BPHC_BACPJ
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 03-AUG-2022, entry version 58.
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; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1921421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND CHARACTERIZATION.
RX 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-methylcatechol
CC > catechol > 4-methylcatechol > 4-chlorocatechol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-
CC dienoate + H(+); Xref=Rhea:RHEA:14413, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16205, ChEBI:CHEBI:58284;
CC EC=1.13.11.39;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12672826};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:12672826};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.095 uM for 2,3-dihydroxybiphenyl (at 60 degrees Celsius and pH
CC 7.5) {ECO:0000269|PubMed:12672826};
CC KM=1.0 uM for 3-methylcatechol (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:12672826};
CC KM=25.0 uM for 4-chlorocatechol (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:12672826};
CC KM=103.0 uM for catechol (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:12672826};
CC KM=111.0 uM for 4-methylcatechol (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:12672826};
CC Vmax=5.7 umol/min/mg enzyme with 2,3-dihydroxybiphenyl as substrate
CC (at 60 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12672826};
CC Vmax=3.4 umol/min/mg enzyme with 3-methylcatechol as substrate (at 60
CC degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12672826};
CC Vmax=1.8 umol/min/mg enzyme with catechol as substrate (at 60 degrees
CC Celsius and pH 7.5) {ECO:0000269|PubMed:12672826};
CC Vmax=1.3 umol/min/mg enzyme with 4-methylcatechol as substrate (at 60
CC degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12672826};
CC Vmax=0.68 umol/min/mg enzyme with 4-chlorocatechol as substrate (at
CC 60 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12672826};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12672826};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:12672826};
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 3/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12672826}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB092521; BAC23089.1; -; Genomic_DNA.
DR RefSeq; WP_020961664.1; NC_022092.1.
DR AlphaFoldDB; Q8GR45; -.
DR SMR; Q8GR45; -.
DR KEGG; ag:BAC23089; -.
DR BRENDA; 1.13.11.39; 691.
DR UniPathway; UPA00155; UER00252.
DR GO; GO:0018583; F:biphenyl-2,3-diol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Manganese; Metal-binding; Oxidoreductase; Repeat.
FT CHAIN 1..315
FT /note="Manganese-dependent 2,3-dihydroxybiphenyl 1,2-
FT dioxygenase"
FT /id="PRO_0000085040"
FT DOMAIN 7..121
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 150..273
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
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
