BPHC_PSES1
ID BPHC_PSES1 Reviewed; 293 AA.
AC P17297; Q52441;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
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 sp. (strain KKS102).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2540155; DOI=10.1128/jb.171.5.2740-2747.1989;
RA Kimbara K., Hashimoto T., Fukuda M., Koana T., Takagi M., Oishi M.,
RA Yano K.;
RT "Cloning and sequencing of two tandem genes involved in degradation of 2,3-
RT dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading
RT soil bacterium Pseudomonas sp. strain KKS102.";
RL J. Bacteriol. 171:2740-2747(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=8048958; DOI=10.1006/bbrc.1994.2008;
RA Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H.,
RA Takagi M., Yano K.;
RT "Identification of the bphA and bphB genes of Pseudomonas sp. strains
RT KKS102 involved in degradation of biphenyl and polychlorinated biphenyls.";
RL Biochem. Biophys. Res. Commun. 202:850-856(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8636975; DOI=10.1006/jmbi.1996.0060;
RA Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M.,
RA Sato M., Yano K., Mitsui Y.;
RT "Three-dimensional structures of free form and two substrate complexes of
RT an extradiol ring-cleavage type dioxygenase, the BphC enzyme from
RT Pseudomonas sp. strain KKS102.";
RL J. Mol. Biol. 255:735-752(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11293547; DOI=10.1016/s0162-0134(00)00172-0;
RA Uragami Y., Senda T., Sugimoto K., Sato N., Nagarajan V., Masai E.,
RA Fukuda M., Mitsui Y.;
RT "Crystal structures of substrate free and complex forms of reactivated
RT BphC, an extradiol type ring-cleavage dioxygenase.";
RL J. Inorg. Biochem. 83:269-279(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF NATIVE ENZYME; SUBSTRATE
RP COMPLEXES AND H145A MUTANT.
RX PubMed=12206778; DOI=10.1016/s0022-2836(02)00673-3;
RA Sato N., Uragami Y., Nishizaki T., Takahashi Y., Sazaki G., Sugimoto K.,
RA Nonaka T., Masai E., Fukuda M., Senda T.;
RT "Crystal structures of the reaction intermediate and its homologue of an
RT extradiol-cleaving catecholic dioxygenase.";
RL J. Mol. Biol. 321:621-636(2002).
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; M26433; AAA25750.1; -; Genomic_DNA.
DR EMBL; D17319; BAA04141.1; -; Genomic_DNA.
DR PIR; A32312; DAPSPC.
DR PDB; 1DHY; X-ray; 2.30 A; A=2-293.
DR PDB; 1EIL; X-ray; 2.00 A; A=2-293.
DR PDB; 1EIQ; X-ray; 2.00 A; A=2-293.
DR PDB; 1EIR; X-ray; 2.00 A; A=2-293.
DR PDB; 1KW3; X-ray; 1.45 A; B=2-293.
DR PDB; 1KW6; X-ray; 1.45 A; B=2-293.
DR PDB; 1KW8; X-ray; 2.00 A; B=2-293.
DR PDB; 1KW9; X-ray; 1.95 A; B=2-293.
DR PDB; 1KWB; X-ray; 2.00 A; B=2-293.
DR PDB; 1KWC; X-ray; 2.10 A; B=2-293.
DR PDBsum; 1DHY; -.
DR PDBsum; 1EIL; -.
DR PDBsum; 1EIQ; -.
DR PDBsum; 1EIR; -.
DR PDBsum; 1KW3; -.
DR PDBsum; 1KW6; -.
DR PDBsum; 1KW8; -.
DR PDBsum; 1KW9; -.
DR PDBsum; 1KWB; -.
DR PDBsum; 1KWC; -.
DR AlphaFoldDB; P17297; -.
DR SMR; P17297; -.
DR DrugBank; DB02923; Biphenyl-2,3-Diol.
DR UniPathway; UPA00155; UER00252.
DR EvolutionaryTrace; P17297; -.
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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..293
FT /note="Biphenyl-2,3-diol 1,2-dioxygenase"
FT /id="PRO_0000085035"
FT DOMAIN 5..119
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 143..265
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 BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1EIR"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1DHY"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 181..194
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 205..217
FT /evidence="ECO:0007829|PDB:1KW3"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1KW3"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1KW3"
SQ SEQUENCE 293 AA; 32245 MW; 53EF1B24502E3B24 CRC64;
MSIERLGYLG FAVKDVPAWD HFLTKSVGLM AAGSAGDAAL YRADQRAWRI AVQPGELDDL
AYAGLEVDDA AALERMADKL RQAGVAFTRG DEALMQQRKV MGLLCLQDPF GLPLEIYYGP
AEIFHEPFLP SAPVSGFVTG DQGIGHFVRC VPDTAKAMAF YTEVLGFVLS DIIDIQMGPE
TSVPAHFLHC NGRHHTIALA AFPIPKRIHH FMLQANTIDD VGYAFDRLDA AGRITSLLGR
HTNDQTLSFY ADTPSPMIEV EFGWGPRTVD SSWTVARHSR TAMWGHKSVR GQR
