YHHW_ECOLI
ID YHHW_ECOLI Reviewed; 231 AA.
AC P46852; Q2M7A2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Quercetin 2,3-dioxygenase;
DE Short=Quercetinase;
DE EC=1.13.11.24;
DE AltName: Full=Pirin-like protein YhhW;
GN Name=yhhW; OrderedLocusNames=b3439, JW3402;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH CADMIUM IONS,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, DOMAIN, AND
RP METAL-BINDING.
RC STRAIN=K12;
RX PubMed=15951572; DOI=10.1074/jbc.m501034200;
RA Adams M., Jia Z.;
RT "Structural and biochemical analysis reveal pirins to possess quercetinase
RT activity.";
RL J. Biol. Chem. 280:28675-28682(2005).
CC -!- FUNCTION: Has quercetin 2,3-dioxygenase activity in vitro. Its
CC physiological role is unknown; however, may provide a mechanism that
CC would avoid inhibition of key cellular proteins, such as DNA gyrase, by
CC quercetin. {ECO:0000269|PubMed:15951572}.
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; Evidence={ECO:0000269|PubMed:15951572};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15951572};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15951572};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:15951572};
CC Note=Binds 1 divalent metal cation, Zn(2+), Co(2+) or Fe(2+).
CC {ECO:0000269|PubMed:15951572};
CC -!- ACTIVITY REGULATION: Inhibited by kojic acid, sodium
CC diethyldithiocarbamate and 1,10-phenanthroline monohydrochloride.
CC {ECO:0000269|PubMed:15951572}.
CC -!- PATHWAY: Flavonoid metabolism; quercetin degradation.
CC -!- DOMAIN: Is composed of two structurally similar domains arranged face
CC to face. {ECO:0000269|PubMed:15951572}.
CC -!- MISCELLANEOUS: Quercetin is a flavonoid compound synthesized by a
CC variety of plants, including foods for human consumption.
CC -!- SIMILARITY: Belongs to the pirin family. {ECO:0000305}.
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DR EMBL; U18997; AAA58237.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76464.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77854.1; -; Genomic_DNA.
DR PIR; B65140; B65140.
DR RefSeq; NP_417896.1; NC_000913.3.
DR RefSeq; WP_000639811.1; NZ_SSZK01000008.1.
DR PDB; 1TQ5; X-ray; 1.76 A; A=1-231.
DR PDB; 6UTS; X-ray; 3.09 A; A=1-231.
DR PDBsum; 1TQ5; -.
DR PDBsum; 6UTS; -.
DR AlphaFoldDB; P46852; -.
DR SMR; P46852; -.
DR BioGRID; 4261175; 19.
DR DIP; DIP-12356N; -.
DR IntAct; P46852; 9.
DR STRING; 511145.b3439; -.
DR jPOST; P46852; -.
DR PaxDb; P46852; -.
DR PRIDE; P46852; -.
DR DNASU; 947945; -.
DR EnsemblBacteria; AAC76464; AAC76464; b3439.
DR EnsemblBacteria; BAE77854; BAE77854; BAE77854.
DR GeneID; 66672678; -.
DR GeneID; 947945; -.
DR KEGG; ecj:JW3402; -.
DR KEGG; eco:b3439; -.
DR PATRIC; fig|1411691.4.peg.3290; -.
DR EchoBASE; EB2777; -.
DR eggNOG; COG1741; Bacteria.
DR HOGENOM; CLU_064194_2_2_6; -.
DR InParanoid; P46852; -.
DR OMA; ERGYADH; -.
DR PhylomeDB; P46852; -.
DR BioCyc; EcoCyc:G7756-MON; -.
DR BioCyc; MetaCyc:G7756-MON; -.
DR UniPathway; UPA00724; -.
DR EvolutionaryTrace; P46852; -.
DR PRO; PR:P46852; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008127; F:quercetin 2,3-dioxygenase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Copper; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="Quercetin 2,3-dioxygenase"
FT /id="PRO_0000214063"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 59
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 103
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1TQ5"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 63..80
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6UTS"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1TQ5"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1TQ5"
FT STRAND 213..228
FT /evidence="ECO:0007829|PDB:1TQ5"
SQ SEQUENCE 231 AA; 26279 MW; 62E5B21331686935 CRC64;
MIYLRKANER GHANHGWLDS WHTFSFANYY DPNFMGFSAL RVINDDVIEA GQGFGTHPHK
DMEILTYVLE GTVEHQDSMG NKEQVPAGEF QIMSAGTGIR HSEYNPSSTE RLHLYQIWIM
PEENGITPRY EQRRFDAVQG KQLVLSPDAR DGSLKVHQDM ELYRWALLKD EQSVHQIAAE
RRVWIQVVKG NVTINGVKAS TSDGLAIWDE QAISIHADSD SEVLLFDLPP V
