Y1773_SYNY3
ID Y1773_SYNY3 Reviewed; 232 AA.
AC P73623;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative quercetin 2,3-dioxygenase sll1773;
DE Short=Putative quercetinase;
DE EC=1.13.11.24;
DE AltName: Full=Pirin-like protein sll1773;
GN OrderedLocusNames=sll1773;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA17668.1; -; Genomic_DNA.
DR PIR; S77110; S77110.
DR AlphaFoldDB; P73623; -.
DR SMR; P73623; -.
DR IntAct; P73623; 2.
DR STRING; 1148.1652749; -.
DR PaxDb; P73623; -.
DR EnsemblBacteria; BAA17668; BAA17668; BAA17668.
DR KEGG; syn:sll1773; -.
DR eggNOG; COG1741; Bacteria.
DR InParanoid; P73623; -.
DR OMA; ERGYADH; -.
DR PhylomeDB; P73623; -.
DR UniPathway; UPA00724; -.
DR Proteomes; UP000001425; 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..232
FT /note="Putative quercetin 2,3-dioxygenase sll1773"
FT /id="PRO_0000214072"
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 232 AA; 25701 MW; 09B9DCC65352A470 CRC64;
MITLRPSEAR GHGKLDWLDS YFSFSFSHYY DPAHMNFSNL RVINEDYIAP GQGFATHGHK
DMEIVTYVLE GELEHKDSIG NGSIIRPGDV QRMSAGTGIL HSEFNPSPDQ PVHLLQIWIT
PNQFGVEPSY EQKFFSPEDK QGQLRLVASP DGRNGSVTIH QDACIYASVL GQGETVSYSL
SNRRAWLQII RGNLTLNGKT LKTGDGAGIN EEQAITCTGQ GEATEFLLFD LP
