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Database: SPTrEMBL
Entry: TMOE_PSEME
LinkDB: TMOE_PSEME
Original site: TMOE_PSEME 
ID   TMOE_PSEME              Reviewed;         327 AA.
AC   Q00460;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-NOV-2009, entry version 45.
DE   RecName: Full=Toluene-4-monooxygenase system protein E;
DE            EC=1.14.13.-;
GN   Name=tmoE;
OS   Pseudomonas mendocina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RC   STRAIN=KR1;
RX   MEDLINE=91358306; PubMed=1885512;
RA   Yen K.-M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B.,
RA   Fausset P.R., Lu H.S., Harcourt A.A., Chen K.K.;
RT   "Cloning and characterization of a Pseudomonas mendocina KR1 gene
RT   cluster encoding toluene-4-monooxygenase.";
RL   J. Bacteriol. 173:5315-5327(1991).
CC   -!- FUNCTION: Hydroxylates toluene to form p-cresol.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: Fe(2+).
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- SUBUNIT: The multicomponent enzyme toluene-4-monooxygenase is
CC       formed by the tmoA, tmoB, tmoC, tmoD, tmoE and tmoF polypeptides.
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DR   EMBL; M65106; AAA26003.1; -; Genomic_DNA.
DR   PDB; 3DHG; X-ray; 1.85 A; B/E=1-327.
DR   PDB; 3DHH; X-ray; 1.94 A; B=1-327.
DR   PDB; 3DHI; X-ray; 1.68 A; B=1-327.
DR   PDB; 3GE3; X-ray; 1.52 A; B=1-327.
DR   PDB; 3GE8; X-ray; 2.19 A; B/F=1-327.
DR   PDB; 3I5J; X-ray; 1.90 A; B=1-327.
DR   PDB; 3I63; X-ray; 2.09 A; B=1-327.
DR   PDBsum; 3DHG; -.
DR   PDBsum; 3DHH; -.
DR   PDBsum; 3DHI; -.
DR   PDBsum; 3GE3; -.
DR   PDBsum; 3GE8; -.
DR   PDBsum; 3I5J; -.
DR   PDBsum; 3I63; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired d...; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR009078; Ferritin/RR-like.
DR   InterPro; IPR012078; MP_mOase_hydro.
DR   InterPro; IPR003430; Phenol_Hydrox.
DR   InterPro; IPR012348; Ribncl_red_rel.
DR   Gene3D; G3DSA:1.10.620.20; Ribncl_red_rel; 1.
DR   Pfam; PF02332; Phenol_Hydrox; 1.
DR   PIRSF; PIRSF000040; MMOH_comp; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism;
KW   Direct protein sequencing; FAD; Flavoprotein; Iron; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    327       Toluene-4-monooxygenase system protein E.
FT                                /FTId=PRO_0000072603.
FT   TURN         13     17
FT   HELIX        24     29
FT   HELIX        34     36
FT   STRAND       42     45
FT   HELIX        50     58
FT   TURN         59     61
FT   HELIX        69     71
FT   HELIX        80     87
FT   HELIX        91    103
FT   HELIX       106    109
FT   HELIX       115    121
FT   TURN        122    124
FT   HELIX       125    142
FT   HELIX       146    176
FT   HELIX       186    192
FT   HELIX       200    206
FT   HELIX       215    220
FT   HELIX       223    230
FT   HELIX       232    241
FT   HELIX       246    272
FT   HELIX       278    282
FT   HELIX       286    305
SQ   SEQUENCE   327 AA;  38386 MW;  65C53BDFF57E040D CRC64;
     MSFESKKPMR TWSHLAEMRK KPSEYDIVSR KLHYSTNNPD SPWELSPDSP MNLWYKQYRN
     ASPLKHDNWD AFTDPDQLVY RTYNLMQDGQ ESYVQSLFDQ FNEREHDQMV REGWEHTMAR
     CYSPLRYLFH CLQMSSAYVQ QMAPASTISN CCILQTADSL RWLTHTAYRT HELSLTYPDA
     GLGEHERELW EKEPGWQGLR ELMEKQLTAF DWGEAFVSLN LVVKPMIVES IFKPLQQQAW
     ENNDTLLPLL IDSQLKDAER HSRWSKALVK HALENPDNHA VIEGWIEKWR PLADRAAEAY
     LSMLSSDILH AQYLERSTSL RASILTV
//
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