[1]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DIETHYLDITHIOCARBAMATE AND KOJIC ACID. DOI=10.1021/bi0159736; PubMed=12069585 [NCBI, ExPASy, EBI, Israel, Japan] Steiner R.A., Kooter I.M., Dijkstra B.W.; "Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights."; Biochemistry 41:7955-7962(2002).
[2]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KAEMPFEROL AND QUERCETIN. DOI=10.1073/pnas.262506299; PubMed=12486225 [NCBI, ExPASy, EBI, Israel, Japan] Steiner R.A., Kalk K.H., Dijkstra B.W.; "Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase."; Proc. Natl. Acad. Sci. U.S.A. 99:16625-16630(2002).
[3]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND MUTAGENESIS OF GLU-73. DOI=10.1016/S0969-2126(02)00704-9; PubMed=11839311 [NCBI, ExPASy, EBI, Israel, Japan] Fusetti F., Schroeter K.H., Steiner R.A., van Noort P.I., Pijning T., Rozeboom H.J., Kalk K.H., Egmond M.R., Dijkstra B.W.; "Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus."; Structure 10:259-268(2002).

Comments

FUNCTION: Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
CATALYTIC ACTIVITY: Quercetin + O₂ = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H⁺.
COFACTOR: Binds 1 copper ion per subunit.
ENZYME REGULATION: Inhibited by diethyldithiocarbamate and kojic acid.
PATHWAY: Flavonoid metabolism; quercetin degradation .
SUBUNIT: Homodimer.
PTM: The N-linked glycan at Asn-191 consists of Man(5)-GlcNAc(2).

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

1GQG; X-ray; 1.70 A; A/B/C/D=1-350.	[ExPASy / RCSB / EBI]
1GQH; X-ray; 2.15 A; A/B/C/D=1-350.	[ExPASy / RCSB / EBI]
1H1I; X-ray; 1.75 A; A/B/C/D=1-350.	[ExPASy / RCSB / EBI]
1H1M; X-ray; 1.90 A; A/B/C/D=1-350.	[ExPASy / RCSB / EBI]
1JUH; X-ray; 1.60 A; A/B/C/D=1-350.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GQG; -.
1GQH; -.
1H1I; -.
1H1M; -.
1JUH; -.

ModBase

Q7SIC2.

Ontologies

GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008127;	Molecular function: quercetin 2,3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Copper; Dioxygenase; Glycoprotein; Metal-binding; Oxidoreductase; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 350`	`350`	`Quercetin 2,3-dioxygenase.`	`PRO_0000097134`
`REGION`	`1 145`	`145`	`Cupin 1.`
`REGION`	`146 205`	`60`	`Linker.`
`REGION`	`206 350`	`145`	`Cupin 2.`
`METAL`	`66 66`		`Copper.`
`METAL`	`68 68`		`Copper.`
`METAL`	`73 73`		`Copper.`
`METAL`	`112 112`		`Copper.`
`BINDING`	`66 66`		`Substrate.`
`BINDING`	`73 73`		`Substrate.`
`CARBOHYD`	`90 90`		`N-linked (GlcNAc...).`
`CARBOHYD`	`109 109`		`N-linked (GlcNAc...).`
`CARBOHYD`	`142 142`		`N-linked (GlcNAc...).`
`CARBOHYD`	`191 191`		`N-linked (GlcNAc...).`
`CARBOHYD`	`248 248`		`N-linked (GlcNAc...).`
`MUTAGEN`	`73 73`		`E->Q: 1000-fold decrease in activity.`
`STRAND`	`5 9`	`5`
`STRAND`	`17 19`	`3`
`STRAND`	`28 30`	`3`
`STRAND`	`33 39`	`7`
`HELIX`	`41 44`	`4`
`STRAND`	`49 55`	`7`
`STRAND`	`72 87`	`16`
`STRAND`	`94 99`	`6`
`STRAND`	`103 106`	`4`
`STRAND`	`111 116`	`6`
`STRAND`	`121 129`	`9`
`TURN`	`130 133`	`4`
`HELIX`	`134 139`	`6`
`STRAND`	`140 142`	`3`
`HELIX`	`173 175`	`3`
`STRAND`	`193 197`	`5`
`STRAND`	`200 203`	`4`
`STRAND`	`215 217`	`3`
`STRAND`	`224 227`	`4`
`STRAND`	`233 239`	`7`
`HELIX`	`241 244`	`4`
`HELIX`	`245 247`	`3`
`STRAND`	`249 256`	`8`
`STRAND`	`274 281`	`8`
`STRAND`	`283 287`	`5`
`STRAND`	`293 295`	`3`
`STRAND`	`300 303`	`4`
`STRAND`	`309 329`	`21`
`HELIX`	`330 336`	`7`
`STRAND`	`338 341`	`4`

Sequence information

Length: 350 AA [This is the length of the unprocessed precursor]

Molecular weight: 37935 Da [This is the MW of the unprocessed precursor]

CRC64: 7F33C372D0DFA5D9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DTSSLIVEDA PDHVRPYVIR HYSHARAVTV DTQLYRFYVT GPSSGYAFTL MGTNAPHSDA 

        70         80         90        100        110        120 
LGVLPHIHQK HYENFYCNKG SFQLWAQSGN ETQQTRVLSS GDYGSVPRNV THTFQIQDPD 

       130        140        150        160        170        180 
TEMTGVIVPG GFEDLFYYLG TNATDTTHTP YIPSSSDSSS TTGPDSSTIS TLQSFDVYAE 

       190        200        210        220        230        240 
LSFTPRTDTV NGTAPANTVW HTGANALAST AGDPYFIANG WGPKYLNSQY GYQIVAPFVT 

       250        260        270        280        290        300 
ATQAQDTNYT LSTISMSTTP STVTVPTWSF PGACAFQVQE GRVVVQIGDY AATELGSGDV 

       310        320        330        340        350 
AFIPGGVEFK YYSEAYFSKV LFVSSGSDGL DQNLVNGGEE WSSVSFPADW

Q7SIC2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools