TMOB_PSEME
ID TMOB_PSEME Reviewed; 84 AA.
AC Q00457; Q6Q8Q6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Toluene-4-monooxygenase system, hydroxylase component subunit gamma {ECO:0000303|PubMed:15240250};
DE Short=T4MO {ECO:0000303|PubMed:1885512};
DE EC=1.14.13.236 {ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873, ECO:0000305|PubMed:2019563};
DE AltName: Full=Toluene-4-monooxygenase hydroxylase subunit {ECO:0000303|PubMed:1885512};
DE Short=T4moH {ECO:0000303|PubMed:1885512};
DE AltName: Full=Toluene-4-monooxygenase system protein B {ECO:0000303|PubMed:1885512};
DE Short=T4moB {ECO:0000303|PubMed:1885512};
GN Name=tmoB {ECO:0000303|PubMed:1885512};
OS Pseudomonas mendocina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=KR1;
RX PubMed=1885512; DOI=10.1128/jb.173.17.5315-5327.1991;
RA Yen K.-M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B., Fausset P.R.,
RA Lu H.S., Harcourt A.A., Chen K.K.;
RT "Cloning and characterization of a Pseudomonas mendocina KR1 gene cluster
RT encoding toluene-4-monooxygenase.";
RL J. Bacteriol. 173:5315-5327(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=KR1 {ECO:0000312|EMBL:AAS66661.1};
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 by
RT 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=KR1;
RX PubMed=2019563; DOI=10.1128/jb.173.9.3010-3016.1991;
RA Whited G.M., Gibson D.T.;
RT "Toluene-4-monooxygenase, a three-component enzyme system that catalyzes
RT the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1.";
RL J. Bacteriol. 173:3010-3016(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), AND SUBUNIT.
RX PubMed=19033467; DOI=10.1073/pnas.0807948105;
RA Bailey L.J., McCoy J.G., Phillips G.N. Jr., Fox B.G.;
RT "Structural consequences of effector protein complex formation in a diiron
RT hydroxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19194-19198(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=19290655; DOI=10.1021/bi900144a;
RA Elsen N.L., Bailey L.J., Hauser A.D., Fox B.G.;
RT "Role for threonine 201 in the catalytic cycle of the soluble diiron
RT hydroxylase toluene 4-monooxygenase.";
RL Biochemistry 48:3838-3846(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=19705873; DOI=10.1021/bi901150a;
RA Bailey L.J., Fox B.G.;
RT "Crystallographic and catalytic studies of the peroxide-shunt reaction in a
RT diiron hydroxylase.";
RL Biochemistry 48:8932-8939(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RC STRAIN=KR1;
RX PubMed=22264099; DOI=10.1021/bi2018333;
RA Bailey L.J., Acheson J.F., McCoy J.G., Elsen N.L., Phillips G.N. Jr.,
RA Fox B.G.;
RT "Crystallographic analysis of active site contributions to regiospecificity
RT in the diiron enzyme toluene 4-monooxygenase.";
RL Biochemistry 51:1101-1113(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-83, AND SUBUNIT.
RX PubMed=25248368; DOI=10.1038/ncomms6009;
RA Acheson J.F., Bailey L.J., Elsen N.L., Fox B.G.;
RT "Structural basis for biomolecular recognition in overlapping binding sites
RT in a diiron enzyme system.";
RL Nat. Commun. 5:5009-5009(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), AND SUBUNIT.
RX PubMed=28346937; DOI=10.1038/nature21681;
RA Acheson J.F., Bailey L.J., Brunold T.C., Fox B.G.;
RT "In-crystal reaction cycle of a toluene-bound diiron hydroxylase.";
RL Nature 544:191-195(2017).
CC -!- FUNCTION: Component of the toluene-4-monooxygenase multicomponent
CC enzyme system which catalyzes the O2- and NADH-dependent hydroxylation
CC of toluene to form p-cresol (PubMed:1885512, PubMed:15240250,
CC PubMed:2019563, PubMed:19290655, PubMed:19705873). Also able to convert
CC benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive
CC hydroxylations (PubMed:15240250). {ECO:0000269|PubMed:15240250,
CC ECO:0000269|PubMed:1885512, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:2019563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + toluene = 4-methylphenol + H2O + NAD(+);
CC Xref=Rhea:RHEA:41380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17578, ChEBI:CHEBI:17847,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.236;
CC Evidence={ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000305|PubMed:2019563};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+).
CC {ECO:0000269|PubMed:2019563}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:2019563};
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC {ECO:0000305|PubMed:15240250}.
