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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//