24;
DE   AltName: Full=Pirin-like protein YhhW;
GN   Name=yhhW; OrderedLocusNames=Z4807, ECs4288;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Has quercetin 2,3-dioxygenase activity in vitro. Its
CC       physiological role is unknown; however, may provide a mechanism that
CC       would avoid inhibition of key cellular proteins, such as DNA gyrase, by
CC       quercetin (By similarity). {ECO:0000250}.
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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal cation, Zn(2+), Co(2+) or Fe(2+).
CC       {ECO:0000250};
CC   -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC   -!- DOMAIN: Is composed of two structurally similar domains arranged face
CC       to face. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Quercetin is a flavonoid compound synthesized by a
CC       variety of plants, including foods for human consumption.
CC   -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58548.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37711.1; -; Genomic_DNA.
DR   PIR; H86010; H86010.
DR   PIR; H91164; H91164.
DR   RefSeq; NP_312315.1; NC_002695.1.
DR   RefSeq; WP_000639806.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P58116; -.
DR   SMR; P58116; -.
DR   STRING; 155864.EDL933_4650; -.
DR   EnsemblBacteria; AAG58548; AAG58548; Z4807.
DR   EnsemblBacteria; BAB37711; BAB37711; ECs_4288.
DR   GeneID; 915854; -.
DR   KEGG; ece:Z4807; -.
DR   KEGG; ecs:ECs_4288; -.
DR   PATRIC; fig|386585.9.peg.4480; -.
DR   eggNOG; COG1741; Bacteria.
DR   HOGENOM; CLU_064194_2_2_6; -.
DR   OMA; ERGYADH; -.
DR   UniPathway; UPA00724; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; IPR012093; Pirin.
DR   InterPro; IPR003829; Pirin_N_dom.
DR   InterPro; IPR041602; Quercetinase_C.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR43212; PTHR43212; 1.
DR   Pfam; PF02678; Pirin; 1.
DR   Pfam; PF17954; Pirin_C_2; 1.
DR   PIRSF; PIRSF006232; Pirin; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Copper; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..231
FT                   /note="Quercetin 2,3-dioxygenase"
FT                   /id="PRO_0000214064"
FT   BINDING         57
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   231 AA;  26291 MW;  DC15B213316875E4 CRC64;
     MIYLRKANER GHANHGWLDS WHTFSFANYY DPNFMGFSAL RVINDDVIEA GQGFGTHPHK
     DMEILTYVLE GTVEHQDSMG NKEQVPAGEF QIMSAGTGIR HSEYNPSSTE RLHLYQIWIM
     PEENGITPRY EQRRFDAVQG KQLVLSPDAR DGSLKVHQDM ELYRWALLKD EQSVHQIAAE
     RRVWIQVVKG NVTINGVKAS ISDGLAIWDE QAISIHADSD SEVLLFDLPP V