ID QDOI_ASPJA Reviewed; 350 AA. AC Q7SIC2; Q7SIE5; Q7SIE7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 13-SEP-2023, entry version 74. DE RecName: Full=Quercetin 2,3-dioxygenase; DE EC=1.13.11.24; DE AltName: Full=2,3QD; DE AltName: Full=Flavonol 2,4-dioxygenase; DE AltName: Full=Quercetinase; OS Aspergillus japonicus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=34381; RN [1] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH RP DIETHYLDITHIOCARBAMATE AND KOJIC ACID. RX PubMed=12069585; DOI=10.1021/bi0159736; RA Steiner R.A., Kooter I.M., Dijkstra B.W.; RT "Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. RT Ligand-induced coordination changes probed by X-ray crystallography: RT inhibition, ordering effect, and mechanistic insights."; RL Biochemistry 41:7955-7962(2002). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KAEMPFEROL AND RP QUERCETIN. RX PubMed=12486225; DOI=10.1073/pnas.262506299; RA Steiner R.A., Kalk K.H., Dijkstra B.W.; RT "Anaerobic enzyme.substrate structures provide insight into the reaction RT mechanism of the copper-dependent quercetin 2,3-dioxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16625-16630(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND MUTAGENESIS OF GLU-73. RX PubMed=11839311; DOI=10.1016/s0969-2126(02)00704-9; RA Fusetti F., Schroeter K.H., Steiner R.A., van Noort P.I., Pijning T., RA Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W.; RT "Crystal structure of the copper-containing quercetin 2,3-dioxygenase from RT Aspergillus japonicus."; RL Structure 10:259-268(2002). CC -!- FUNCTION: Performs the first step in the degradation of the flavonoid CC quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage CC of the O-heteroaromatic ring of the flavonol quercetin yielding the CC depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon CC monoxide. This involves the remarkable dioxygenolytic cleavage of two CC carbon-carbon bonds. 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=Cu cation; Xref=ChEBI:CHEBI:23378; CC Note=Binds 1 copper ion per subunit.; CC -!- ACTIVITY REGULATION: Inhibited by diethyldithiocarbamate and kojic CC acid. CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12069585, CC ECO:0000269|PubMed:12486225}. CC -!- PTM: The N-linked glycan at Asn-191 consists of Man(5)-GlcNAc(2). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1GQG; X-ray; 1.70 A; A/B/C/D=1-350. DR PDB; 1GQH; X-ray; 2.15 A; A/B/C/D=1-350. DR PDB; 1H1I; X-ray; 1.75 A; A/B/C/D=1-350. DR PDB; 1H1M; X-ray; 1.90 A; A/B/C/D=1-350. DR PDB; 1JUH; X-ray; 1.60 A; A/B/C/D=1-350. DR PDBsum; 1GQG; -. DR PDBsum; 1GQH; -. DR PDBsum; 1H1I; -. DR PDBsum; 1H1M; -. DR PDBsum; 1JUH; -. DR AlphaFoldDB; Q7SIC2; -. DR SMR; Q7SIC2; -. DR BioCyc; MetaCyc:MONOMER-16751; -. DR BRENDA; 1.13.11.24; 513. DR UniPathway; UPA00724; -. DR EvolutionaryTrace; Q7SIC2; -. 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 CDD; cd20281; cupin_QDO_C; 1. DR CDD; cd02215; cupin_QDO_N_C; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR43346:SF2; -; 1. DR PANTHER; PTHR43346; LIGAND BINDING DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14370)-RELATED; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW 3D-structure; Copper; Dioxygenase; Glycoprotein; Metal-binding; KW Oxidoreductase; Repeat. FT CHAIN 1..350 FT /note="Quercetin 2,3-dioxygenase" FT /id="PRO_0000097134" FT REGION 1..145 FT /note="Cupin 1" FT REGION 146..205 FT /note="Linker" FT REGION 148..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 206..350 FT /note="Cupin 2" FT BINDING 66 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT BINDING 66 FT /ligand="substrate" FT BINDING 68 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT BINDING 73 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT BINDING 73 FT /ligand="substrate" FT BINDING 112 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 142 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 191 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 248 FT /note="N-linked (GlcNAc...) asparagine" FT MUTAGEN 73 FT /note="E->Q: 1000-fold decrease in activity." FT /evidence="ECO:0000269|PubMed:11839311" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:1GQG" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1JUH" FT HELIX 41..44 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 72..87 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 121..130 FT /evidence="ECO:0007829|PDB:1JUH" FT HELIX 134..139 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:1H1I" FT HELIX 166..169 FT /evidence="ECO:0007829|PDB:1H1I" FT HELIX 170..175 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 193..198 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 200..203 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1JUH" FT TURN 219..221 FT /evidence="ECO:0007829|PDB:1GQH" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 233..239 FT /evidence="ECO:0007829|PDB:1JUH" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:1JUH" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 249..256 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 274..281 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 309..329 FT /evidence="ECO:0007829|PDB:1JUH" FT HELIX 330..337 FT /evidence="ECO:0007829|PDB:1JUH" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:1JUH" SQ SEQUENCE 350 AA; 37935 MW; 7F33C372D0DFA5D9 CRC64; DTSSLIVEDA PDHVRPYVIR HYSHARAVTV DTQLYRFYVT GPSSGYAFTL MGTNAPHSDA LGVLPHIHQK HYENFYCNKG SFQLWAQSGN ETQQTRVLSS GDYGSVPRNV THTFQIQDPD TEMTGVIVPG GFEDLFYYLG TNATDTTHTP YIPSSSDSSS TTGPDSSTIS TLQSFDVYAE LSFTPRTDTV NGTAPANTVW HTGANALAST AGDPYFIANG WGPKYLNSQY GYQIVAPFVT ATQAQDTNYT LSTISMSTTP STVTVPTWSF PGACAFQVQE GRVVVQIGDY AATELGSGDV AFIPGGVEFK YYSEAYFSKV LFVSSGSDGL DQNLVNGGEE WSSVSFPADW //