POBA_PSEOL
ID POBA_PSEOL Reviewed; 409 AA.
AC Q52185;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Phenoxybenzoate dioxygenase subunit alpha;
DE EC=1.14.12.-;
DE AltName: Full=4-carboxydiphenyl ether;phenoxybenzoate dioxygenase;
GN Name=pobA;
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC Note=Binds 1 Fe cation. {ECO:0000305};
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 bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; X78823; CAA55400.1; -; Genomic_DNA.
DR PIR; S44171; S44171.
DR AlphaFoldDB; Q52185; -.
DR SMR; Q52185; -.
DR UniPathway; UPA00730; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..409
FT /note="Phenoxybenzoate dioxygenase subunit alpha"
FT /id="PRO_0000085057"
FT DOMAIN 45..149
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 46259 MW; 721B634A8FA7FD2F CRC64;
MSKTIPIVDA QHAGSAYQHV PGHPDPQLSA VAKGTPTGEY LRRYWQPVAL SADVTDRPQM
VRILGEDLVL FRDKAGRPGL LYPRCMHRGT SLYYGHVEEA GIRCCYHGWL FAVDGTCLNQ
PCEPEGGLRR EAARQPWYPV EERYGLVFAY MGPPEKKPVL PRYDILEDLE EGEFIEVISG
GFVSYADHVE DPNVPYHWLQ NWENIMDPYH VYILHSTFSG IQFAENFKIL PRVDFEAVDG
GVIYHAWRDL EDGRQLERIN SALFPNISAI PMIDLSPGQG RWIGWHVAVD DQHYRGFFAA
RTRQPGNFAP IKMHNGKSWT ELSEQEKQDF PGDFEAQFGQ GRVTLHGEEH LATSDHGIAL
LRRQMKQQIA IVQQGGDPAG VHFNEADALV RIRSGNFYTT SDKTETAAD