ID   POBB_PSEOL              Reviewed;         319 AA.
AC   Q52186;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phenoxybenzoate dioxygenase subunit beta;
DE            EC=1.-.-.-;
DE   AltName: Full=4-carboxydiphenyl ether;phenoxybenzoate dioxygenase subunit beta;
GN   Name=pobB;
OS   Pseudomonas oleovorans.
OG   Plasmid pPOB.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=POB310;
RX   PubMed=7710319; DOI=10.1007/bf00262201;
RA   Dehmel U., Engesser K.-H., Timmis K.N., Dwyer D.F.;
RT   "Cloning, nucleotide sequence, and expression of the gene encoding a novel
RT   dioxygenase involved in metabolism of carboxydiphenyl ethers in Pseudomonas
RT   pseudoalcaligenes POB310.";
RL   Arch. Microbiol. 163:35-41(1995).
CC   -!- FUNCTION: Degrades exclusively diarylether compounds having carboxyl
CC       groups in the 3- or 4-position. Yields a hemiacetal that spontaneously
CC       hydrolyzes to phenol and protocatechuate.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; carboxydiphenyl ether
CC       degradation.
CC   -!- SUBUNIT: This dioxygenase system consists of two proteins: the alpha
CC       subunit (PobA) and a subunit (PobB) that acts as a ferredoxin and a
CC       ferredoxin reductase.
CC   -!- INDUCTION: By 3- or 4-carboxydiphenyl ether and by phenol.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR   EMBL; X78823; CAA55401.1; -; Genomic_DNA.
DR   PIR; S44172; S44172.
DR   AlphaFoldDB; Q52186; -.
DR   SMR; Q52186; -.
DR   UniPathway; UPA00730; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid;
KW   Transport.
FT   CHAIN           1..319
FT                   /note="Phenoxybenzoate dioxygenase subunit beta"
FT                   /id="PRO_0000189399"
FT   DOMAIN          7..109
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          234..319
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         113..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         273
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         276
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         306
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   319 AA;  33591 MW;  14CDB6B17D6CF606 CRC64;
     MSAAATMAPV SLRIHAIAYG ADDVLLFDLR APARDGLAPF DAGAHIDLRL PRGITRSYSL
     LNDPAERHRY VIGVKREPES RGGSAWLHAD ARVGALIEVD GPSNHFALDE SAPHAVFIAG
     GIGITPLWSM VQRLEHLGTP WTLHYRARSR RGAALLDELA GHGDRVHLSF SDEGAPSLDL
     AAIVAAAPEG AHFYCCGPVP MLEAFEAACV GLDPARVHLE YFAAKEAPAT EGGFVVHLAR
     SGRTIPIAAG CTILDALQAG GVAVPSSCQQ GVCGICETAV LAGVPDHRDL VLSDQERAAG
     RTMMICCSGS KTAELTLDL