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Escherichia coli K-12 substr. MG1655 Polypeptide: TorC trimethylamine N-oxide reductase, cytochrome c-type subunit



Gene: torC Accession Numbers: EG11815 (EcoCyc), b0996, ECK0987

Regulation Summary Diagram: ?

Component of: trimethylamine N-oxide reductase I (summary available)

Summary:
TorC is a pentahemic c-type cytochrome that is anchored to the inner membrane. [Gon00, Mejean94, Gon01]

The C-terminal domain of the TorC apoprotein is involved in autoregulation of the tor operon [Gon01a].

Gene Citations: [Jourlin96, IobbiNivol96]

Locations: cell wall, inner membrane

Map Position: [1,057,307 -> 1,058,479] (22.79 centisomes)
Length: 1173 bp / 390 aa

Molecular Weight of Polypeptide: 43.607 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003370 , CGSC:29977 , DIP:DIP-11014N , EchoBASE:EB1762 , EcoGene:EG11815 , EcoliWiki:b0996 , Mint:MINT-1285841 , ModBase:P33226 , OU-Microarray:b0996 , PortEco:torC , PR:PRO_000024086 , Pride:P33226 , Protein Model Portal:P33226 , RefSeq:NP_415516 , RegulonDB:EG11815 , SMR:P33226 , String:511145.b0996 , UniProt:P33226

Relationship Links: InterPro:IN-FAMILY:IPR005126 , InterPro:IN-FAMILY:IPR009154 , InterPro:IN-FAMILY:IPR011031 , Pfam:IN-FAMILY:PF03264 , Prosite:IN-FAMILY:PS51008

In Paralogous Gene Group: 237 (2 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Ansaldi07]
GO:0009061 - anaerobic respiration Inferred from experiment [Ansaldi07]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Gon01a]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01, Gon01]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA01, Gon01a]
GO:0020037 - heme binding Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
GO:0050626 - trimethylamine-N-oxide reductase (cytochrome c) activity Inferred by computational analysis [GOA01a, GOA01]
Cellular Component: GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Mejean94]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09]
GO:0009276 - Gram-negative-bacterium-type cell wall Inferred by computational analysis [GOA01]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers cytochromes
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors
regulation genetic unit regulated operon

Essentiality data for torC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 28-Apr-2008 by Nolan L , Macquarie University


Subunit of: trimethylamine N-oxide reductase I

Subunit composition of trimethylamine N-oxide reductase I = [TorC][TorA]2
         TorC trimethylamine N-oxide reductase, cytochrome c-type subunit = TorC (summary available)
         trimethylamine N-oxide reductase, catalytic subunit = TorA (summary available)

Summary:
There are three to four forms of trimethylamine N-oxide (TMAO) reductase in E. coli, one is a constitutive form and the others inducible. TorA and TorC constitute the inducible TMAO reductase I which can accept electrons from various physiological donors via several carriers. Unlike other anaerobic respiratory systems, which are only expressed under anaerobic conditions, TMAO reductase is expressed in both anaerobic and aerobic [Ansaldi07] conditions. The enzyme contains molybdenum, iron, zinc and acid-labile sulfur. Ubiquinones may substitute for menaquinones in TMAO respiration [Yamamoto86, Barrett85, Silvestro88, Silvestro89].

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [Ansaldi07]
GO:0009061 - anaerobic respiration Inferred from experiment [Ansaldi07]
GO:0006810 - transport Inferred by computational analysis [GOA00]
Molecular Function: GO:0009055 - electron carrier activity Inferred from experiment [Gon01]
GO:0050626 - trimethylamine-N-oxide reductase (cytochrome c) activity Inferred by computational analysis [GOA01a]

Credits:
Last-Curated ? 28-Apr-2008 by Nolan L , Macquarie University


Enzymatic reaction of: trimethylamine N-oxide reductase

Synonyms: trimethylamine oxidase, TMAO reductase, NADH:trimethylamine-N-oxide oxidoreductase

Alternative Substrates for trimethylamine N-oxide [Silvestro88 , Yamamoto86 ]: α-picoline N-oxide , adenosine-N-oxide , chlorate , hydroxylamine

In Pathways: formate to trimethylamine N-oxide electron transfer , NADH to trimethylamine N-oxide electron transfer

Summary:
The representation of the TMAO reductase complex indiates transfer of protons across the membrane where protons from MQH2 are moved from the cytoplasmic side to the periplasmic side of the cytoplasmic membrane. This representation has not been experimentally established and is therefore speculative.

Cofactors or Prosthetic Groups: Mo2+ [Yamamoto86]

Cofactor Binding Comment: Besides molybdenum, iron and zinc are also present in the enzyme. [Yamamoto86]

Activators (Unknown Mechanism): Fe3+ [Silvestro88]

Inhibitors (Unknown Mechanism): p-chloromercuribenzoate [Shimokawa79, Silvestro88] , Na+ [Shimokawa79, Silvestro88] , EGTA [Shimokawa79, Silvestro88] , potassium cyanide [Shimokawa79, Silvestro88] , urea [Shimokawa79, Silvestro88] , Cu2+ [Shimokawa79, Silvestro88]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
trimethylamine N-oxide
1440.0
[Gon00, BRENDA14]
trimethylamine N-oxide
670.0, 950.0
[Yamamoto86, BRENDA14]
trimethylamine N-oxide
70.0
151.0
[IobbiNivol96, BRENDA14]
trimethylamine N-oxide
7.65, 27.8, 31.6
58.0, 114.0, 258.0
[Buc99, BRENDA14]

