ID   O87803_PSEST            Unreviewed;       341 AA.
AC   O87803;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 2.
DT   19-JAN-2010, entry version 52.
DE   SubName: Full=Oxidoreductase;
GN   Name=touF;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OX1;
RX   MEDLINE=98432776; PubMed=9758777;
RA   Bertoni G., Martino M., Galli E., Barbieri P.;
RT   "Analysis of the gene cluster encoding toluene/o-xylene monooxygenase
RT   from Pseudomonas stutzeri OX1.";
RL   Appl. Environ. Microbiol. 64:3626-3632(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OX1;
RX   MEDLINE=99402750; PubMed=10473416;
RA   Arenghi F.L., Pinti M., Galli E., Barbieri P.;
RT   "Identification of the Pseudomonas stutzeri OX1 toluene-o-xylene
RT   monooxygenase regulatory gene (touR) and of its cognate promoter.";
RL   Appl. Environ. Microbiol. 65:4057-4063(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OX1;
RA   Bertoni G.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type 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; AJ005663; CAA06659.2; -; Genomic_DNA.
DR   SMR; O87803; 2-341.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; b-grasp_ferredoxin-like.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR008333; OxRdtase_FAD-bd_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
SQ   SEQUENCE   341 AA;  38159 MW;  51E4F70583026AA4 CRC64;
     MSNKIKIADT DVEFTISDRD TILRAALRDG IPISYECNSG GCGSCKIDVV EGQVETLWGE
     APGLSPRDKR KSRKLACQCL ASGPVTIKAQ LTDNKLPEIR PFRRRVRYVG RRDLTSDMAE
     FSFQAEEPAL FLPGQYAMLT VPGIEGDRAY SMSNVSNDSG RWQFIIKRMP GGKASNWLFD
     ELKPGGMIEI DGPFGLAYLH PEIQRDVVCI AGGSGLSPVM SIVRAITGDP RLSERKVHLF
     YGGRTPQDLC TSELLSEIEP LNTKAKVISK TAVSDHQSAE KENWEGPCCY IHELAEQTLG
     DHMMEFEYYF CGPPPLTEAV QRMLMIDHKV PFDRIHFDRF F
//