QDOI_ASPJA
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 03-AUG-2022, entry version 71.
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).
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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:MON-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 Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR SUPFAM; SSF51182; SSF51182; 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
