TMOC_PSEME
ID TMOC_PSEME Reviewed; 112 AA.
AC Q00458; Q6Q8Q5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Toluene-4-monooxygenase system, ferredoxin component {ECO:0000303|PubMed:15240250};
DE Short=T4MO {ECO:0000303|PubMed:1885512};
DE AltName: Full=Toluene-4-monooxygenase system protein C {ECO:0000303|PubMed:1885512};
DE Short=T4moC {ECO:0000303|PubMed:1885512};
GN Name=tmoC {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], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP DISRUPTION PHENOTYPE, AND SUBUNIT.
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:AAS66662.1};
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 IN COMPLEX WITH IRON-SULFUR (2FE-2S), AND COFACTOR.
RX PubMed=15452777; DOI=10.1007/s00775-004-0594-4;
RA Skjeldal L., Peterson F.C., Doreleijers J.F., Moe L.A., Pikus J.D.,
RA Westler W.M., Markley J.L., Volkman B.F., Fox B.G.;
RT "Solution structure of T4moC, the Rieske ferredoxin component of the
RT toluene 4-monooxygenase complex.";
RL J. Biol. Inorg. Chem. 9:945-953(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S), AND COFACTOR.
RX PubMed=16627939; DOI=10.1107/s0907444906006056;
RA Moe L.A., Bingman C.A., Wesenberg G.E., Phillips G.N. Jr., Fox B.G.;
RT "Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-
RT monooxygenase.";
RL Acta Crystallogr. D 62:476-482(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S), AND COFACTOR.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-112 IN COMPLEX WITH IRON-SULFUR
RP (2FE-2S), COFACTOR, 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).
CC -!- FUNCTION: Ferredoxin 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). Functions as an intermediate electron transfer
CC protein (PubMed:15240250). {ECO:0000269|PubMed:15240250,
CC ECO:0000269|PubMed:1885512}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:15452777, ECO:0000269|PubMed:16627939,
CC ECO:0000269|PubMed:17850744, ECO:0000269|PubMed:25248368};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:15452777,
CC ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
CC ECO:0000269|PubMed:25248368};
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC {ECO:0000305|PubMed:15240250}.
CC -!- SUBUNIT: Homodimer (PubMed:1885512). The alkene monooxygenase
CC multicomponent enzyme system is composed of an electron transfer
CC component and a monooxygenase component interacting with the effector
CC protein TmoD (PubMed:25248368). The electron transfer component is
CC composed of a ferredoxin reductase (TmoF) and a ferredoxin (TmoC), and
CC the monooxygenase component is formed by a heterohexamer (dimer of
CC heterotrimers) of two alpha subunits (TmoA), two beta subunits (TmoE)
CC and two gamma subunits (TmoB) (PubMed:25248368).
CC {ECO:0000269|PubMed:1885512, ECO:0000269|PubMed:25248368}.
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 bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; M65106; AAA26001.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66662.1; -; Genomic_DNA.
DR PDB; 1SJG; NMR; -; A=1-112.
DR PDB; 1VM9; X-ray; 1.48 A; A=2-112.
DR PDB; 2Q3W; X-ray; 1.48 A; A=2-112.
DR PDB; 4P1B; X-ray; 2.05 A; H/I=2-112.
DR PDB; 4P1C; X-ray; 2.40 A; H/I=2-112.
DR PDBsum; 1SJG; -.
DR PDBsum; 1VM9; -.
DR PDBsum; 2Q3W; -.
DR PDBsum; 4P1B; -.
DR PDBsum; 4P1C; -.
DR AlphaFoldDB; Q00458; -.
DR SMR; Q00458; -.
DR KEGG; ag:AAA26001; -.
DR BioCyc; MetaCyc:MON-2502; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; Q00458; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
KW Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..112
FT /note="Toluene-4-monooxygenase system, ferredoxin
FT component"
FT /id="PRO_0000072601"
FT DOMAIN 4..100
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:15452777,
FT ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
FT ECO:0000269|PubMed:25248368, ECO:0007744|PDB:1SJG,
FT ECO:0007744|PDB:1VM9, ECO:0007744|PDB:2Q3W,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:15452777,
FT ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
FT ECO:0000269|PubMed:25248368, ECO:0007744|PDB:1SJG,
FT ECO:0007744|PDB:1VM9, ECO:0007744|PDB:2Q3W,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:15452777,
FT ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
FT ECO:0000269|PubMed:25248368, ECO:0007744|PDB:1SJG,
FT ECO:0007744|PDB:1VM9, ECO:0007744|PDB:2Q3W,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:15452777,
FT ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
FT ECO:0000269|PubMed:25248368, ECO:0007744|PDB:1SJG,
FT ECO:0007744|PDB:1VM9, ECO:0007744|PDB:2Q3W,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1VM9"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1VM9"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1VM9"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1VM9"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1VM9"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1VM9"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1VM9"
SQ SEQUENCE 112 AA; 12326 MW; B13CD9A7FC832D07 CRC64;
MSFEKICSLD DIWVGEMETF ETSDGTEVLI VNSEEHGVKA YQAMCPHQEI LLSEGSYEGG
VITCRAHLWT FNDGTGHGIN PDDCCLAEYP VEVKGDDIYV STKGILPNKA HS
