Y133_THEAC
ID Y133_THEAC Reviewed; 261 AA.
AC Q9HLU2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative quercetin 2,3-dioxygenase Ta0133;
DE Short=Putative quercetinase;
DE EC=1.13.11.24;
DE AltName: Full=Pirin-like protein Ta0133;
GN OrderedLocusNames=Ta0133;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445063; CAC11280.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HLU2; -.
DR SMR; Q9HLU2; -.
DR STRING; 273075.Ta0133m; -.
DR EnsemblBacteria; CAC11280; CAC11280; CAC11280.
DR KEGG; tac:Ta0133; -.
DR eggNOG; arCOG02935; Archaea.
DR HOGENOM; CLU_045717_5_0_2; -.
DR OMA; TPWHPHR; -.
DR UniPathway; UPA00724; -.
DR Proteomes; UP000001024; 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; IPR008778; Pirin_C_dom.
DR InterPro; IPR003829; Pirin_N_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR13903; PTHR13903; 1.
DR Pfam; PF02678; Pirin; 1.
DR Pfam; PF05726; Pirin_C; 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..261
FT /note="Putative quercetin 2,3-dioxygenase Ta0133"
FT /id="PRO_0000214075"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 261 AA; 29701 MW; 24BCBB331161C1FF CRC64;
MFGSDNRADY DNGFPWHPHR GIETITYQIK GKTFHEDSEG HRGIIAPGEI QWMTAGSGIF
HEEMPKPIYY GEENKYRERN DSNAGIQLWL NMPASSKMAD PAYRSIRSDQ IPQISDDYGN
RIRIVAGTVN RVSGALNENF QYDLMQRIDP YYVEILMEPD TRTSLSVPEG HRAIMAIVEG
SIRVNGSTFN EKNVAVLSKE GTDIFIDSQA NSRLIFLAGK PLNEPIAWYG PIVMNTRDQL
IQAFNELQEG KFVKNRNPVW Q
