BPHC_SPHPI
ID BPHC_SPHPI Reviewed; 299 AA.
AC P11122;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=13689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=3137968; DOI=10.1021/bi00411a015;
RA Taira K., Hayase N., Arimura N., Yamashita S., Miyazaki T., Furukawa K.;
RT "Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase
RT gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1.";
RL Biochemistry 27:3990-3996(1988).
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; M20640; AAA25678.1; -; Genomic_DNA.
DR PIR; A28718; A28718.
DR AlphaFoldDB; P11122; -.
DR SMR; P11122; -.
DR STRING; 13689.BV96_03597; -.
DR eggNOG; COG0346; Bacteria.
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; 1.
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..299
FT /note="Biphenyl-2,3-diol 1,2-dioxygenase"
FT /id="PRO_0000085036"
FT DOMAIN 6..121
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 146..267
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 33095 MW; 29746CAB79D6FC7B CRC64;
MVAVTELGYL GLTVTNLDAW RSYAAEVAGM EIVDEGEGDR LYLRMDQWHH RIVLHASDSD
DLAYLGWRVA DPVEFDAMVA KLTAAGISLT VASEAEARER RVLGLAKLAD PGGNPTEIFY
GPQVDTHKPF HPGRPMYGKF VTGSEGIGHC ILRQDDVPAA AAFYGLLGLR GSVEYHLQLP
NGMVAQPYFM HCNERQHSVA FGLGPMEKRI NHLMFEYTDL DDLGLAHDIV RARKIDVALQ
LGKHANDQAL TFYCANPSGW LWEFGWGARK APSQQEYYTR DIFGHGNEAA GYGMDIPLG
