ID   BPHC2_RHOGO             Reviewed;         190 AA.
AC   P47232;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Biphenyl-2,3-diol 1,2-dioxygenase 2;
DE            EC=1.13.11.39;
DE   AltName: Full=2,3-dihydroxybiphenyl dioxygenase II;
DE            Short=DHBD II;
DE   AltName: Full=23OHBP oxygenase II;
DE   AltName: Full=Biphenyl-2,3-diol 1,2-dioxygenase II;
GN   Name=bphC2;
OS   Rhodococcus globerulus.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=33008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28, AND
RP   CHARACTERIZATION.
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   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; X75634; CAA53298.1; -; Genomic_DNA.
DR   PIR; C53419; C53419.
DR   AlphaFoldDB; P47232; -.
DR   SMR; P47232; -.
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   Gene3D; 3.10.180.10; -; 1.
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; 1.
DR   PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8126007"
FT   CHAIN           2..190
FT                   /note="Biphenyl-2,3-diol 1,2-dioxygenase 2"
FT                   /id="PRO_0000085038"
FT   DOMAIN          6..124
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         9
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  20844 MW;  F0B362C3BECF3679 CRC64;
     MTATPKFAHV VLQTSRFEAM RDWYCTVLDA HVVYEGHGLC FITFDEEHHR VALLGAPTAL
     EPRNPGAAGM HHTAYTFDTL GDLLDRYESL KSKGIEPKVP IQHGVTTSLY YQDPDGNFVE
     LQIDNFSTPD EATAYMNGPE YGGNPVGVSF DPVLIPQALS AGTPVDRITT HAWALETTPD
     LPNPMIALTS