ID   Y1337_ZYMMO             Reviewed;         235 AA.
AC   Q9XBR7; Q5NMU9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative quercetin 2,3-dioxygenase ZMO1337;
DE            Short=Putative quercetinase;
DE            EC=1.13.11.24;
DE   AltName: Full=Pirin-like protein ZMO1337;
GN   OrderedLocusNames=ZMO1337; ORFNames=zm10orf8;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Um H.W., Kang H.S.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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; AF157493; AAD42408.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89961.1; -; Genomic_DNA.
DR   RefSeq; WP_011241135.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9XBR7; -.
DR   SMR; Q9XBR7; -.
DR   EnsemblBacteria; AAV89961; AAV89961; ZMO1337.
DR   GeneID; 58027087; -.
DR   KEGG; zmo:ZMO1337; -.
DR   eggNOG; COG1741; Bacteria.
DR   HOGENOM; CLU_064194_2_2_5; -.
DR   OMA; NLRVWND; -.
DR   OrthoDB; 729805at2; -.
DR   UniPathway; UPA00724; -.
DR   Proteomes; UP000001173; 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..235
FT                   /note="Putative quercetin 2,3-dioxygenase ZMO1337"
FT                   /id="PRO_0000214074"
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   235 AA;  26119 MW;  94B108881DBCEC43 CRC64;
     MIVKRPYKNL GFADHGWLQA RHHFSFARYF DPDRINWGAV RVWNDDRIAP DTGFGMHPHK
     DMEIVTYIRE GALTHEDSLG NKGRIEAGDV QVMSAGTGIV HSEYNREASD TRLFQIWIMP
     NQSGHKPSWG SRSFPKKDHA GRFVVLASGY PEDKEALPIH ADAAVLGATL NKGDVINYPL
     EEQRYGYLVV SKGIIAIENC TLQEGDAAGL AEVETISIEA KEDSEIVMVV TGAKI