ID   PHT2_PSEPU              Reviewed;         324 AA.
AC   Q05182;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phthalate 4,5-dioxygenase oxygenase reductase subunit;
DE            EC=1.14.12.7;
GN   Name=pht2;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid PHT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NMH102-2;
RA   Nomura Y., Nakagawa M., Ogawa N., Harashima S., Oshima Y.;
RT   "Genes in PHT plasmid encoding the initial degradation pathway of phthalate
RT   in Pseudomonas putida.";
RL   J. Ferment. Bioeng. 74:333-344(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + phthalate = cis-4,5-dihydroxycyclohexa-2,6-
CC         diene-1,2-dicarboxylate + NAD(+); Xref=Rhea:RHEA:17489,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17563,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58237;
CC         EC=1.14.12.7;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- PATHWAY: Xenobiotic degradation; phthalate degradation; 3,4-
CC       dihydroxybenzoate from phthalate: step 1/3.
CC   -!- SUBUNIT: This dioxygenase system consists of two proteins: phthalate
CC       oxygenase and phthalate oxygenase reductase.
CC   -!- INDUCTION: Induced by phthalate and repressed by glucose.
CC   -!- SIMILARITY: Belongs to the PDR/VanB family. {ECO:0000305}.
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DR   EMBL; D13229; BAA02510.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05182; -.
DR   SMR; Q05182; -.
DR   KEGG; ag:BAA02510; -.
DR   UniPathway; UPA00726; UER00728.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0018620; F:phthalate 4,5-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046239; P:phthalate catabolic process; IEA:UniProtKB-UniPathway.
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; IPR001433; OxRdtase_FAD/NAD-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   Pfam; PF00175; NAD_binding_1; 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; Monooxygenase; NAD; Oxidoreductase;
KW   Plasmid; Transport.
FT   CHAIN           1..324
FT                   /note="Phthalate 4,5-dioxygenase oxygenase reductase
FT                   subunit"
FT                   /id="PRO_0000189400"
FT   DOMAIN          9..111
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   DOMAIN          241..324
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         115..229
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         280
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         283
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         311
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   324 AA;  36000 MW;  2D211236644E1956 CRC64;
     MSSSEQLDDG FTGLKVIAKT EIAQGIFRFE LAHPQGMLLP AFTAGAHLRV RVPNGSIRNY
     SLSNDPQERE RYVIAVKRDA NGRGGSVSMA DDIEAGDLLP VATPQNEFEL IENARQFIFV
     AGGIGITPIL SMMRHLKAST DLPFKLYYCT RNPELTAFRD ELLGAEFANT VVIHHDFGNR
     ADAYDFWPVF DKPSSGTHVY CCGPRPLMDS VLDMTGHWPP GSIHFESFGV DQSRFAENRP
     FSVTLGRSGI DLEIPVDRSI LEVLRDNGIR APSSCESGTC GSCRTRLIEG DVEHRDMVLR
     EDEQHDQIMI CVSRARNDVL VLDL