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   16-JUN-2009, entry version 49.
DE   RecName: Full=Phthalate 4,5-dioxygenase oxygenase subunit;
DE            EC=1.14.12.7;
GN   Name=pht3;
OS   Pseudomonas putida.
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
RT   phthalate in Pseudomonas putida.";
RL   J. Ferment. Bioeng. 74:333-344(1992).
CC   -!- CATALYTIC ACTIVITY: Phthalate + NADH + O(2) = cis-4,5-
CC       dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster (Probable).
CC   -!- COFACTOR: Binds 1 iron ion (Probable).
CC   -!- PATHWAY: Xenobiotic degradation; phtalic acid degradation; 3,4-
CC       dihydroxybenzoate from phtalic acid: step 1/3.
CC   -!- SUBUNIT: This dioxygenase system consists of two proteins:
CC       phthalate oxygenase and phthalate oxygenase reductase.
CC   -!- INDUCTION: Induced by phthalate and repressed by glucose.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
CC       dioxygenase alpha subunit family.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D13229; BAA02511.1; -; Genomic_DNA.
DR   BRENDA; 1.14.12.7; 403.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0018620; F:phthalate 4,5-dioxygenase activity; IEA:EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   Pfam; PF00355; Rieske; 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;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT   CHAIN         1    439       Phthalate 4,5-dioxygenase oxygenase
FT                                subunit.
FT                                /FTId=PRO_0000085056.
FT   DOMAIN       27    134       Rieske.
FT   METAL        70     70       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        72     72       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL        89     89       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        92     92       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       181    181       Iron (By similarity).
FT   METAL       186    186       Iron (By similarity).
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
//