ID   CBDC_BURCE     STANDARD;      PRT;   339 AA.
AC   Q51603; O08068;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   2-halobenzoate 1,2-dioxygenase electron transfer component [Includes:
DE   Ferredoxin; Ferredoxin--NAD(+) reductase (EC 1.18.1.3)].
GN   Name=cbdC;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OG   Plasmid pBAH1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=2CBS;
RX   MEDLINE=95138027; PubMed=7530709;
RA   Haak B., Fetzner S., Lingens F.;
RT   "Cloning, nucleotide sequence, and expression of the plasmid-encoded
RT   genes for the two-component 2-halobenzoate 1,2-dioxygenase from
RT   Pseudomonas cepacia 2CBS.";
RL   J. Bacteriol. 177:667-675(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-19, AND CHARACTERIZATION.
RC   STRAIN=2CBS;
RX   MEDLINE=92104974; PubMed=1370284;
RA   Fetzner S., Mueller R., Lingens F.;
RT   "Purification and some properties of 2-halobenzoate 1,2-dioxygenase, a
RT   two-component enzyme system from Pseudomonas cepacia 2CBS.";
RL   J. Bacteriol. 174:279-290(1992).
CC   -!- FUNCTION: Electron transfer component of 2-halobenzoate 1,2-
CC       dioxygenase system.
CC   -!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
CC       ferredoxin + NADH.
CC   -!- COFACTOR: Binds 1 FAD and 1 2Fe-2S cluster per subunit (By
CC       similarity).
CC   -!- PATHWAY: First step in the catabolic degradation of 2-
CC       halobenzoate.
CC   -!- SUBUNIT: Monomer. It is part of 2-halobenzoate dioxygenase two
CC       component enzyme system. The other component is a dioxygenase
CC       component consisiting of 3 large (CbdA) subunits and 3 small
CC       (CbdB) subunits.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase ferredoxin reductase family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 2Fe2S plant-
CC       type ferredoxin 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; X79076; CAA55683.1; -.
DR   HSSP; P07771; 1KRH.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR008333; FAD_binding_6.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR001433; Oxred_FAD/NAD(P).
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   PROSITE; PS00197; 2FE2S_FERREDOXIN; 1.
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Plasmid.
FT   DOMAIN       29     97       Ferredoxin.
FT   DOMAIN       98    336       Ferredoxin-reductase.
FT   METAL        40     40       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        45     45       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        48     48       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        80     80       Iron-sulfur (2Fe-2S) (By similarity).
SQ   SEQUENCE   339 AA;  37265 MW;  075DFCC7A9F9AE63 CRC64;
     MLHSIALRFE DDVTYFITSS EHETVADAAY QHGIRIPLDC RNGVCGTCKG FCEHGEYDGG
     DYIEDALSAD EAREGFVLPC QMQARTDCVV RILASSSACQ VKKSTMTGQM TEIDRGSSST
     LQFTLAIDPS SKVDFLPGQY AQLRIPGTTE SRAYSYSSMP GSSHVTFLVR DVPNGKMSGY
     LRNQATITET FTFDGPYGAF YLREPVRPIL MLAGGTGLAP FLSMLQYMAG LQRNDLPSVR
     LVYGVNRDDD LVGLDKLDEL ATQLSGFSYI TTVVDKDSAQ LRRGYVTQQI TNDDMNGGDV
     DIYVCGPPPM VEAVRSWLAA EKLNPVNFYF EKFAPTVGN
//