ID   BPHA_BURCE     STANDARD;      PRT;   458 AA.
AC   P37333;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 2.
DT   07-FEB-2006, entry version 38.
DE   Biphenyl dioxygenase alpha subunit (EC 1.14.12.18) (Biphenyl
DE   2,3-dioxygenase).
GN   Name=bphA;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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) =
CC       (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit.
CC   -!- COFACTOR: Binds 1 iron ion 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   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; M86348; AAB63425.1; -; Genomic_DNA.
DR   HSSP; P23094; 1O7N.
DR   SMR; P37333; 17-457.
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.
FT   INIT_MET      0      0
FT   CHAIN         1    458       Biphenyl dioxygenase alpha subunit.
FT                                /FTId=PRO_0000085046.
FT   DOMAIN       56    163       Rieske.
FT   METAL        99     99       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       101    101       Iron-sulfur (2Fe-2S) (via pros nitrogen)
FT                                (By similarity).
FT   METAL       119    119       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       122    122       Iron-sulfur (2Fe-2S) (via pros nitrogen)
FT                                (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
//