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Toluene-4-monooxygenase system protein E (T4moE) (EC 1.14.13.-)

 TMOE_PSEME              Reviewed;         327 AA.
Q00460;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 74.
RecName: Full=Toluene-4-monooxygenase system protein E;
Short=T4moE;
EC=1.14.13.-;
Name=tmoE;
Pseudomonas mendocina.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=300;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
STRAIN=KR1;
PubMed=1885512; DOI=10.1128/jb.173.17.5315-5327.1991;
Yen K.-M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B.,
Fausset P.R., Lu H.S., Harcourt A.A., Chen K.K.;
"Cloning and characterization of a Pseudomonas mendocina KR1 gene
cluster encoding toluene-4-monooxygenase.";
J. Bacteriol. 173:5315-5327(1991).
[2]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), AND SUBUNIT.
PubMed=19033467; DOI=10.1073/pnas.0807948105;
Bailey L.J., McCoy J.G., Phillips G.N. Jr., Fox B.G.;
"Structural consequences of effector protein complex formation in a
diiron hydroxylase.";
Proc. Natl. Acad. Sci. U.S.A. 105:19194-19198(2008).
[3]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS), AND SUBUNIT.
PubMed=19290655; DOI=10.1021/bi900144a;
Elsen N.L., Bailey L.J., Hauser A.D., Fox B.G.;
"Role for threonine 201 in the catalytic cycle of the soluble diiron
hydroxylase toluene 4-monooxygenase.";
Biochemistry 48:3838-3846(2009).
[4]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
PubMed=19705873; DOI=10.1021/bi901150a;
Bailey L.J., Fox B.G.;
"Crystallographic and catalytic studies of the peroxide-shunt reaction
in a diiron hydroxylase.";
Biochemistry 48:8932-8939(2009).
-!- FUNCTION: Subunit of the multicomponent enzyme toluene-4-
monooxygenase that hydroxylates toluene to form p-cresol.
-!- PATHWAY: Xenobiotic degradation; toluene degradation.
-!- SUBUNIT: The multicomponent enzyme toluene-4-monooxygenase is
formed by the TmoA, TmoB, TmoC, TmoD, TmoE and TmoF polypeptides.
The heterohexamer formed by two molecules each of TmoA, TmoB and
TmoE interacts with the effector protein TmoD, the Rieske iron-
sulfur protein TmoC and the NADH-containing oxidoreductase TmoF.
{ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655,
ECO:0000269|PubMed:19705873}.
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EMBL; M65106; AAA26003.1; -; Genomic_DNA.
PDB; 3DHG; X-ray; 1.85 A; B/E=1-327.
PDB; 3DHH; X-ray; 1.94 A; B=1-327.
PDB; 3DHI; X-ray; 1.68 A; B=1-327.
PDB; 3GE3; X-ray; 1.52 A; B=1-327.
PDB; 3GE8; X-ray; 2.19 A; B/F=1-327.
PDB; 3I5J; X-ray; 1.90 A; B=1-327.
PDB; 3I63; X-ray; 2.09 A; B=1-327.
PDB; 3Q14; X-ray; 1.75 A; B=1-307.
PDB; 3Q2A; X-ray; 1.99 A; B=1-307.
PDB; 3Q3M; X-ray; 1.75 A; B/F=1-307.
PDB; 3Q3N; X-ray; 1.84 A; B=1-307.
PDB; 3Q3O; X-ray; 1.95 A; B=1-307.
PDB; 3RI7; X-ray; 2.10 A; B=2-306.
PDB; 3RMK; X-ray; 1.95 A; B/E=2-307.
PDB; 4P1B; X-ray; 2.05 A; B/E=2-306.
PDB; 4P1C; X-ray; 2.40 A; B/E=2-306.
PDB; 5TDS; X-ray; 1.72 A; B/E=1-327.
PDB; 5TDT; X-ray; 1.82 A; B/F=1-307.
PDB; 5TDU; X-ray; 1.74 A; B=1-308.
PDB; 5TDV; X-ray; 2.00 A; B/F=1-327.
PDBsum; 3DHG; -.
PDBsum; 3DHH; -.
PDBsum; 3DHI; -.
PDBsum; 3GE3; -.
PDBsum; 3GE8; -.
PDBsum; 3I5J; -.
PDBsum; 3I63; -.
PDBsum; 3Q14; -.
PDBsum; 3Q2A; -.
PDBsum; 3Q3M; -.
PDBsum; 3Q3N; -.
PDBsum; 3Q3O; -.
PDBsum; 3RI7; -.
PDBsum; 3RMK; -.
PDBsum; 4P1B; -.
PDBsum; 4P1C; -.
PDBsum; 5TDS; -.
PDBsum; 5TDT; -.
PDBsum; 5TDU; -.
PDBsum; 5TDV; -.
ProteinModelPortal; Q00460; -.
SMR; Q00460; -.
DIP; DIP-48647N; -.
IntAct; Q00460; 1.
UniPathway; UPA00273; -.
EvolutionaryTrace; Q00460; -.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
CDD; cd01058; AAMH_B; 1.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR012078; MP_mOase_hydro.
InterPro; IPR003430; Phenol_Hydrox.
Pfam; PF02332; Phenol_Hydrox; 1.
PIRSF; PIRSF000040; MMOH_comp; 1.
SUPFAM; SSF47240; SSF47240; 1.
1: Evidence at protein level;
3D-structure; Aromatic hydrocarbons catabolism;
Direct protein sequencing; Monooxygenase; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1885512}.
CHAIN 2 327 Toluene-4-monooxygenase system protein E.
/FTId=PRO_0000072603.
TURN 13 17 {ECO:0000244|PDB:3GE3}.
STRAND 18 20 {ECO:0000244|PDB:3I63}.
HELIX 24 29 {ECO:0000244|PDB:3GE3}.
HELIX 34 36 {ECO:0000244|PDB:3GE3}.
STRAND 42 45 {ECO:0000244|PDB:3GE3}.
HELIX 50 58 {ECO:0000244|PDB:3GE3}.
TURN 59 61 {ECO:0000244|PDB:3GE3}.
HELIX 69 71 {ECO:0000244|PDB:3GE3}.
HELIX 80 103 {ECO:0000244|PDB:3GE3}.
HELIX 106 109 {ECO:0000244|PDB:3GE3}.
HELIX 114 121 {ECO:0000244|PDB:3GE3}.
TURN 122 124 {ECO:0000244|PDB:3GE3}.
HELIX 125 142 {ECO:0000244|PDB:3GE3}.
HELIX 146 176 {ECO:0000244|PDB:3GE3}.
TURN 182 184 {ECO:0000244|PDB:3GE3}.
HELIX 186 192 {ECO:0000244|PDB:3GE3}.
HELIX 194 206 {ECO:0000244|PDB:3GE3}.
HELIX 212 221 {ECO:0000244|PDB:3GE3}.
HELIX 223 230 {ECO:0000244|PDB:3GE3}.
HELIX 232 241 {ECO:0000244|PDB:3GE3}.
HELIX 246 272 {ECO:0000244|PDB:3GE3}.
HELIX 278 305 {ECO:0000244|PDB:3GE3}.
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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