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 28-JAN-2026, entry version 81. 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; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR InterPro; IPR037523; VOC_core. DR InterPro; IPR000486; Xdiol_ring_cleave_dOase_1/2. DR Pfam; PF00903; Glyoxalase; 1. DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 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 //