TMOE_PSEME
ID TMOE_PSEME Reviewed; 327 AA.
AC Q00460; Q6Q8Q3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Toluene-4-monooxygenase system, hydroxylase component subunit beta {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 E {ECO:0000303|PubMed:1885512};
DE Short=T4moE {ECO:0000303|PubMed:1885512};
GN Name=tmoE {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 2-15, 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:AAS66664.1};
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) OF 1-307, 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 2-306, 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 TmoE/XamoE family. {ECO:0000305}.
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DR EMBL; M65106; AAA26003.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66664.1; -; 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 PDB; 3Q14; X-ray; 1.75 A; B=1-307.
DR PDB; 3Q2A; X-ray; 1.99 A; B=1-307.
DR PDB; 3Q3M; X-ray; 1.75 A; B/F=1-307.
DR PDB; 3Q3N; X-ray; 1.84 A; B=1-307.
DR PDB; 3Q3O; X-ray; 1.95 A; B=1-307.
DR PDB; 3RI7; X-ray; 2.10 A; B=2-306.
DR PDB; 3RMK; X-ray; 1.95 A; B/E=2-307.
DR PDB; 4P1B; X-ray; 2.05 A; B/E=2-306.
DR PDB; 4P1C; X-ray; 2.40 A; B/E=2-306.
DR PDB; 5TDS; X-ray; 1.72 A; B/E=1-327.
DR PDB; 5TDT; X-ray; 1.82 A; B/F=1-307.
DR PDB; 5TDU; X-ray; 1.74 A; B=1-308.
DR PDB; 5TDV; X-ray; 2.00 A; B/F=1-327.
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; Q00460; -.
DR SMR; Q00460; -.
DR DIP; DIP-48647N; -.
DR IntAct; Q00460; 1.
DR KEGG; ag:AAA26003; -.
DR BioCyc; MetaCyc:MON-2508; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; Q00460; -.
DR 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.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01058; AAMH_B; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012078; MP_mOase_hydro.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR PIRSF; PIRSF000040; MMOH_comp; 1.
DR SUPFAM; SSF47240; SSF47240; 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..327
FT /note="Toluene-4-monooxygenase system, hydroxylase
FT component subunit beta"
FT /id="PRO_0000072603"
FT CONFLICT 310
FT /note="P -> H (in Ref. 1; AAA26003)"
FT /evidence="ECO:0000305"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3I63"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 80..103
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 146..176
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 246..272
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 278..305
FT /evidence="ECO:0007829|PDB:3GE3"
SQ SEQUENCE 327 AA; 38346 MW; 65D6575FF57E040D 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
LSMLSSDILP AQYLERSTSL RASILTV
