ID   BPHC_BACPJ              Reviewed;         315 AA.
AC   Q8GR45;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   20-JAN-2009, entry version 26.
DE   RecName: Full=Manganese-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase;
DE            EC=1.13.11.39;
DE   AltName: Full=Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase;
DE   AltName: Full=Mn(II)-dependent 23OHBP oxygenase;
GN   Name=bphC;
OS   Bacillus sp. (strain JF8).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=209076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND
RP   CHARACTERIZATION.
RX   MEDLINE=22679171; PubMed=12672826; DOI=10.1074/jbc.M210240200;
RA   Hatta T., Mukerjee-Dhar G., Damborsky J., Kiyohara H., Kimbara K.;
RT   "Characterization of a novel thermostable Mn(II)-dependent 2,3-
RT   dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and
RT   naphthalene-degrading Bacillus sp. JF8.";
RL   J. Biol. Chem. 278:21483-21492(2003).
CC   -!- FUNCTION: Catalyzes the meta-cleavage of the hydroxylated biphenyl
CC       ring. The enzyme can oxidize a wide range of substrates, and the
CC       substrate preference order is 2,3-dihydroxybiphenyl > 3-
CC       methylcatechol > catechol > 4-methylcatechol > 4-chlorocatechol.
CC   -!- CATALYTIC ACTIVITY: Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6-
CC       phenylhexa-2,4-dienoate + H(2)O.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.095 uM for 2,3-dihydroxybiphenyl (at 60 degrees Celsius and
CC         pH 7.5);
CC         KM=1.0 uM for 3-methylcatechol (at 60 degrees Celsius and pH
CC         7.5);
CC         KM=25.0 uM for 4-chlorocatechol (at 60 degrees Celsius and pH
CC         7.5);
CC         KM=103.0 uM for catechol (at 60 degrees Celsius and pH 7.5);
CC         KM=111.0 uM for 4-methylcatechol (at 60 degrees Celsius and pH
CC         7.5);
CC         Vmax=5.7 umol/min/mg enzyme with 2,3-dihydroxybiphenyl as
CC         substrate (at 60 degrees Celsius and pH 7.5);
CC         Vmax=3.4 umol/min/mg enzyme with 3-methylcatechol as substrate
CC         (at 60 degrees Celsius and pH 7.5);
CC         Vmax=1.8 umol/min/mg enzyme with catechol as substrate (at 60
CC         degrees Celsius and pH 7.5);
CC         Vmax=1.3 umol/min/mg enzyme with 4-methylcatechol as substrate
CC         (at 60 degrees Celsius and pH 7.5);
CC         Vmax=0.68 umol/min/mg enzyme with 4-chlorocatechol as substrate
CC         (at 60 degrees Celsius and pH 7.5);
CC       pH dependence:
CC         Optimum pH is 7.5;
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius;
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-
CC       2,4-pentadienoic acid and benzoic acid from biphenyl: step 3/4.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase
CC       family.
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DR   EMBL; AB092521; BAC23089.1; -; Genomic_DNA.
DR   HSSP; Q44048; 1F1U.
DR   BRENDA; 1.13.11.39; 1000.
DR   GO; GO:0018583; F:biphenyl-2,3-diol 1,2-dioxygenase activity; IEA:EC.
DR   GO; GO:0030145; F:manganese ion binding; 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; IPR004360; Glyas_bleo-R_dOase.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   ProDom; PD002334; Gly_diox; 2.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase;
KW   Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN         1    315       Manganese-dependent 2,3-dihydroxybiphenyl
FT                                1,2-dioxygenase.
FT                                /FTId=PRO_0000085040.
FT   METAL       153    153       Manganese (By similarity).
FT   METAL       216    216       Manganese (By similarity).
FT   METAL       269    269       Manganese (By similarity).
SQ   SEQUENCE   315 AA;  36323 MW;  306CD094914E1AF4 CRC64;
     MTAEIAKFGH IALITPNLEK SVWFFRDIVG LEEVDRQGDT IFLRAWGDWE HHTLSLTPGN
     RARVDHIAWR TKRPEDVETF AEQLKAKGTE VQWIEPGEEK GQGKAIRFRL PNGYPFEIYY
     DVEKPKAPEG KKSRLKNNVY RPSYGIAPRR IDHVNVWTTN PSEIHQWLKD NMGFKMREYI
     RLNNGFVAGG WMSVTPLVHD IGVMVDPKGQ PNRLHHFAYY LDNVTDILRA ADILREHDIT
     IEMGGPGRHG ISQAFFLYVK DPGSGHRLEL FSGGYLIFDP DWEPIEWQEH ELQEGLIWYG
     PEMKPGGPMD DTTEC
//