Y187_MYCBO
ID Y187_MYCBO Reviewed; 244 AA.
AC P65725; A0A1R3XUK7; O07425; X2BEB5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Putative quercetin 2,3-dioxygenase Mb0187c;
DE Short=Putative quercetinase;
DE EC=1.13.11.24;
DE AltName: Full=Pirin-like protein Mb0187c;
GN OrderedLocusNames=BQ2027_MB0187C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT98648.1; -; Genomic_DNA.
DR RefSeq; NP_853852.1; NC_002945.3.
DR RefSeq; WP_003401107.1; NC_002945.4.
DR AlphaFoldDB; P65725; -.
DR SMR; P65725; -.
DR PATRIC; fig|233413.5.peg.211; -.
DR OMA; NLRVWND; -.
DR UniPathway; UPA00724; -.
DR Proteomes; UP000001419; 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; 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 3: Inferred from homology;
KW Dioxygenase; Metal-binding; Oxidoreductase.
FT CHAIN 1..244
FT /note="Putative quercetin 2,3-dioxygenase Mb0187c"
FT /id="PRO_0000214066"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 26286 MW; BE4EEE9C26F9FE61 CRC64;
MTATVEIRRA ADRAVTTTSW LKSRHSFSFG DHYDPDNTHH GLLLVNNDDQ MEPASGFDPH
PHRDMEIVTW VLRGALRHQD SAGNSGVIYP GLAQRMSAGT GILHSEMNDS ATEPVHFVQM
WVIPDATGIT ASYQQQEIDD ELLRAGLVTI ASGIPGQDAA LTLHNSSASL HGARLRPGAT
VSLPCAPFLH LFVAYGRLTL EGGGELADGD AVRFTDADAR GLTANEPSEV LIWEMHAKLG
DSAT