ID   CBDC_BURCE     STANDARD;      PRT;   339 AA.
AC   Q51603; O08068;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   18-APR-2006, entry version 48.
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   pBAH1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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
CC       1,2-dioxygenase system.
CC   -!- CATALYTIC ACTIVITY: Reduced ferredoxin + NAD(+) = oxidized
CC       ferredoxin + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC   -!- PATHWAY: First step in the catabolic degradation of
CC       2-halobenzoate.
CC   -!- SUBUNIT: Monomer. It is part of 2-halobenzoate dioxygenase two
CC       component enzyme system. The other component is a dioxygenase
CC       component consisting of 3 large (CbdA) subunits and 3 small (CbdB)
CC       subunits.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase ferredoxin reductase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
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DR   EMBL; X79076; CAA55683.1; -; Genomic_DNA.
DR   HSSP; P07771; 1KRH.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR012675; Ferredoxin_fold.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR012254; MP_mOase_red.
DR   InterPro; IPR008333; Oxred_FAD_bd.
DR   InterPro; IPR001433; Oxred_FAD_NAD_bd.
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   PIRSF; PIRSF000044; Cis_Diol_DH_RD; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Plasmid.
FT   CHAIN         1    339       2-halobenzoate 1,2-dioxygenase electron
FT                                transfer component.
FT                                /FTId=PRO_0000167656.
FT   DOMAIN        3     96       2Fe-2S ferredoxin-type.
FT   REGION       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
//