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Toluene-4-monooxygenase system, hydroxylase component subunit gamma (T4MO) (EC 1.14.13.236) (Toluene-4-monooxygenase hydroxylase subunit) (T4moH) (Toluene-4-monooxygenase system protein B) (T4moB)

 TMOB_PSEME              Reviewed;          84 AA.
Q00457; Q6Q8Q6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-FEB-2018, entry version 67.
RecName: Full=Toluene-4-monooxygenase system, hydroxylase component subunit gamma {ECO:0000303|PubMed:15240250};
Short=T4MO {ECO:0000303|PubMed:1885512};
EC=1.14.13.236 {ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873, ECO:0000305|PubMed:2019563};
AltName: Full=Toluene-4-monooxygenase hydroxylase subunit {ECO:0000303|PubMed:1885512};
Short=T4moH {ECO:0000303|PubMed:1885512};
AltName: Full=Toluene-4-monooxygenase system protein B {ECO:0000303|PubMed:1885512};
Short=T4moB {ECO:0000303|PubMed:1885512};
Name=tmoB {ECO:0000303|PubMed:1885512};
Pseudomonas mendocina.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=300;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28, FUNCTION,
AND DISRUPTION PHENOTYPE.
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, AND PATHWAY.
STRAIN=KR1 {ECO:0000312|EMBL:AAS66661.1};
PubMed=15240250; DOI=10.1128/AEM.70.7.3814-3820.2004;
Tao Y., Fishman A., Bentley W.E., Wood T.K.;
"Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene
by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-
monooxygenase of Ralstonia pickettii PKO1.";
Appl. Environ. Microbiol. 70:3814-3820(2004).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
ENZYME REGULATION.
STRAIN=KR1;
PubMed=2019563;
Whited G.M., Gibson D.T.;
"Toluene-4-monooxygenase, a three-component enzyme system that
catalyzes the oxidation of toluene to p-cresol in Pseudomonas
mendocina KR1.";
J. Bacteriol. 173:3010-3016(1991).
[4]
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).
[5]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
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).
[6]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
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).
[7]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
STRAIN=KR1;
PubMed=22264099; DOI=10.1021/bi2018333;
Bailey L.J., Acheson J.F., McCoy J.G., Elsen N.L., Phillips G.N. Jr.,
Fox B.G.;
"Crystallographic analysis of active site contributions to
regiospecificity in the diiron enzyme toluene 4-monooxygenase.";
Biochemistry 51:1101-1113(2012).
[8]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-83, AND SUBUNIT.
PubMed=25248368; DOI=10.1038/ncomms6009;
Acheson J.F., Bailey L.J., Elsen N.L., Fox B.G.;
"Structural basis for biomolecular recognition in overlapping binding
sites in a diiron enzyme system.";
Nat. Commun. 5:5009-5009(2014).
[9]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), AND SUBUNIT.
PubMed=28346937; DOI=10.1038/nature21681;
Acheson J.F., Bailey L.J., Brunold T.C., Fox B.G.;
"In-crystal reaction cycle of a toluene-bound diiron hydroxylase.";
Nature 544:191-195(2017).
-!- FUNCTION: Component of the toluene-4-monooxygenase multicomponent
enzyme system which catalyzes the O2- and NADH-dependent
hydroxylation of toluene to form p-cresol (PubMed:1885512,
PubMed:15240250, PubMed:2019563, PubMed:19290655,
PubMed:19705873). Also able to convert benzene to phenol,
catechol, and 1,2,3-trihydroxybenzene by successive hydroxylations
(PubMed:15240250). {ECO:0000269|PubMed:15240250,
ECO:0000269|PubMed:1885512, ECO:0000269|PubMed:19290655,
ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:2019563}.
-!- CATALYTIC ACTIVITY: Toluene + NADH + O(2) = 4-methylphenol +
NAD(+) + H(2)O. {ECO:0000269|PubMed:15240250,
ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
ECO:0000305|PubMed:2019563}.
-!- ENZYME REGULATION: Inhibited by Zn(2+) and Cu(2+).
{ECO:0000269|PubMed:2019563}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.8. {ECO:0000269|PubMed:2019563};
-!- PATHWAY: Xenobiotic degradation; toluene degradation.
