DBFB_SPHPI
ID DBFB_SPHPI Reviewed; 294 AA.
AC P47243;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2,2',3-trihydroxybiphenyl dioxygenase;
DE EC=1.13.11.-;
GN Name=dbfB;
OS Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=13689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-64.
RC STRAIN=RW1;
RX PubMed=8226678; DOI=10.1128/jb.175.22.7313-7320.1993;
RA Happe B., Eltis L.D., Poth H., Hedderich R., Timmis K.N.;
RT "Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol
RT dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium
RT Sphingomonas sp. strain RW1.";
RL J. Bacteriol. 175:7313-7320(1993).
RN [2]
RP SEQUENCE REVISION.
RA Armengaud J.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for meta-cleavage of the first aromatic ring of
CC 2,2',3-trihydroxybiphenyl and 2,3-dihydroxybiphenyl. 2,2',3-
CC trihydroxydiphenyl ether, catechol, 3-methylcatechol, and 4-
CC methylcatechol are oxidized less efficiently and 3,4-dihydroxybiphenyl
CC is oxidized considerably less efficiently.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC -!- PATHWAY: Xenobiotic degradation; dibenzo-p-dioxin degradation; 2-
CC hydroxymuconate and catechol from dibenzo-p-dioxin: step 2/3.
CC -!- PATHWAY: Xenobiotic degradation; dibenzofuran degradation; 2-hydroxy-
CC 2,4-pentadienoate and salicylate from dibenzofuran: step 2/3.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; X72850; CAA51364.1; -; Genomic_DNA.
DR AlphaFoldDB; P47243; -.
DR SMR; P47243; -.
DR UniPathway; UPA00808; UER00777.
DR UniPathway; UPA00809; UER00780.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019340; P:dibenzofuran catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.180.10; -; 2.
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 PROSITE; PS00082; EXTRADIOL_DIOXYGENAS; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8226678"
FT CHAIN 2..294
FT /note="2,2',3-trihydroxybiphenyl dioxygenase"
FT /id="PRO_0000085041"
FT DOMAIN 7..120
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 144..264
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 209
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 294 AA; 32278 MW; 9315F5B922E1BF8D CRC64;
MSVKQLGYLI FECRADVLEQ MVVVYQDIIG AVVERDEGGR ALVRLDGRPF RIRLDPGPAN
RLAAIGWNVD PSDLAAIAEQ VEKACYSVVT ADAELAADRA AAQVRQFADN DGFTHELYVE
SSFPTDPVLE SLFVCGEEAN GIFGLGHLVV IVADRAKTQS FFTDVLGFGL SDRVTWPEAD
IFFLHCNQRH HTVALSAPAL GLKPGMVHHL MLEAKSKEQV DRAFAAVKRL GYDVLMTIGQ
HSNDKVYSFY MMAPAGFAVE LGFGGQVIGD LESWHVGFYD APSIWGHELQ LPAH
