ID   BPHA_BURCE     STANDARD;      PRT;   458 AA.
AC   P37333;
DT   01-OCT-1994 (Rel. 30, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Biphenyl dioxygenase alpha subunit (EC 1.14.12.18) (Biphenyl 2,3-
DE   dioxygenase).
GN   Name=bphA;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LB400;
RX   MEDLINE=92234948; PubMed=1569021;
RA   Erickson B.D., Mondello F.J.;
RT   "Nucleotide sequencing and transcriptional mapping of the genes
RT   encoding biphenyl dioxygenase, a multicomponent polychlorinated-
RT   biphenyl-degrading enzyme in Pseudomonas strain LB400.";
RL   J. Bacteriol. 174:2903-2912(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION.
RC   STRAIN=LB400;
RX   MEDLINE=96011369; PubMed=7592331;
RA   Haddock J.D., Gibson D.T.;
RT   "Purification and characterization of the oxygenase component of
RT   biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400.";
RL   J. Bacteriol. 177:5834-5839(1995).
RN   [3]
RP   ERRATUM.
RA   Haddock J.D., Gibson D.T.;
RL   J. Bacteriol. 178:2158-2158(1996).
CC   -!- CATALYTIC ACTIVITY: Biphenyl + NADH + O(2) = (1S,2R)-3-
CC       phenylcyclohexa-3,5-diene-1,2-diol + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster and 1 iron atom per subunit.
CC   -!- PATHWAY: Biphenyl-polychlorinated biphenyl degradation pathway;
CC       first step.
CC   -!- SUBUNIT: Heterohexamer consisting of three BphA subunits and three
CC       BphE subunits. A ferredoxin (BphF) and a ferredoxin reductase
CC       (BphG) must be present to obtain activity.
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
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DR   EMBL; M86348; AAB63425.1; -.
DR   HSSP; P23094; 1O7N.
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.
FT   INIT_MET      0      0
FT   METAL        99     99       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       101    101       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       119    119       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       122    122       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       232    232       Iron (By similarity).
FT   METAL       238    238       Iron (By similarity).
SQ   SEQUENCE   458 AA;  51382 MW;  AF5BF1E05BAFFDF4 CRC64;
     SSAIKEVQGA PVKWVTNWTP EAIRGLVDQE KGLLDPRIYA DQSLYELELE RVFGRSWLLL
     GHESHVPETG DFLATYMGED PVVMVRQKDK SIKVFLNQCR HRGMRICRSD AGNAKAFTCS
     YHGWAYDIAG KLVNVPFEKE AFCDKKEGDC GFDKAEWGPL QARVATYKGL VFANWDVQAP
     DLETYLGDAR PYMDVMLDRT PAGTVAIGGM QKWVIPCNWK FAAEQFCSDM YHAGTTTHLS
     GILAGIPPEM DLSQAQIPTK GNQFRAAWGG HGSGWYVDEP GSLLAVMGPK VTQYWTEGPA
     AELAEQRLGH TGMPVRRMVG QHMTIFPTCS FLPTFNNIRI WHPRGPNEIE VWAFTLVDAD
     APAEIKEEYR RHNIRNFSAG GVFEQDDGEN WVEIQKGLRG YKAKSQPLNA QMGLGRSQTG
     HPDFPGNVGY VYAEEAARGM YHHWMRMMSE PSWATLKP
//