BPHC_PARXL
ID BPHC_PARXL Reviewed; 298 AA.
AC P47228; Q13FT6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Biphenyl-2,3-diol 1,2-dioxygenase;
DE EC=1.13.11.39;
DE AltName: Full=2,3-dihydroxybiphenyl dioxygenase;
DE Short=DHBD;
DE AltName: Full=23OHBP oxygenase;
GN Name=bphC; OrderedLocusNames=Bxeno_C1125; ORFNames=Bxe_C1191;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8344527; DOI=10.1016/0378-1119(93)90345-4;
RA Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.;
RT "Genetic analysis of a Pseudomonas locus encoding a pathway for
RT biphenyl/polychlorinated biphenyl degradation.";
RL Gene 130:47-55(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-32, SUBSTRATE CHARACTERIZATION, PRELIMINARY
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=8428946; DOI=10.1016/s0021-9258(18)53834-5;
RA Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.;
RT "Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-
RT dioxygenase.";
RL J. Biol. Chem. 268:2727-2732(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=7481800; DOI=10.1126/science.270.5238.976;
RA Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T.;
RT "Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a
RT PCB-degrading pseudomonad.";
RL Science 270:976-980(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9857017; DOI=10.1074/jbc.273.52.34887;
RA Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.;
RT "Molecular basis for the stabilization and inhibition of 2,3-
RT dihydroxybiphenyl 1,2-dioxygenase by t-butanol.";
RL J. Biol. Chem. 273:34887-34895(1998).
CC -!- FUNCTION: Shows a preference for catechols with groups immediately
CC adjacent to the hydroxyl substituents.
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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for biphenyl-2,3-diol;
CC Note=Substrate inhibition occurs at 300 uM (+/- 20 uM).;
CC pH dependence:
CC Optimum pH is 8.0.;
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 3/4.
CC -!- SUBUNIT: Homooctamer. The enzyme is composed of two planar tetramers
CC rotated at 45 degrees relative to each other, with a channel in the
CC middle. {ECO:0000269|PubMed:8428946}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; X66122; CAA46910.1; -; Genomic_DNA.
DR EMBL; CP000272; ABE37053.1; -; Genomic_DNA.
DR PIR; JN0815; JN0815.
DR PDB; 1HAN; X-ray; 1.90 A; A=2-298.
DR PDB; 1KMY; X-ray; 2.00 A; A=2-298.
DR PDB; 1KND; X-ray; 1.90 A; A=2-298.
DR PDB; 1KNF; X-ray; 1.90 A; A=2-298.
DR PDB; 1LGT; X-ray; 1.70 A; A=2-298.
DR PDB; 1LKD; X-ray; 1.70 A; A=2-298.
DR PDBsum; 1HAN; -.
DR PDBsum; 1KMY; -.
DR PDBsum; 1KND; -.
DR PDBsum; 1KNF; -.
DR PDBsum; 1LGT; -.
DR PDBsum; 1LKD; -.
DR AlphaFoldDB; P47228; -.
DR SMR; P47228; -.
DR STRING; 266265.Bxe_C1191; -.
DR DrugBank; DB02232; 1,2-Dihydroxybenzene.
DR DrugBank; DB03259; 2',6'-Dichloro-Biphenyl-2,6-Diol.
DR DrugBank; DB01925; 2'-Chloro-Biphenyl-2,3-Diol.
DR DrugBank; DB03454; 3-methyl-benzene-1,2-diol.
DR DrugBank; DB02923; Biphenyl-2,3-Diol.
DR DrugBank; DB03900; tert-butanol.
DR EnsemblBacteria; ABE37053; ABE37053; Bxe_C1191.
DR KEGG; bxb:DR64_8614; -.
DR KEGG; bxe:Bxe_C1191; -.
DR eggNOG; COG0346; Bacteria.
DR OMA; EFGTDGM; -.
DR SABIO-RK; P47228; -.
DR UniPathway; UPA00155; UER00252.
DR EvolutionaryTrace; P47228; -.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0018583; F:biphenyl-2,3-diol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:InterPro.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR017626; DiOHbiphenyl_dOase.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 2.
DR TIGRFAMs; TIGR03213; 23dbph12diox; 1.
DR PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8428946"
FT CHAIN 2..298
FT /note="Biphenyl-2,3-diol 1,2-dioxygenase"
FT /id="PRO_0000085033"
FT DOMAIN 5..119
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 143..264
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 146
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 181..194
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 205..216
FT /evidence="ECO:0007829|PDB:1LGT"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:1LGT"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 234..244
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1LGT"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:1LGT"
SQ SEQUENCE 298 AA; 32471 MW; ADC0E4709E193FAB CRC64;
MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI AVQQGEVDDL
AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV TGLITFADPF GLPLEIYYGA
SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC VPDSDKALAF YTDVLGFQLS DVIDMKMGPD
VTVPAYFLHC NERHHTLAIA AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR
HTNDHMVSFY ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KAAARNKA
