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Toluene-4-monooxygenase system ferredoxin subunit (Toluene-4-monooxygenase system protein C) (T4moC)

 TMOC_PSEME              Reviewed;         112 AA.
Q00458; Q6Q8Q5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 80.
RecName: Full=Toluene-4-monooxygenase system, ferredoxin component {ECO:0000303|PubMed:15240250};
Short=T4MO {ECO:0000303|PubMed:1885512};
AltName: Full=Toluene-4-monooxygenase system protein C {ECO:0000303|PubMed:1885512};
Short=T4moC {ECO:0000303|PubMed:1885512};
Name=tmoC {ECO:0000303|PubMed:1885512};
Pseudomonas mendocina.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=300;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
DISRUPTION PHENOTYPE, AND SUBUNIT.
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, AND PATHWAY.
STRAIN=KR1 {ECO:0000312|EMBL:AAS66662.1};
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]
STRUCTURE BY NMR IN COMPLEX WITH IRON-SULFUR (2FE-2S), AND COFACTOR.
PubMed=15452777; DOI=10.1007/s00775-004-0594-4;
Skjeldal L., Peterson F.C., Doreleijers J.F., Moe L.A., Pikus J.D.,
Westler W.M., Markley J.L., Volkman B.F., Fox B.G.;
"Solution structure of T4moC, the Rieske ferredoxin component of the
toluene 4-monooxygenase complex.";
J. Biol. Inorg. Chem. 9:945-953(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
(2FE-2S), AND COFACTOR.
PubMed=16627939; DOI=10.1107/S0907444906006056;
Moe L.A., Bingman C.A., Wesenberg G.E., Phillips G.N. Jr., Fox B.G.;
"Structure of T4moC, the Rieske-type ferredoxin component of toluene
4-monooxygenase.";
Acta Crystallogr. D 62:476-482(2006).
[5]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
(2FE-2S), AND COFACTOR.
PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
"Ensemble refinement of protein crystal structures: validation and
application.";
Structure 15:1040-1052(2007).
[6]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-112 IN COMPLEX WITH
IRON-SULFUR (2FE-2S), COFACTOR, 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).
-!- FUNCTION: Ferredoxin 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). Functions as an intermediate
electron transfer protein (PubMed:15240250).
{ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:1885512}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368};
Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939, ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368};
-!- PATHWAY: Xenobiotic degradation; toluene degradation.
{ECO:0000305|PubMed:15240250}.
-!- SUBUNIT: Homodimer (PubMed:1885512). The alkene monooxygenase
multicomponent enzyme system is composed of an electron transfer
component and a monooxygenase component interacting with the
effector protein TmoD (PubMed:25248368). 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)
(PubMed:25248368). {ECO:0000269|PubMed:1885512,
ECO:0000269|PubMed:25248368}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show a complete loss
of toluene-4-monooxygenase activity. {ECO:0000269|PubMed:1885512}.
-!- SIMILARITY: Belongs to the bacterial ring-hydroxylating
dioxygenase ferredoxin component family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M65106; AAA26001.1; -; Genomic_DNA.
EMBL; AY552601; AAS66662.1; -; Genomic_DNA.
PDB; 1SJG; NMR; -; A=1-112.
PDB; 1VM9; X-ray; 1.48 A; A=2-112.
PDB; 2Q3W; X-ray; 1.48 A; A=2-112.
PDB; 4P1B; X-ray; 2.05 A; H/I=2-112.
PDB; 4P1C; X-ray; 2.40 A; H/I=2-112.
PDBsum; 1SJG; -.
PDBsum; 1VM9; -.
PDBsum; 2Q3W; -.
PDBsum; 4P1B; -.
PDBsum; 4P1C; -.
ProteinModelPortal; Q00458; -.
SMR; Q00458; -.
PRIDE; Q00458; -.
BioCyc; MetaCyc:MONOMER-2502; -.
UniPathway; UPA00273; -.
EvolutionaryTrace; Q00458; -.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 2.102.10.10; -; 1.
InterPro; IPR017941; Rieske_2Fe-2S.
InterPro; IPR036922; Rieske_2Fe-2S_sf.
Pfam; PF00355; Rieske; 1.
SUPFAM; SSF50022; SSF50022; 1.
PROSITE; PS51296; RIESKE; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism;
Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
Metal-binding; Transport.
INIT_MET 1 1 Removed.
CHAIN 2 112 Toluene-4-monooxygenase system,
ferredoxin component.
/FTId=PRO_0000072601.
DOMAIN 4 100 Rieske. {ECO:0000255|PROSITE-
ProRule:PRU00628}.
METAL 45 45 Iron-sulfur (2Fe-2S).
{ECO:0000244|PDB:1SJG,
ECO:0000244|PDB:1VM9,
ECO:0000244|PDB:2Q3W,
ECO:0000244|PDB:4P1B,
ECO:0000244|PDB:4P1C,
ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939,
ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368}.
METAL 47 47 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000244|PDB:1SJG,
ECO:0000244|PDB:1VM9,
ECO:0000244|PDB:2Q3W,
ECO:0000244|PDB:4P1B,
ECO:0000244|PDB:4P1C,
ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939,
ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368}.
METAL 64 64 Iron-sulfur (2Fe-2S).
{ECO:0000244|PDB:1SJG,
ECO:0000244|PDB:1VM9,
ECO:0000244|PDB:2Q3W,
ECO:0000244|PDB:4P1B,
ECO:0000244|PDB:4P1C,
ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939,
ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368}.
METAL 67 67 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000244|PDB:1SJG,
ECO:0000244|PDB:1VM9,
ECO:0000244|PDB:2Q3W,
ECO:0000244|PDB:4P1B,
ECO:0000244|PDB:4P1C,
ECO:0000269|PubMed:15452777,
ECO:0000269|PubMed:16627939,
ECO:0000269|PubMed:17850744,
ECO:0000269|PubMed:25248368}.
STRAND 4 8 {ECO:0000244|PDB:1VM9}.
HELIX 9 11 {ECO:0000244|PDB:1VM9}.
STRAND 16 21 {ECO:0000244|PDB:1VM9}.
STRAND 27 33 {ECO:0000244|PDB:1VM9}.
TURN 34 36 {ECO:0000244|PDB:1VM9}.
STRAND 37 44 {ECO:0000244|PDB:1VM9}.
STRAND 46 49 {ECO:0000244|PDB:1VM9}.
HELIX 52 54 {ECO:0000244|PDB:1VM9}.
STRAND 55 58 {ECO:0000244|PDB:1VM9}.
STRAND 61 63 {ECO:0000244|PDB:1VM9}.
TURN 65 67 {ECO:0000244|PDB:1VM9}.
STRAND 70 72 {ECO:0000244|PDB:1VM9}.
TURN 73 75 {ECO:0000244|PDB:1VM9}.
STRAND 77 83 {ECO:0000244|PDB:1VM9}.
STRAND 91 94 {ECO:0000244|PDB:1VM9}.
STRAND 97 100 {ECO:0000244|PDB:1VM9}.
SEQUENCE 112 AA; 12326 MW; B13CD9A7FC832D07 CRC64;
MSFEKICSLD DIWVGEMETF ETSDGTEVLI VNSEEHGVKA YQAMCPHQEI LLSEGSYEGG
VITCRAHLWT FNDGTGHGIN PDDCCLAEYP VEVKGDDIYV STKGILPNKA HS


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