ID   Q51939_BURPI            Unreviewed;       501 AA.
AC   Q51939;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   19-JAN-2010, entry version 49.
DE   SubName: Full=Alpha hydroxylase subunit;
DE   SubName: Full=Toluene-3-monooxygenase oxygenase subunit;
GN   Name=tbuA1;
OS   Burkholderia pickettii (Ralstonia pickettii) (Pseudomonas pickettii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PKO1;
RX   MEDLINE=95172404; PubMed=7867951; DOI=10.1016/0378-1119(94)00844-I;
RA   Byrne A.M., Kukor J.J., Olsen R.H.;
RT   "Sequence analysis of the gene cluster encoding toluene-3-
RT   monooxygenase from Pseudomonas pickettii PKO1.";
RL   Gene 154:65-70(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PKO1;
RA   Byrne A.M., Olsen R.H.;
RT   "Cascade regulation of the toluene-3-monooxygenase operon
RT   (tbuA1UBVA2C) of Burkholderia pickettii PKO1: Role of the tbuA1
RT   promoter (PtbuA1) in the expression of its cognate activator, TbuT.";
RL   J. Bacteriol. 178:0-0(0).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PKO1;
RX   PubMed=15240250; DOI=10.1128/AEM.70.7.3814-3820.2004;
RA   Tao Y., Fishman A., Bentley W.E., Wood T.K.;
RT   "Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene
RT   by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-
RT   monooxygenase of Ralstonia pickettii PKO1.";
RL   Appl. Environ. Microbiol. 70:3814-3820(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PKO1;
RX   PubMed=15126473; DOI=10.1128/JB.186.10.3117-3123.2004;
RA   Fishman A., Tao Y., Wood T.K.;
RT   "Toluene 3-monooxygenase of Ralstonia pickettii PKO1 is a para-
RT   hydroxylating enzyme.";
RL   J. Bacteriol. 186:3117-3123(2004).
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DR   EMBL; U04052; AAB09618.1; -; Genomic_DNA.
DR   EMBL; AY541701; AAS48547.1; -; Genomic_DNA.
DR   SMR; Q51939; 2-492.
DR   BioCyc; MetaCyc:MON-11184; -.
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   4: Predicted;
KW   Monooxygenase.
SQ   SEQUENCE   501 AA;  57555 MW;  D2E2B52C94AD74C2 CRC64;
     MALLERAAWY DIARTTNWTP SYVTESELFP DIMTGAQGVP METWETYDEP YKTSYPEYVS
     IQREKDAGAY SVKAALERSR MFEDADPGWL SILKAHYGAI ALGEYAAMSA EARMARFGRA
     PGMRNMATFG MLDENRHGQL QLYFPHDYCA KDRQFDWAHK AYHTNEWGAI AARSTFDDLF
     MSRSAIDIAI MLTFAFETGF TNMQFLGLAA DAAEAGDFTF ASLISSIQTD ESRHAQIGGP
     ALQILIASGR KEQAQKLVDI AIARAWRLFS LLTGTSMDYA TPLHHRKESF KEFMTEWIVG
     QFERTLIDLG LDLPWYWDQM INEFDYQHHA YQMGIWFWRP TIWWNPAAGI TPDCRDWLEE
     KYPGWNDTFG KAWDVIIDNL LAGKPELTVP ETLPIVCNMS QLPICAVPGN GWIVKDYPLD
     YKGRTYHFNS EIDRWVFQQD PLRYRDHLTL VDRFLAGQIQ PPNLMGALQY MNLAPGECGD
     DAHHYAWVEA YRNQRYQKKA A
//