ID   CBDB_BURCE     STANDARD;      PRT;   164 AA.
AC   Q51602; O08067;
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 small subunit (EC 1.14.12.13) (2-
DE   chlorobenzoate 1,2-dioxygenase).
GN   Name=cbdB;
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 1-14, 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   -!- 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 beta 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; CAA55682.1; -.
DR   InterPro; IPR000391; Ring_hydroxyl_B.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
KW   Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; NAD; Oxidoreductase; Plasmid.
FT   INIT_MET      0      0
FT   CONFLICT     11     11       V -> C (in Ref. 2).
SQ   SEQUENCE   164 AA;  19501 MW;  442FF5EFA8ED2F68 CRC64;
     TSLESSYLDV VAFIFREARL LDDRSWDEWL ECYDPEAVFW MPCWDDADTL VDDPRKHVSL
     IYYSDRMGLE DRVFRLRSER SGASTPEPRT THNIANVEIL ERTERQIEAR FNWHTMNYRY
     KLLDHYFGTS FYTLKVSSSG LSILNKKVVL KNDLIHQVID VYHV
//