ID BPHC_BURCE STANDARD; PRT; 297 AA. AC P47228; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 02-MAY-2006, entry version 48. 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 Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LB400; RX MEDLINE=93345822; PubMed=8344527; DOI=10.1016/0378-1119(93)90345-4; RA Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.; RT "Genetic analysis of a Pseudomonas locus encoding a pathway for RT biphenyl/polychlorinated biphenyl degradation."; RL Gene 130:47-55(1993). RN [2] RP PROTEIN SEQUENCE OF 1-31, SUBSTRATE CHARACTERIZATION, PRELIMINARY RP CRYSTALLIZATION, AND SUBUNITS. RC STRAIN=LB400; RX PubMed=8428946; RA Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.; RT "Purification and crystallization of 2,3-dihydroxybiphenyl RT 1,2-dioxygenase."; RL J. Biol. Chem. 268:2727-2732(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RC STRAIN=LB400; RX MEDLINE=96069815; PubMed=7481800; RA Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T.; RT "Crystal structure of the biphenyl-cleaving extradiol dioxygenase from RT a PCB-degrading pseudomonad."; RL Science 270:976-980(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RC STRAIN=LB400; RX MEDLINE=99074262; PubMed=9857017; DOI=10.1074/jbc.273.52.34887; RA Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.; RT "Molecular basis for the stabilization and inhibition of RT 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol."; RL J. Biol. Chem. 273:34887-34895(1998). CC -!- FUNCTION: Shows a preference for catechols with groups immediately CC adjacent to the hydroxyl substituents. CC -!- CATALYTIC ACTIVITY: Biphenyl-2,3-diol + O(2) = CC 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(2)O. CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7 uM for biphenyl-2,3-diol; CC Note=Substrate inhibition occurs at 300 uM (+/- 20 uM); CC pH dependence: CC Optimum pH is 8.0; CC -!- PATHWAY: Degradation of biphenyls and polychlorobiphenyls (PCB) to CC benzoic acid and chlorobenzoic acids. CC -!- SUBUNIT: Homooctamer. The enzyme is composed of two planar CC tetramers rotated at 45 degrees relative to each other, with a CC channel in the middle. CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X66122; CAA46910.1; -; Genomic_DNA. DR PIR; JN0815; JN0815. DR PDB; 1HAN; X-ray; @=1-297. DR PDB; 1KMY; X-ray; A=1-297. DR PDB; 1KND; X-ray; A=1-297. DR PDB; 1KNF; X-ray; A=1-297. DR PDB; 1LGT; X-ray; A=1-297. DR PDB; 1LKD; X-ray; A=1-297. DR LinkHub; P47228; -. 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; 2. DR ProDom; PD000977; Xdiol_dioxygnse; 1. DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1. KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase. FT INIT_MET 0 0 FT CHAIN 1 297 Biphenyl-2,3-diol 1,2-dioxygenase. FT /FTId=PRO_0000085033. FT METAL 145 145 Iron. FT METAL 209 209 Iron. FT METAL 259 259 Iron. FT STRAND 2 13 FT HELIX 15 24 FT TURN 25 26 FT STRAND 29 34 FT TURN 35 36 FT STRAND 37 46 FT STRAND 48 53 FT TURN 55 56 FT STRAND 58 68 FT HELIX 69 81 FT TURN 82 83 FT STRAND 87 88 FT HELIX 91 97 FT TURN 98 98 FT STRAND 100 106 FT TURN 108 109 FT STRAND 110 110 FT STRAND 112 117 FT STRAND 120 121 FT TURN 123 124 FT STRAND 125 125 FT STRAND 130 132 FT STRAND 134 134 FT STRAND 136 136 FT HELIX 139 141 FT STRAND 143 143 FT STRAND 145 149 FT STRAND 151 151 FT HELIX 153 162 FT TURN 163 164 FT STRAND 167 177 FT TURN 178 179 FT STRAND 180 193 FT STRAND 195 199 FT STRAND 204 215 FT HELIX 217 228 FT TURN 229 231 FT STRAND 233 243 FT STRAND 246 251 FT TURN 253 254 FT STRAND 255 255 FT STRAND 257 262 FT STRAND 266 266 FT TURN 269 270 FT STRAND 274 277 FT STRAND 279 283 FT STRAND 286 286 SQ SEQUENCE 297 AA; 32340 MW; A2AA664C7A77AD21 CRC64; SIRSLGYMGF AVSDVAAWRS FLTQKLGLME AGTTDNGDLF RIDSRAWRIA VQQGEVDDLA FAGYEVADAA GLAQMADKLK QAGIAVTTGD ASLARRRGVT GLITFADPFG LPLEIYYGAS EVFEKPFLPG AAVSGFLTGE QGLGHFVRCV PDSDKALAFY TDVLGFQLSD VIDMKMGPDV TVPAYFLHCN ERHHTLAIAA FPLPKRIHHF MLEVASLDDV GFAFDRVDAD GLITSTLGRH TNDHMVSFYA STPSGVEVEY GWSARTVDRS WVVVRHDSPS MWGHKSVRDK AAARNKA //