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Database: UniProt
Entry: A0A0P6XA70_9SPHN
LinkDB: A0A0P6XA70_9SPHN
Original site: A0A0P6XA70_9SPHN 
ID   A0A0P6XA70_9SPHN        Unreviewed;       287 AA.
AC   A0A0P6XA70;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Quercetin 2,3-dioxygenase {ECO:0000313|EMBL:KPL68180.1};
GN   ORFNames=SZ64_08635 {ECO:0000313|EMBL:KPL68180.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68180.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68180.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68180.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the pirin family.
CC       {ECO:0000256|ARBA:ARBA00008416, ECO:0000256|RuleBase:RU003457}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPL68180.1}.
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DR   EMBL; JXQC01000003; KPL68180.1; -; Genomic_DNA.
DR   RefSeq; WP_054530439.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XA70; -.
DR   PATRIC; fig|1603897.4.peg.1638; -.
DR   OrthoDB; 9780903at2; -.
DR   Proteomes; UP000049978; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   CDD; cd02247; cupin_pirin_C; 1.
DR   CDD; cd02909; cupin_pirin_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 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; PTHR43594; QUERCETIN 2,3-DIOXYGENASE; 1.
DR   PANTHER; PTHR43594:SF1; QUERCETIN 2,3-DIOXYGENASE PA2418-RELATED; 1.
DR   Pfam; PF02678; Pirin; 1.
DR   Pfam; PF05726; Pirin_C; 1.
DR   PIRSF; PIRSF006232; Pirin; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000313|EMBL:KPL68180.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KPL68180.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978}.
FT   DOMAIN          21..128
FT                   /note="Pirin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02678"
FT   DOMAIN          182..282
FT                   /note="Pirin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05726"
SQ   SEQUENCE   287 AA;  30778 MW;  EF763969F62BB3BC CRC64;
     MKTLETILRN DRAHWVGDGF PVRSLFSYHG ETAPISPFLL FDYAGPWNFE PTGGHPRGVG
     EHPHKGFETV TIVYDGEVSH RDSSGGGGTI GTGEVQWMTA GAGVLHEEFH SPGYSKTGGP
     FRMVQLWVNL PAKDKLTPAK YQAITRDMIP EVSFEGGRAR IIAGEFGDTK GPASTFTPVN
     LWDVRLSAGA EATLPLPDGH TTMVAVLSGH VTIDGKGLRE AEIARLSRDG AEVAIKADGD
     AMLLVMTGEP IDEPVFGYGP FVMNTEAEIR EAIAEFNSGR FGALAPA
//
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