ID   BPHA_COMTE              Reviewed;         457 AA.
AC   Q46372;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Biphenyl dioxygenase subunit alpha;
DE            EC=1.14.12.18;
DE   AltName: Full=Biphenyl 2,3-dioxygenase;
GN   Name=bphA;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-356;
RX   MEDLINE=97045812; PubMed=8890734; DOI=10.1016/0378-1119(96)00039-X;
RA   Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D.,
RA   Shareck F., Barriault D., Guillemette I., Juteau J.-M.;
RT   "Sequencing of Comamonas testosteroni strain B-356-
RT   biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships
RT   among Gram-negative bacterial biphenyl dioxygenases.";
RL   Gene 174:195-202(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 per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-
CC       2,4-pentadienoic acid and benzoic acid from biphenyl: step 1/4.
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 (By similarity).
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; U47637; AAC44526.1; -; Genomic_DNA.
DR   PIR; JC4993; JC4993.
DR   HSSP; P23094; 1O7N.
DR   SMR; Q46372; 18-456.
DR   BRENDA; 1.14.12.18; 4566.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   PANTHER; PTHR21266:SF2; Rng_hydr_dOase-A; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN         1    457       Biphenyl dioxygenase subunit alpha.
FT                                /FTId=PRO_0000085047.
FT   DOMAIN       58    174       Rieske.
FT   METAL       100    100       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       102    102       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       120    120       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       123    123       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       233    233       Iron (By similarity).
FT   METAL       239    239       Iron (By similarity).
SQ   SEQUENCE   457 AA;  51692 MW;  D133FC0635FACBF5 CRC64;
     MSSTMKDTQE APVRWSRNWT PDAIRALVDQ DNGKLDARIY ADQDLYQLEL ERVFGRSWLM
     LGHETHIPKI GDYLTTYMGE DPVIMVRQKD QSIKVFLNQC RHRGMRIVRS DGGNAKAFTC
     TYHGWAYDIA GNLVNVPFEK EAFCDKKEGD CGFDKADWGP LQARVETYKG LVFANWDPEA
     PDLKTYLSDA MPYMDVMLDR TEAGTEAIGG IQKWVIPCNW KFAAEQFCSD MYHAGTMSHL
     SGVLAGLPPE MDLTQIQLSK NGNQFRSAWG GHGAGWFIND SSILLSVVGP KITQYWTQGP
     AAEKAARRVP QLPILDMFGQ HMTVFPTCSF LPGINTIRTW HPRGPNEVEV WAFVLVDADA
     PEDIKEEFRL QNIRTFNAGG VFEQDDGENW VEIQRVMRGH KAKSTSLCAK MGLNVPNKNN
     PAYPGKTAYV YAEEAARGMY HHWSRMMSEP SWDTLKP
//