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   27-MAR-2024, entry version 157.
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; Pseudomonadota; 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   KEGG; bxb:DR64_8614; -.
DR   KEGG; bxe:Bxe_C1191; -.
DR   eggNOG; COG0346; Bacteria.
DR   OrthoDB; 9803142at2; -.
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   CDD; cd07237; BphC1-RGP6_C_like; 1.
DR   CDD; cd07252; BphC1-RGP6_N_like; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 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   NCBIfam; TIGR03213; 23dbph12diox; 1.
DR   PANTHER; PTHR21366; GLYOXALASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR21366:SF34; IRON-DEPENDENT EXTRADIOL DIOXYGENASE; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
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; 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
//