ID   BPHC1_RHOGO             Reviewed;         291 AA.
AC   P47231;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Biphenyl-2,3-diol 1,2-dioxygenase 1;
DE            EC=1.13.11.39;
DE   AltName: Full=2,3-dihydroxybiphenyl dioxygenase I;
DE            Short=DHBD I;
DE   AltName: Full=23OHBP oxygenase I;
DE   AltName: Full=Biphenyl-2,3-diol 1,2-dioxygenase I;
GN   Name=bphC1;
OS   Rhodococcus globerulus.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=33008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P6;
RX   PubMed=8126007; DOI=10.1016/s0021-9258(17)37358-1;
RA   Asturias J.A., Eltis L.D., Prucha M., Timmis K.N.;
RT   "Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in
RT   Rhodococcus globerulus P6. Identification of a new family of extradiol
RT   dioxygenases.";
RL   J. Biol. Chem. 269:7807-7815(1994).
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   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC       pentadienoate and benzoate from biphenyl: step 3/4.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; X75633; CAA53297.1; -; Genomic_DNA.
DR   PIR; B53419; B53419.
DR   AlphaFoldDB; P47231; -.
DR   SMR; P47231; -.
DR   UniPathway; UPA00155; UER00252.
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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase; Repeat.
FT   CHAIN           1..291
FT                   /note="Biphenyl-2,3-diol 1,2-dioxygenase 1"
FT                   /id="PRO_0000085037"
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                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32081 MW;  104F189FE1EDDA6A CRC64;
     MSVQRLGYLG IEVSDVDAWR TYATMRLGAM EAPAPEGTAR FRLDSRAWRF MVTPGPADDL
     SVAGYEVDSE GALMQVKTRL EAYGVKVTSE SSELAAERGV LGLISCVDPA GTRLEIYYGG
     TEMFEVPFAS PTGVKEFRTD DQGMGHYVLA VPDVDAALDF YVQGLGFHLS DVIDWQVSPE
     VSVRLHFLHC NGRHHTLAVV GMPSDKKMHH LMIETTNLDD VGLAYDRCVE DDAVILTLGR
     HTNDHMVSFY GATPSGFAVE FGWGSRVVEP GWSVVRYDAI SIWGHKIMRG E