ID   O87798_PSEST            Unreviewed;       498 AA.
AC   O87798;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   03-NOV-2009, entry version 45.
DE   SubName: Full=Toluene, o-xylene monooxygenase oxygenase subunit;
GN   Name=touA;
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.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX   PubMed=15096510; DOI=10.1074/jbc.M400710200;
RA   Sazinsky M.H., Bard J., Di Donato A., Lippard S.J.;
RT   "Crystal structure of the toluene/o-xylene monooxygenase hydroxylase
RT   from Pseudomonas stutzeri OX1. Insight into the substrate specificity,
RT   substrate channeling, and active site tuning of multicomponent
RT   monooxygenases.";
RL   J. Biol. Chem. 279:30600-30610(2004).
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DR   EMBL; AJ005663; CAA06654.1; -; Genomic_DNA.
DR   PDB; 1T0Q; X-ray; 2.15 A; A=1-498.
DR   PDB; 1T0R; X-ray; 2.30 A; A=1-498.
DR   PDB; 1T0S; X-ray; 2.20 A; A=1-498.
DR   PDB; 2INC; X-ray; 1.85 A; A=2-492.
DR   PDB; 2IND; X-ray; 2.20 A; A=2-492.
DR   PDB; 2RDB; X-ray; 2.10 A; A=1-498.
DR   PDBsum; 2INC; -.
DR   PDBsum; 2IND; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR009078; Ferritin/RR-like.
DR   InterPro; IPR003430; Phenol_Hydrox.
DR   InterPro; IPR012348; Ribncl_red_rel.
DR   InterPro; IPR007029; YHS.
DR   Gene3D; G3DSA:1.10.620.20; Ribncl_red_rel; 1.
DR   Pfam; PF02332; Phenol_Hydrox; 1.
DR   Pfam; PF04945; YHS; 1.
PE   1: Evidence at protein level;
KW   Monooxygenase.
SQ   SEQUENCE   498 AA;  57725 MW;  E49B0C06D5BB43D8 CRC64;
     MSMLKREDWY DLTRTTNWTP KYVTENELFP EEMSGARGIS MEAWEKYDEP YKITYPEYVS
     IQREKDSGAY SIKAALERDG FVDRADPGWV STMQLHFGAI ALEEYAASTA EARMARFAKA
     PGNRNMATFG MMDENRHGQI QLYFPYANVK RSRKWDWAHK AIHTNEWAAI AARSFFDDMM
     MTRDSVAVSI MLTFAFETGF TNMQFLGLAA DAAEAGDHTF ASLISSIQTD ESRHAQQGGP
     SLKILVENGK KDEAQQMVDV AIWRSWKLFS VLTGPIMDYY TPLESRNQSF KEFMLEWIVA
     QFERQLLDLG LDKPWYWDQF MQDLDETHHG MHLGVWYWRP TVWWDPAAGV SPEEREWLEE
     KYPGWNDTWG QCWDVITDNL VNGKPELTVP ETLPTICNMC NLPIAHTPGN KWNVKDYQLE
     YEGRLYHFGS EADRWCFQID PERYKNHTNL VDRFLKGEIQ PADLAGALMY MSLEPGVMGD
     DAHDYEWVKA YQKKTNAA
//