ID   Y3769_VIBCH             Reviewed;         282 AA.
AC   Q9KKY1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative quercetin 2,3-dioxygenase VC_A0969;
DE            Short=Putative quercetinase;
DE            EC=1.13.11.24;
DE   AltName: Full=Pirin-like protein VC_A0969;
GN   OrderedLocusNames=VC_A0969;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96865.1; -; Genomic_DNA.
DR   PIR; H82394; H82394.
DR   RefSeq; NP_233353.1; NC_002506.1.
DR   RefSeq; WP_000159137.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KKY1; -.
DR   SMR; Q9KKY1; -.
DR   STRING; 243277.VC_A0969; -.
DR   DNASU; 2612679; -.
DR   EnsemblBacteria; AAF96865; AAF96865; VC_A0969.
DR   GeneID; 57742330; -.
DR   KEGG; vch:VC_A0969; -.
DR   PATRIC; fig|243277.26.peg.3577; -.
DR   eggNOG; COG1741; Bacteria.
DR   HOGENOM; CLU_045717_5_0_6; -.
DR   OMA; PHPHRGM; -.
DR   BioCyc; VCHO:VCA0969-MON; -.
DR   UniPathway; UPA00724; -.
DR   Proteomes; UP000000584; Chromosome 2.
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; IPR008778; Pirin_C_dom.
DR   InterPro; IPR003829; Pirin_N_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR13903; PTHR13903; 1.
DR   Pfam; PF02678; Pirin; 1.
DR   Pfam; PF05726; Pirin_C; 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..282
FT                   /note="Putative quercetin 2,3-dioxygenase VC_A0969"
FT                   /id="PRO_0000214073"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   282 AA;  31324 MW;  5010C3933BE13197 CRC64;
     MTKDREIRQT VPAQPTSDGD GVKIQRIAGF QRPNFSPFLM LDELKADSQA DYIGGFPPHP
     HRGIETLTYM LQGHFQHRDQ MGNVGELRSG GAQWMAAGHG VIHSEMPIMQ EGQLHGFQIW
     INQPARNKMS PAKYQDFQPE SIVERHHPQQ GLLRVIAGSV EVEDQTITGP LTDTGVPATV
     VDWRAEAGQD ISINTPPHFN AMLYVYRGSL NVGKQSVKTG HMAMLTAGEQ LTLRAEQPCG
     SLLLMGQPID EPVVHYGPFV MNSMAEIEQA IRDYNAGHFE TY