ID   CBDA_BURCE     STANDARD;      PRT;   464 AA.
AC   Q51601;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   2-halobenzoate 1,2-dioxygenase large subunit (EC 1.14.12.13) (2-
DE   chlorobenzoate 1,2-dioxygenase).
GN   Name=cbdA;
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 1-20, 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: Component of 2-halobenzoate dioxygenase multicomponent
CC       enzyme system which catalyzes the incorporation of both atoms of
CC       molecular oxygen into 2-halobenzoate to form catechol.
CC   -!- CATALYTIC ACTIVITY: 2-chlorobenzoate + NADH + O(2) = catechol +
CC       chloride + NAD(+) + CO(2).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster and 1 iron(II) ion per subunit
CC       (By similarity).
CC   -!- PATHWAY: First step in the catabolic degradation of 2-
CC       halobenzoate.
CC   -!- SUBUNIT: Heterohexamer of 3 large (CbdA) subunits and 3 small
CC       (CbdB) subunits. The heterohexamer is part of 2-halobenzoate
CC       dioxygenase two component enzyme system. The other component is a
CC       NADH:acceptor reductase (CdbC).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase alpha subunit 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; CAA55681.1; -.
DR   InterPro; IPR005806; Rieske_reg.
DR   InterPro; IPR001663; Ring_hydroxyl_A.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Oxidoreductase; Plasmid.
FT   INIT_MET      0      0
FT   METAL        97     97       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        99     99       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       117    117       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       120    120       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       226    226       Iron (By similarity).
FT   METAL       231    231       Iron (By similarity).
SQ   SEQUENCE   464 AA;  52346 MW;  F356DCA226D39BFE CRC64;
     STPLIAGTGP SAVRQLISNA VQNDPVSGNF RCRRDIFTDA ALFDYEMKYI FEQNWVFLAH
     ESQVANPDDY LVSNIGRQPV IITRNKAGDV SAVINACSHR GAELCRRKQG NRSTFTCQFH
     GWTFSNTGKL LKVKDGQDDN YPEGFNVDGS HDLTRIPSFA NYRGFLFGSM NPDACPIEEH
     LGGSKAILDQ VIDQTPGELE VLRGSSSYIY DGNWKLQIEN GADGYHVGSV HWNYVATIGR
     RDRTSDTIRT VDVTTWSKKN IGGTYTFEHG HMLLWTRLPN PEVRPVFARR EELKARVGEE
     VADAIVNQTR NLCIYPNLYV MDQISTQIRV VRPISVDKTE VTIYCFAPRD ESEEVRNARI
     RQYEDFFNVS GMGTPDDLEE FRACQSGYRG SAREWNDLSR GAPHWISGPD DNARRLGLAP
     LMSGARMEDE GLFVQQHTYW AETMLRGIEA EPKVFNVQPV EVAQ
//