ID   BPHG_BURCE     STANDARD;      PRT;   408 AA.
AC   P37337;
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--NAD(+) reductase component
DE   (EC 1.18.1.3).
GN   Name=bphG;
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.
CC   -!- FUNCTION: Part of the electron transfer component of biphenyl
CC       dioxygenase, transfers electrons from ferredoxin (bphF) to NADH.
CC   -!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
CC       ferredoxin + NADH.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Biphenyl and polychlorinated biphenyl degradation.
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 reductase 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; M86348; AAB63429.1; -.
DR   PIR; F41858; F41858.
DR   HSSP; Q52437; 1D7Y.
DR   InterPro; IPR000759; Adrndx_reductase.
DR   InterPro; IPR001327; FAD_pyr_redox.
DR   InterPro; IPR000205; NAD_BS.
DR   InterPro; IPR001100; Pyr_redox.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD;
KW   Oxidoreductase.
FT   NP_BIND       4     35       FAD (ADP part) (Potential).
FT   NP_BIND     145    173       NAD (ADP part) (Potential).
SQ   SEQUENCE   408 AA;  42954 MW;  8A52BB01688667A9 CRC64;
     MIDTIAIIGA GLAGSTAARA LRAQGYEGRI HLLGDESHQA YDRTTLSKTV LAGEQPEPPA
     ILDSAWYASA HVDVQLGRRV SCLDLANRQI QFESGAPLAY DRLLLATGAR ARRMAIRGGD
     LAGIHTLRDL ADSQALRQAL QPGQSLVIVG GGLIGCEVAT TARKLSVHVT ILEAGDELLV
     RVLGHRTGAW CRAELERMGV RVERNAQAAR FEGQGQVRAV ICADGRRVPA DVVLVSIGAE
     PADELARAAG IACARGVLVD ATGATSCPEV FAAGDVAAWP LRQGGQRSLE TYLNSQMEAE
     IAASAMLSQP VPAPQVPTSW TEIAGHRIQM IGDAEGPGEI VVRGDAQSGQ PIVLLRLLDG
     CVEAATAINA TREFSVATRL VGTRVSVSAE QLQDVGSNLR DLLKAKPN
//