ID BPHC_PSEPA STANDARD; PRT; 299 AA. AC P11122; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 17-OCT-2006, entry version 44. DE Biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) (23OHBP oxygenase) DE (2,3-dihydroxybiphenyl dioxygenase) (DHBD). GN Name=bphC; OS Pseudomonas paucimobilis (Sphingomonas paucimobilis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=13689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Q1; RX MEDLINE=88326911; PubMed=3137968; DOI=10.1021/bi00411a015; RA Taira K., Hayase N., Arimura N., Yamashita S., Miyazaki T., RA Furukawa K.; RT "Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl RT dioxygenase gene from the PCB-degrading strain of Pseudomonas RT paucimobilis Q1."; RL Biochemistry 27:3990-3996(1988). CC -!- CATALYTIC ACTIVITY: Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6- CC phenylhexa-2,4-dienoate + H(2)O. CC -!- COFACTOR: Fe(2+) ion. CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-oxopent- CC 4-enoate and benzoate from biphenyl: step 3. CC -!- SUBUNIT: Homooctamer. CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase CC family. 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 HSSP; P17297; 1DHY. DR InterPro; IPR011588; Gly_Xdiol_dOase. DR InterPro; IPR004360; Glyas_bleo_dOase. DR InterPro; IPR000486; Xdiol_dOase_1_2. DR Pfam; PF00903; Glyoxalase; 2. DR ProDom; PD002334; Gly_diox; 3. DR ProDom; PD000977; Xdiol_dioxygnse; 1. DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1. KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase. FT CHAIN 1 299 Biphenyl-2,3-diol 1,2-dioxygenase. FT /FTId=PRO_0000085036. FT METAL 149 149 Iron (By similarity). FT METAL 212 212 Iron (By similarity). FT METAL 263 263 Iron (By similarity). 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 //