ID   CBDA_BURCE     STANDARD;      PRT;   464 AA.
AC   Q51601;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   07-FEB-2006, entry version 35.
DE   2-halobenzoate 1,2-dioxygenase large subunit (EC 1.14.12.13)
DE   (2-chlorobenzoate 1,2-dioxygenase).
GN   Name=cbdA;
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 1-20, 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 per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- PATHWAY: First step in the catabolic degradation of
CC       2-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   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; X79076; CAA55681.1; -; Genomic_DNA.
DR   InterPro; IPR005806; Rieske_reg.
DR   InterPro; IPR001663; Rng_hydr_dOase_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   CHAIN         1    464       2-halobenzoate 1,2-dioxygenase large
FT                                subunit.
FT                                /FTId=PRO_0000085051.
FT   DOMAIN       54    157       Rieske.
FT   METAL        97     97       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        99     99       Iron-sulfur (2Fe-2S) (via pros nitrogen)
FT                                (By similarity).
FT   METAL       117    117       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       120    120       Iron-sulfur (2Fe-2S) (via pros nitrogen)
FT                                (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
//