{ECO:0000305|PubMed:15240250}.
-!- SUBUNIT: The alkene monooxygenase multicomponent enzyme system is
composed of an electron transfer component and a monooxygenase
component interacting with the effector protein TmoD. The electron
transfer component is composed of a ferredoxin reductase (TmoF)
and a ferredoxin (TmoC), and the monooxygenase component is formed
by a heterohexamer (dimer of heterotrimers) of two alpha subunits
(TmoA), two beta subunits (TmoE) and two gamma subunits (TmoB).
{ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655,
ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:22264099,
ECO:0000269|PubMed:25248368, ECO:0000269|PubMed:28346937}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show a complete loss
of toluene-4-monooxygenase activity. {ECO:0000269|PubMed:1885512}.
-!- SIMILARITY: Belongs to the TmoB/XamoB family. {ECO:0000305}.
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EMBL; M65106; AAA26000.1; -; Genomic_DNA.
EMBL; AY552601; AAS66661.1; -; Genomic_DNA.
PDB; 3DHG; X-ray; 1.85 A; C/F=1-84.
PDB; 3DHH; X-ray; 1.94 A; C=1-84.
PDB; 3DHI; X-ray; 1.68 A; C=1-84.
PDB; 3GE3; X-ray; 1.52 A; C=1-84.
PDB; 3GE8; X-ray; 2.19 A; C/G=1-84.
PDB; 3I5J; X-ray; 1.90 A; C=1-84.
PDB; 3I63; X-ray; 2.09 A; C=1-84.
PDB; 3Q14; X-ray; 1.75 A; C=1-84.
PDB; 3Q2A; X-ray; 1.99 A; C=1-84.
PDB; 3Q3M; X-ray; 1.75 A; C/G=1-84.
PDB; 3Q3N; X-ray; 1.84 A; C=1-84.
PDB; 3Q3O; X-ray; 1.95 A; C=1-84.
PDB; 3RI7; X-ray; 2.10 A; C=2-84.
PDB; 3RMK; X-ray; 1.95 A; C/F=2-84.
PDB; 4P1B; X-ray; 2.05 A; C/F=2-83.
PDB; 4P1C; X-ray; 2.40 A; C/F=2-83.
PDB; 5TDS; X-ray; 1.72 A; C/F=1-84.
PDB; 5TDT; X-ray; 1.82 A; C/G=1-84.
PDB; 5TDU; X-ray; 1.74 A; C=1-84.
PDB; 5TDV; X-ray; 2.00 A; C/G=1-84.
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; Q00457; -.
SMR; Q00457; -.
DIP; DIP-48645N; -.
IntAct; Q00457; 1.
BioCyc; MetaCyc:MONOMER-2507; -.
UniPathway; UPA00273; -.
EvolutionaryTrace; Q00457; -.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.10.20.270; -; 1.
InterPro; IPR036713; TmoB-like_sf.
InterPro; IPR009355; Toluene_mOase_B.
Pfam; PF06234; TmoB; 1.
SUPFAM; SSF110814; SSF110814; 1.
1: Evidence at protein level;
3D-structure; Aromatic hydrocarbons catabolism;
Direct protein sequencing; Monooxygenase; NAD; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1885512}.
CHAIN 2 84 Toluene-4-monooxygenase system,
hydroxylase component subunit gamma.
/FTId=PRO_0000072600.
STRAND 3 10 {ECO:0000244|PDB:3GE3}.
STRAND 14 22 {ECO:0000244|PDB:3GE3}.
HELIX 27 36 {ECO:0000244|PDB:3GE3}.
TURN 37 41 {ECO:0000244|PDB:3GE3}.
STRAND 50 54 {ECO:0000244|PDB:3GE3}.
STRAND 58 60 {ECO:0000244|PDB:3Q2A}.
HELIX 67 70 {ECO:0000244|PDB:3GE3}.
STRAND 77 82 {ECO:0000244|PDB:3GE3}.
SEQUENCE 84 AA; 9588 MW; 9EB4FE89F0A7218B CRC64;
MSAFPVHAAF EKDFLVQLVV VDLNDSMDQV AEKVAYHCVN RRVAPREGVM RVRKHRSTEL
FPRDMTIAES GLNPTEVIDV VFEE


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