TMOD_PSEME
ID TMOD_PSEME Reviewed; 103 AA.
AC Q00459; Q6Q8Q4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Toluene-4-monooxygenase system, effector component {ECO:0000303|PubMed:15240250};
DE Short=T4MO {ECO:0000303|PubMed:1885512};
DE AltName: Full=Toluene-4-monooxygenase effector protein;
DE AltName: Full=Toluene-4-monooxygenase system protein D {ECO:0000303|PubMed:1885512};
DE Short=T4moD {ECO:0000303|PubMed:1885512};
GN Name=tmoD {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 2-22, 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, AND PATHWAY.
RC STRAIN=KR1 {ECO:0000312|EMBL:AAS66663.1};
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 STRUCTURE BY NMR, AND FUNCTION.
RX PubMed=11297417; DOI=10.1021/bi0013703;
RA Hemmi H., Studts J.M., Chae Y.K., Song J., Markley J.L., Fox B.G.;
RT "Solution structure of the toluene 4-monooxygenase effector protein
RT (T4moD).";
RL Biochemistry 40:3512-3524(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS), AND FUNCTION.
RX PubMed=15882052; DOI=10.1021/bi047459g;
RA Lountos G.T., Mitchell K.H., Studts J.M., Fox B.G., Orville A.M.;
RT "Crystal structures and functional studies of T4moD, the toluene 4-
RT monooxygenase catalytic effector protein.";
RL Biochemistry 44:7131-7142(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), FUNCTION, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS), AND 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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND 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 [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.74 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: Effector component of the toluene-4-monooxygenase
CC multicomponent enzyme system which catalyzes the O2- and NADH-dependent
CC hydroxylation of toluene to form p-cresol (PubMed:1885512,
CC PubMed:15240250, PubMed:11297417, PubMed:15882052, PubMed:19033467).
CC Required for optimal efficiency and specificity of the holoenzyme
CC (PubMed:15882052, PubMed:19033467). {ECO:0000269|PubMed:11297417,
CC ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:15882052,
CC ECO:0000269|PubMed:1885512, ECO:0000269|PubMed:19033467}.
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: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 TmoD/XamoD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M65106; AAA26002.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66663.1; -; Genomic_DNA.
DR PDB; 1G10; NMR; -; A=2-103.
DR PDB; 1G11; NMR; -; A=2-103.
DR PDB; 2BF2; X-ray; 2.10 A; A/B=2-103.
DR PDB; 2BF3; X-ray; 1.96 A; A/B=12-103.
DR PDB; 2BF5; X-ray; 1.71 A; A/B=6-103.
DR PDB; 3DHH; X-ray; 1.94 A; E=1-103.
DR PDB; 3DHI; X-ray; 1.68 A; E=1-103.
DR PDB; 3GE3; X-ray; 1.52 A; E=1-103.
DR PDB; 3GE8; X-ray; 2.19 A; E/H=1-103.
DR PDB; 3I5J; X-ray; 1.90 A; E=1-103.
DR PDB; 3I63; X-ray; 2.09 A; E=1-103.
DR PDB; 3Q14; X-ray; 1.75 A; E=1-103.
DR PDB; 3Q2A; X-ray; 1.99 A; E=1-103.
DR PDB; 3Q3M; X-ray; 1.75 A; E/H=1-103.
DR PDB; 3Q3N; X-ray; 1.84 A; E=1-103.
DR PDB; 3Q3O; X-ray; 1.95 A; E=1-103.
DR PDB; 3RI7; X-ray; 2.10 A; E=3-103.
DR PDB; 5TDT; X-ray; 1.82 A; E/H=1-103.
DR PDB; 5TDU; X-ray; 1.74 A; E=1-103.
DR PDB; 5TDV; X-ray; 2.00 A; E/H=1-103.
DR PDBsum; 1G10; -.
DR PDBsum; 1G11; -.
DR PDBsum; 2BF2; -.
DR PDBsum; 2BF3; -.
DR PDBsum; 2BF5; -.
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; 5TDT; -.
DR PDBsum; 5TDU; -.
DR PDBsum; 5TDV; -.
DR AlphaFoldDB; Q00459; -.
DR BMRB; Q00459; -.
DR SMR; Q00459; -.
DR DIP; DIP-48646N; -.
DR IntAct; Q00459; 1.
DR KEGG; ag:AAA26002; -.
DR BioCyc; MetaCyc:MON-2504; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; Q00459; -.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.56.10; -; 1.
DR InterPro; IPR003454; MOase_MmoB_DmpM.
DR InterPro; IPR036889; mOase_MmoB_DmpM_sf.
DR Pfam; PF02406; MmoB_DmpM; 1.
DR SUPFAM; SSF56029; SSF56029; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1885512"
FT CHAIN 2..103
FT /note="Toluene-4-monooxygenase system, effector component"
FT /id="PRO_0000072602"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 46..60
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1G11"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3GE3"
SQ SEQUENCE 103 AA; 11618 MW; 262B14CC1B80644A CRC64;
MSTLADQALH NNNVGPIIRA GDLVEPVIET AEIDNPGKEI TVEDRRAYVR IAAEGELILT
RKTLEEQLGR PFNMQELEIN LASFAGQIQA DEDQIRFYFD KTM
