ID   Y1685_PASMU             Reviewed;         233 AA.
AC   Q9CKD7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative quercetin 2,3-dioxygenase PM1685;
DE            Short=Putative quercetinase;
DE            EC=1.13.11.24;
DE   AltName: Full=Pirin-like protein PM1685;
GN   OrderedLocusNames=PM1685;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Putative quercetin 2,3-dioxygenase. {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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal cation. {ECO:0000250};
CC   -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC   -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR   EMBL; AE004439; AAK03769.1; -; Genomic_DNA.
DR   RefSeq; WP_010907288.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKD7; -.
DR   SMR; Q9CKD7; -.
DR   STRING; 747.DR93_677; -.
DR   EnsemblBacteria; AAK03769; AAK03769; PM1685.
DR   KEGG; pmu:PM1685; -.
DR   PATRIC; fig|272843.6.peg.1705; -.
DR   HOGENOM; CLU_064194_2_2_6; -.
DR   OMA; ERGYADH; -.
DR   UniPathway; UPA00724; -.
DR   Proteomes; UP000000809; 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   Dioxygenase; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Putative quercetin 2,3-dioxygenase PM1685"
FT                   /id="PRO_0000214067"
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
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"
FT   BINDING         105
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  26804 MW;  28500A6C859F65D5 CRC64;
     MLRVRYAHER GKSHPAIHWL RGYHSFSFAD YYSPQHIHFS HLRVINEDII APQHGFDMHP
     HQDMEILTYI LSGTIEHQDS MGNHTQLHAG EFQIMSAGSG VHHAEINPSS EHDVHLYQIW
     ILPKSKGIAP RYEQGCFADT EGATLILSPE AKDGAFYIHQ DMSLWRWQLS LEQSAVKTIP
     LLPTRRYWLQ LVKGQLRVND VLLNTSDGLA ITHENVLQIE LIQNSEFLLF DLV