ID   Y181_MYCTO              Reviewed;         244 AA.
AC   P9WI84; L0T5S0; O07425; P65724;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Putative quercetin 2,3-dioxygenase MT0190;
DE            Short=Putative quercetinase;
DE            EC=1.13.11.24;
DE   AltName: Full=Pirin-like protein MT0190;
GN   OrderedLocusNames=MT0190;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44410.1; -; Genomic_DNA.
DR   PIR; H70905; H70905.
DR   RefSeq; WP_003401107.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI84; -.
DR   SMR; P9WI84; -.
DR   EnsemblBacteria; AAK44410; AAK44410; MT0190.
DR   KEGG; mtc:MT0190; -.
DR   PATRIC; fig|83331.31.peg.207; -.
DR   HOGENOM; CLU_064194_2_0_11; -.
DR   UniPathway; UPA00724; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..244
FT                   /note="Putative quercetin 2,3-dioxygenase MT0190"
FT                   /id="PRO_0000428051"
FT   BINDING         60
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   244 AA;  26286 MW;  BE4EEE9C26F9FE61 CRC64;
     MTATVEIRRA ADRAVTTTSW LKSRHSFSFG DHYDPDNTHH GLLLVNNDDQ MEPASGFDPH
     PHRDMEIVTW VLRGALRHQD SAGNSGVIYP GLAQRMSAGT GILHSEMNDS ATEPVHFVQM
     WVIPDATGIT ASYQQQEIDD ELLRAGLVTI ASGIPGQDAA LTLHNSSASL HGARLRPGAT
     VSLPCAPFLH LFVAYGRLTL EGGGELADGD AVRFTDADAR GLTANEPSEV LIWEMHAKLG
     DSAT