ID A0A6V8SLB8_9CLOT Unreviewed; 237 AA. AC A0A6V8SLB8; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 24-JUL-2024, entry version 10. DE SubName: Full=Quercetin 2,3-dioxygenase {ECO:0000313|EMBL:GFP77690.1}; GN ORFNames=bsdtw1_03850 {ECO:0000313|EMBL:GFP77690.1}; OS Clostridium fungisolvens. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1604897 {ECO:0000313|EMBL:GFP77690.1, ECO:0000313|Proteomes:UP000580568}; RN [1] {ECO:0000313|EMBL:GFP77690.1, ECO:0000313|Proteomes:UP000580568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW1 {ECO:0000313|EMBL:GFP77690.1, RC ECO:0000313|Proteomes:UP000580568}; RA Ueki A., Tonouchi A.; RT "A new beta-1,3-glucan-decomposing anaerobic bacterium isolated from anoxic RT soil subjected to biological soil disinfestation."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|PIRSR:PIRSR006232-1}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|PIRSR:PIRSR006232-1}; 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:GFP77690.1}. 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; BLZR01000001; GFP77690.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6V8SLB8; -. DR Proteomes; UP000580568; Unassembled WGS sequence. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd02910; cupin_Yhhw_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 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; QUERCETIN 2,3-DIOXYGENASE; 1. DR PANTHER; PTHR43212:SF3; QUERCETIN 2,3-DIOXYGENASE; 1. DR Pfam; PF02678; Pirin; 1. DR Pfam; PF17954; Pirin_C_2; 1. DR PIRSF; PIRSF006232; Pirin; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 3: Inferred from homology; KW Dioxygenase {ECO:0000313|EMBL:GFP77690.1}; KW Iron {ECO:0000256|PIRSR:PIRSR006232-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR006232-1}; KW Oxidoreductase {ECO:0000313|EMBL:GFP77690.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000580568}. FT DOMAIN 13..118 FT /note="Pirin N-terminal" FT /evidence="ECO:0000259|Pfam:PF02678" FT DOMAIN 147..229 FT /note="Quercetin 2,3-dioxygenase C-terminal cupin" FT /evidence="ECO:0000259|Pfam:PF17954" FT BINDING 57 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR006232-1" FT BINDING 59 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR006232-1" FT BINDING 101 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR006232-1" FT BINDING 103 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|PIRSR:PIRSR006232-1" SQ SEQUENCE 237 AA; 27402 MW; FB5EBCFE92CAC632 CRC64; MIRKIKSSDM GRSKNQWLDS LFHFSFADYF NVENISFGDL RVINDDLIQP HTGFDMHPHK DMEIISYGIE GELTHEDSMG SKGVIGRGQV QYMSAGTGVY HSEHNRGDVT ARFLQIWVLP DKKNHTPQYG DFKFDWEERK NKWFHFVSSK QGDAPIKVNQ DINFYALELE EGKEIDFAVG NRRQAYMVQI EGTSTVNGTE LNQRDAAEIV EEDVKIKAIE KSHILVIEMT KKNVIWR //