ID   BPHB_BURCE     STANDARD;      PRT;   277 AA.
AC   P47227; Q52435;
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   Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56)
DE   (Biphenyl-2,3-dihydro-2,3-diol dehydrogenase) (2,3-dihydro-2,3-
DE   dihydroxybiphenyl dehydrogenase) (Biphenyl-cis-diol dehydrogenase)
DE   (2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase).
GN   Name=bphB;
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   NUCLEOTIDE SEQUENCE OF 1-22.
RC   STRAIN=LB400;
RX   MEDLINE=92234948; PubMed=1569021;
RA   Erickson B.D., Mondello F.J.;
RT   "Nucleotide sequencing and transcriptional mapping of genes encoding
RT   biphenyl dioxygenase, a multicomponent PCB-degrading enzyme in
RT   pseudomonas strain LB400.";
RL   J. Bacteriol. 174:2903-2912(1992).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=98318037; PubMed=9655331;
RA   Huelsmeyer M., Hecht H.-J., Niefind K., Hofer B., Eltis L.D.,
RA   Timmis K.N., Schomburg D.;
RT   "Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase
RT   from a PCB degrader at 2.0-A resolution.";
RL   Protein Sci. 7:1286-1293(1998).
CC   -!- CATALYTIC ACTIVITY: Cis-3-phenylcyclohexa-3,5-diene-1,2-diol +
CC       NAD(+) = biphenyl-2,3-diol + NADH.
CC   -!- PATHWAY: Degradation of biphenyls and polychlorobiphenyls (PCB) to
CC       benzoic acid and chlorobenzoic acids; second step.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) 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
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CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X66122; CAA46909.1; -.
DR   EMBL; M86348; AAB63430.2; -.
DR   PIR; JN0814; JN0814.
DR   PDB; 1BDB; X-ray; @=-.
DR   InterPro; IPR002198; ADH_short.
DR   InterPro; IPR002347; Adh_short_C2.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
KW   3D-structure; Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   NP_BIND       9     33       NAD (By similarity).
FT   ACT_SITE    155    155       Proton acceptor.
FT   BINDING     142    142       Substrate (By similarity).
FT   TURN          2      5
FT   STRAND        7     11
FT   TURN         12     14
FT   HELIX        16     27
FT   TURN         28     29
FT   STRAND       31     36
FT   HELIX        39     49
FT   HELIX        50     52
FT   STRAND       53     57
FT   TURN         60     61
FT   HELIX        63     77
FT   STRAND       82     84
FT   TURN         92     93
FT   HELIX        96     98
FT   TURN        101    103
FT   HELIX       104    115
FT   TURN        116    116
FT   HELIX       117    133
FT   TURN        134    134
FT   STRAND      136    140
FT   HELIX       143    145
FT   TURN        146    146
FT   TURN        148    149
FT   HELIX       153    173
FT   TURN        174    176
FT   STRAND      178    184
FT   HELIX       195    197
FT   HELIX       209    213
FT   TURN        214    216
FT   TURN        218    219
FT   HELIX       225    228
FT   HELIX       230    236
FT   HELIX       238    241
FT   TURN        242    243
FT   STRAND      248    251
FT   HELIX       255    257
FT   TURN        267    268
FT   HELIX       269    273
FT   TURN        274    274
SQ   SEQUENCE   277 AA;  28901 MW;  00194120BD4E12D1 CRC64;
     MKLKGEAVLI TGGASGLGRA LVDRFVAEGA KVAVLDKSAE RLAELETDHG DNVLGIVGDV
     RSLEDQKQAA SRCVARFGKI DTLIPNAGIW DYSTALVDLP EESLDAAFDE VFHINVKGYI
     HAVKACLPAL VASRGNVIFT ISNAGFYPNG GGPLYTAAKH AIVGLVRELA FELAPYVRVN
     GVGSGGINSD LRGPSSLGMG SKAISTVPLA DMLKSVLPIG RMPEVEEYTG AYVFFATRGD
     AAPATGALLN YDGGLGVRGF FSGAGGNDLL EQLNIHP
//