ID   BPHC_BURCE     STANDARD;      PRT;   297 AA.
AC   P47228;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
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.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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 SUBUNIT ORGANIZATION.
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 1,2-
RT   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 2,3-
RT   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) = 2-hydroxy-6-oxo-6-
CC       phenylhexa-2,4-dienoate + H(2)O.
CC   -!- COFACTOR: Binds 1 ferrous 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   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X66122; CAA46910.1; -.
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=-.
DR   PDB; 1KNF; X-ray; A=-.
DR   PDB; 1LGT; X-ray; A=1-297.
DR   PDB; 1LKD; X-ray; A=1-297.
DR   InterPro; IPR004360; Gly_bleo_diox.
DR   InterPro; IPR000486; Xdiol_dioxygnse.
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   METAL       145    145       Iron.
FT   METAL       209    209       Iron.
FT   METAL       259    259       Iron.
FT   STRAND        2     12
FT   HELIX        15     24
FT   TURN         25     26
FT   STRAND       29     34
FT   TURN         35     36
FT   STRAND       37     41
FT   STRAND       45     45
FT   STRAND       49     53
FT   STRAND       58     66
FT   HELIX        69     81
FT   TURN         82     83
FT   STRAND       87     88
FT   HELIX        91     97
FT   TURN         98     98
FT   STRAND      101    106
FT   TURN        108    109
FT   STRAND      112    117
FT   STRAND      121    121
FT   TURN        123    124
FT   STRAND      136    136
FT   HELIX       139    141
FT   STRAND      145    149
FT   HELIX       153    162
FT   TURN        163    164
FT   STRAND      167    175
FT   STRAND      181    188
FT   STRAND      192    192
FT   STRAND      196    199
FT   STRAND      207    214
FT   HELIX       217    228
FT   TURN        229    231
FT   STRAND      233    240
FT   STRAND      246    251
FT   TURN        253    254
FT   STRAND      257    262
FT   STRAND      266    266
FT   TURN        269    270
FT   STRAND      274    276
FT   STRAND      280    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
//