ID   BPHF_BURCE     STANDARD;      PRT;   109 AA.
AC   P37332;
DT   01-OCT-1994 (Rel. 30, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Biphenyl dioxygenase system ferredoxin component.
GN   Name=bphF;
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=92234948; PubMed=1569021;
RA   Erickson B.D., Mondello F.J.;
RT   "Nucleotide sequencing and transcriptional mapping of the genes
RT   encoding biphenyl dioxygenase, a multicomponent polychlorinated-
RT   biphenyl-degrading enzyme in Pseudomonas strain LB400.";
RL   J. Bacteriol. 174:2903-2912(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Erickson B.D., Mondello F.J.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=20580187; PubMed=11141059; DOI=10.1021/bi001780r;
RA   Couture M.M.-J., Colbert C.L., Babini E., Rosell F.I., Mauk A.G.,
RA   Bolin J.T., Eltis L.D.;
RT   "Characterization of BphF, a Rieske-type ferredoxin with a low
RT   reduction potential.";
RL   Biochemistry 40:84-92(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   MEDLINE=21029088; PubMed=11188691; DOI=10.1016/S0969-2126(00)00536-0;
RA   Colbert C.L., Couture M.M.-J., Eltis L.D., Bolin J.T.;
RT   "A cluster exposed: structure of the Rieske ferredoxin from biphenyl
RT   dioxygenase and the redox properties of Rieske Fe-S proteins.";
RL   Structure 8:1267-1278(2000).
CC   -!- FUNCTION: This protein seems to be a 2Fe-2S ferredoxin.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -157 mV;
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the
CC       two subunits of the hydroxylase component (bphA and bphE), a
CC       ferredoxin (bphF) and a ferredoxin reductase (bphG).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase ferredoxin component 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; M86348; AAB63428.1; -.
DR   PIR; E41858; E41858.
DR   PDB; 1FQT; X-ray; A/B=1-109.
DR   InterPro; IPR005806; Rieske_reg.
DR   Pfam; PF00355; Rieske; 1.
KW   2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding.
FT   METAL        43     43       Iron-sulfur (2Fe-2S).
FT   METAL        45     45       Iron-sulfur (2Fe-2S).
FT   METAL        63     63       Iron-sulfur (2Fe-2S).
FT   METAL        66     66       Iron-sulfur (2Fe-2S).
FT   STRAND        4      8
FT   HELIX         9     11
FT   TURN         14     15
FT   STRAND       17     22
FT   TURN         23     24
FT   STRAND       25     32
FT   TURN         33     34
FT   STRAND       35     40
FT   STRAND       42     42
FT   TURN         44     45
FT   STRAND       49     49
FT   TURN         52     53
FT   STRAND       56     57
FT   TURN         58     59
FT   STRAND       60     62
FT   TURN         64     66
FT   STRAND       69     71
FT   TURN         72     74
FT   STRAND       77     79
FT   STRAND       88     88
FT   STRAND       91     94
FT   TURN         95     96
FT   STRAND       97    100
FT   TURN        102    103
FT   STRAND      106    106
SQ   SEQUENCE   109 AA;  11955 MW;  39AE9C8B84232FA4 CRC64;
     MKFTRVCDRR DVPEGEALKV ESGGTSVAIF NVDGELFATQ DRCTHGDWSL SDGGYLEGDV
     VECSLHMGKF CVRTGKVKSP PPCEALKIFP IRIEDNDVLV DFEAGYLAP
//