ID BPHC_SPHPI Reviewed; 299 AA. AC P11122; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 14-DEC-2022, entry version 93. DE RecName: Full=Biphenyl-2,3-diol 1,2-dioxygenase; DE EC=1.13.11.39; DE AltName: Full=2,3-dihydroxybiphenyl dioxygenase; DE Short=DHBD; DE AltName: Full=23OHBP oxygenase; GN Name=bphC; OS Sphingomonas paucimobilis (Pseudomonas paucimobilis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=13689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=3137968; DOI=10.1021/bi00411a015; RA Taira K., Hayase N., Arimura N., Yamashita S., Miyazaki T., Furukawa K.; RT "Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase RT gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1."; RL Biochemistry 27:3990-3996(1988). CC -!- CATALYTIC ACTIVITY: CC Reaction=biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4- CC dienoate + H(+); Xref=Rhea:RHEA:14413, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16205, ChEBI:CHEBI:58284; CC EC=1.13.11.39; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4- CC pentadienoate and benzoate from biphenyl: step 3/4. CC -!- SUBUNIT: Homooctamer. CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family. CC {ECO:0000305}. 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; M20640; AAA25678.1; -; Genomic_DNA. DR PIR; A28718; A28718. DR AlphaFoldDB; P11122; -. DR SMR; P11122; -. DR STRING; 13689.BV96_03597; -. DR eggNOG; COG0346; Bacteria. DR UniPathway; UPA00155; UER00252. DR GO; GO:0018583; F:biphenyl-2,3-diol 1,2-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:InterPro. DR Gene3D; 3.10.180.10; -; 2. DR InterPro; IPR017626; DiOHbiphenyl_dOase. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR InterPro; IPR037523; VOC. DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2. DR Pfam; PF00903; Glyoxalase; 1. DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1. DR TIGRFAMs; TIGR03213; 23dbph12diox; 1. DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1. DR PROSITE; PS51819; VOC; 2. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Repeat. FT CHAIN 1..299 FT /note="Biphenyl-2,3-diol 1,2-dioxygenase" FT /id="PRO_0000085036" FT DOMAIN 6..121 FT /note="VOC 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163" FT DOMAIN 146..267 FT /note="VOC 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163" FT BINDING 149 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" SQ SEQUENCE 299 AA; 33095 MW; 29746CAB79D6FC7B CRC64; MVAVTELGYL GLTVTNLDAW RSYAAEVAGM EIVDEGEGDR LYLRMDQWHH RIVLHASDSD DLAYLGWRVA DPVEFDAMVA KLTAAGISLT VASEAEARER RVLGLAKLAD PGGNPTEIFY GPQVDTHKPF HPGRPMYGKF VTGSEGIGHC ILRQDDVPAA AAFYGLLGLR GSVEYHLQLP NGMVAQPYFM HCNERQHSVA FGLGPMEKRI NHLMFEYTDL DDLGLAHDIV RARKIDVALQ LGKHANDQAL TFYCANPSGW LWEFGWGARK APSQQEYYTR DIFGHGNEAA GYGMDIPLG //