BPHC_PSEFK
ID BPHC_PSEFK Reviewed; 303 AA.
AC P08695;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
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;
OS Pseudomonas furukawaii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=1149133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 10086 / NBRC 110670 / KF707;
RX PubMed=3793719; DOI=10.1128/jb.169.1.427-429.1987;
RA Furukawa K., Arimura N., Miyazaki T.;
RT "Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of
RT Pseudomonas pseudoalcaligenes.";
RL J. Bacteriol. 169:427-429(1987).
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: Homooctamer.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; M15333; AAA25753.1; -; Genomic_DNA.
DR AlphaFoldDB; P08695; -.
DR SMR; P08695; -.
DR STRING; 1149133.ppKF707_3400; -.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..303
FT /note="Biphenyl-2,3-diol 1,2-dioxygenase"
FT /id="PRO_0000085034"
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 REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 303 AA; 33206 MW; 6844D0ABBD81FED5 CRC64;
MSIRSLGYMG FAVSDVAAWR SFLTQKLGLM EAGTTDNGDL FRIDSRAWRI AVQQGEVDDL
AFAGYEVADA AGLAQMADKL KQAGIAVTTG DASLARRRGV TGLITFADPF GLPLEIYYGA
SEVFEKPFLP GAAVSGFLTG EQGLGHFVRC VPDSDKALAF YTDVLGFQLS DVIDMKMGPD
VTVPVYFLHC NERHHTLAIA AFPLPKRIHH FMLEVASLDD VGFAFDRVDA DGLITSTLGR
HTNDHMVSFY ASTPSGVEVE YGWSARTVDR SWVVVRHDSP SMWGHKSVRD KALRATKHEQ
QPE
