ID   PHT3_PSEPU              Reviewed;         439 AA.
AC   Q05183;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phthalate 4,5-dioxygenase oxygenase subunit;
DE            EC=1.14.12.7;
GN   Name=pht3;
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=[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: 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 bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000305}.
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DR   EMBL; D13229; BAA02511.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05183; -.
DR   SMR; Q05183; -.
DR   KEGG; ag:BAA02511; -.
DR   UniPathway; UPA00726; UER00728.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR045623; LigXa_C.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   Pfam; PF19301; LigXa_C; 1.
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..439
FT                   /note="Phthalate 4,5-dioxygenase oxygenase subunit"
FT                   /id="PRO_0000085056"
FT   DOMAIN          27..134
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         70
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         72
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         89
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         92
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  49298 MW;  57D14F0D70E8D0DA CRC64;
     MLTPEENLLL CRVEGDAPMG QMMRRHWTPV CLLEEVSEPD GTPVRARLFG EDLVVFRDTD
     GRVGVMDEYC PHRRVSLIYG RNENSGLRCL YHGWKMDVDG NVVEMVSEPA ASNMCQKVKH
     TAYKTREWGG FVWAYMGPQD AIPEFVPPAW APHEHVRVSI AKAIIPCNWA QILEGAIDSA
     HSSSLHSSDF VPARVGGAEA TSKNWLRPST DKAPRMQVER TSYGFRYAAL RRPIQNAATS
     EYVRSTVFVA PATALIPPNN LYNVANINVP IDDTHTAFYF MAWGNPDNTP ETETWRKFLG
     QQVGIDLDDS YRPLRNDGNR FFQDREAMKN GNFTGIKGFP NQDIAMWVTM GPIADRSDER
     LGASDLAVVE FRRVMLDALA AFQAGESAIG TGEKAIPSRI CSFQAIVSKD IDWRDYQARY
     VWALDDANIV AEPDYEVHT