CC -!- SUBUNIT: The alkene monooxygenase multicomponent enzyme system is
CC composed of an electron transfer component and a monooxygenase
CC component interacting with the effector protein TmoD. The electron
CC transfer component is composed of a ferredoxin reductase (TmoF) and a
CC ferredoxin (TmoC), and the monooxygenase component is formed by a
CC heterohexamer (dimer of heterotrimers) of two alpha subunits (TmoA),
CC two beta subunits (TmoE) and two gamma subunits (TmoB).
CC {ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:22264099,
CC ECO:0000269|PubMed:25248368, ECO:0000269|PubMed:28346937}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a complete loss of
CC toluene-4-monooxygenase activity. {ECO:0000269|PubMed:1885512}.
CC -!- SIMILARITY: Belongs to the TmoB/XamoB family. {ECO:0000305}.
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DR EMBL; M65106; AAA26000.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66661.1; -; Genomic_DNA.
DR PDB; 3DHG; X-ray; 1.85 A; C/F=1-84.
DR PDB; 3DHH; X-ray; 1.94 A; C=1-84.
DR PDB; 3DHI; X-ray; 1.68 A; C=1-84.
DR PDB; 3GE3; X-ray; 1.52 A; C=1-84.
DR PDB; 3GE8; X-ray; 2.19 A; C/G=1-84.
DR PDB; 3I5J; X-ray; 1.90 A; C=1-84.
DR PDB; 3I63; X-ray; 2.09 A; C=1-84.
DR PDB; 3Q14; X-ray; 1.75 A; C=1-84.
DR PDB; 3Q2A; X-ray; 1.99 A; C=1-84.
DR PDB; 3Q3M; X-ray; 1.75 A; C/G=1-84.
DR PDB; 3Q3N; X-ray; 1.84 A; C=1-84.
DR PDB; 3Q3O; X-ray; 1.95 A; C=1-84.
DR PDB; 3RI7; X-ray; 2.10 A; C=2-84.
DR PDB; 3RMK; X-ray; 1.95 A; C/F=2-84.
DR PDB; 4P1B; X-ray; 2.05 A; C/F=2-83.
DR PDB; 4P1C; X-ray; 2.40 A; C/F=2-83.
DR PDB; 5TDS; X-ray; 1.72 A; C/F=1-84.
DR PDB; 5TDT; X-ray; 1.82 A; C/G=1-84.
DR PDB; 5TDU; X-ray; 1.74 A; C=1-84.
DR PDB; 5TDV; X-ray; 2.00 A; C/G=1-84.
DR PDBsum; 3DHG; -.
DR PDBsum; 3DHH; -.
DR PDBsum; 3DHI; -.
DR PDBsum; 3GE3; -.
DR PDBsum; 3GE8; -.
DR PDBsum; 3I5J; -.
DR PDBsum; 3I63; -.
DR PDBsum; 3Q14; -.
DR PDBsum; 3Q2A; -.
DR PDBsum; 3Q3M; -.
DR PDBsum; 3Q3N; -.
DR PDBsum; 3Q3O; -.
DR PDBsum; 3RI7; -.
DR PDBsum; 3RMK; -.
DR PDBsum; 4P1B; -.
DR PDBsum; 4P1C; -.
DR PDBsum; 5TDS; -.
DR PDBsum; 5TDT; -.
DR PDBsum; 5TDU; -.
DR PDBsum; 5TDV; -.
DR AlphaFoldDB; Q00457; -.
DR SMR; Q00457; -.
DR DIP; DIP-48645N; -.
DR IntAct; Q00457; 1.
DR KEGG; ag:AAA26000; -.
DR BioCyc; MetaCyc:MON-2507; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; Q00457; -.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.20.270; -; 1.
DR InterPro; IPR036713; TmoB-like_sf.
DR InterPro; IPR009355; Toluene_mOase_B.
DR Pfam; PF06234; TmoB; 1.
DR SUPFAM; SSF110814; SSF110814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Monooxygenase; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1885512"
FT CHAIN 2..84
FT /note="Toluene-4-monooxygenase system, hydroxylase
FT component subunit gamma"
FT /id="PRO_0000072600"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3Q2A"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3GE3"
SQ SEQUENCE 84 AA; 9588 MW; 9EB4FE89F0A7218B CRC64;
MSAFPVHAAF EKDFLVQLVV VDLNDSMDQV AEKVAYHCVN RRVAPREGVM RVRKHRSTEL
FPRDMTIAES GLNPTEVIDV VFEE