T(opt): 60 °C [BRENDA14, Buc99], 80 °C [BRENDA14, Buc99]

pH(opt): 5 [BRENDA14, Buc99], 5.5 [BRENDA14, Yamamoto86], 6.9 [BRENDA14, Yamamoto86]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 17 -> 37
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Amino-Acid-Sites-That-Bind 48
[UniProt10]
UniProt: Heme 1 (covalent); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 51
[UniProt10]
UniProt: Heme 1 (covalent); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 52
[UniProt10]
UniProt: Iron (heme 1 axial ligand); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 77
[UniProt10]
UniProt: Heme 2 (covalent); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 80
[UniProt10]
UniProt: Heme 2 (covalent); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 81
[UniProt10]
UniProt: Iron (heme 2 axial ligand); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 138
[UniProt10]
UniProt: Heme 3 (covalent); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 141
[UniProt10]
UniProt: Heme 3 (covalent); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 142
[UniProt10]
UniProt: Iron (heme 3 axial ligand); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 170
[UniProt10]
UniProt: Heme 4 (covalent); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 173
[UniProt10]
UniProt: Heme 4 (covalent); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 174
[UniProt10]
UniProt: Iron (heme 4 axial ligand); Non-Experimental Qualifier: by similarity;
Sequence-Conflict 194 -> 195
[Mejean94, UniProt10a]
Alternate sequence: EL → DV; UniProt: (in Ref. 1; CAA52094);
Mutagenesis-Variant 329
[Gon01a, UniProt11]
Alternate sequence: C → S; UniProt: Decrease in expression of the torCAD operon.
Amino-Acid-Sites-That-Bind 329
[UniProt10]
UniProt: Heme 5 (covalent); Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 332
[UniProt10]
UniProt: Heme 5 (covalent); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 333
[UniProt10]
UniProt: Iron (heme 5 axial ligand); Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0996 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11815; confirmed by SwissProt match.


References

Ansaldi07: Ansaldi M, Theraulaz L, Baraquet C, Panis G, Mejean V (2007). "Aerobic TMAO respiration in Escherichia coli." Mol Microbiol 66(2);484-94. PMID: 17850256

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barrett85: Barrett EL, Kwan HS (1985). "Bacterial reduction of trimethylamine oxide." Annu Rev Microbiol 1985;39;131-49. PMID: 3904597

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Buc99: Buc J, Santini CL, Giordani R, Czjzek M, Wu LF, Giordano G (1999). "Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli." Mol Microbiol 32(1);159-68. PMID: 10216869

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA00: GOA (2000). "Gene Ontology annotation based on Swiss-Prot keyword mapping."

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Gon00: Gon S, Patte JC, Mejean V, Iobbi-Nivol C (2000). "The torYZ (yecK bisZ) operon encodes a third respiratory trimethylamine N-oxide reductase in Escherichia coli." J Bacteriol 2000;182(20);5779-86. PMID: 11004177

Gon01: Gon S, Giudici-Orticoni MT, Mejean V, Iobbi-Nivol C (2001). "Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli." J Biol Chem 276(15);11545-51. PMID: 11056172

Gon01a: Gon S, Jourlin-Castelli C, Theraulaz L, Mejean V (2001). "An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli." Proc Natl Acad Sci U S A 98(20);11615-20. PMID: 11562502

IobbiNivol96: Iobbi-Nivol C, Pommier J, Simala-Grant J, Mejean V, Giordano G (1996). "High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli." Biochim Biophys Acta 1996;1294(1);77-82. PMID: 8639717

Jourlin96: Jourlin C, Simon G, Pommier J, Chippaux M, Mejean V (1996). "The periplasmic TorT protein is required for trimethylamine N-oxide reductase gene induction in Escherichia coli." J Bacteriol 1996;178(4);1219-23. PMID: 8576063

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Mejean94: Mejean V, Iobbi-Nivol C, Lepelletier M, Giordano G, Chippaux M, Pascal MC (1994). "TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon." Mol Microbiol 1994;11(6);1169-79. PMID: 8022286

Pascal84: Pascal MC, Burini JF, Chippaux M (1984). "Regulation of the trimethylamine N-oxide (TMAO) reductase in Escherichia coli: analysis of tor::Mud1 operon fusion." Mol Gen Genet 195(1-2);351-5. PMID: 6387391

Pascal91: Pascal MC, Lepelletier M, Giordano G, Chippaux M (1991). "A regulatory mutant of the trimethylamine N-oxide reductase of Escherichia coli K12." FEMS Microbiol Lett 62(2-3);297-300. PMID: 2040436

Shimokawa79: Shimokawa O, Ishimoto M (1979). "Purification and some properties of inducible tertiary amine N-oxide reductase from Escherichia coli." J Biochem (Tokyo) 1979;86(6);1709-17. PMID: 393699

Silvestro88: Silvestro A, Pommier J, Giordano G (1988). "The inducible trimethylamine-N-oxide reductase of Escherichia coli K12: biochemical and immunological studies." Biochim Biophys Acta 1988;954(1);1-13. PMID: 3282544

Silvestro89: Silvestro A, Pommier J, Pascal MC, Giordano G (1989). "The inducible trimethylamine N-oxide reductase of Escherichia coli K12: its localization and inducers." Biochim Biophys Acta 1989;999(2);208-16. PMID: 2512991

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Yamamoto86: Yamamoto I, Okubo N, Ishimoto M (1986). "Further characterization of trimethylamine N-oxide reductase from Escherichia coli, a molybdoprotein." J Biochem (Tokyo) 1986;99(6);1773-9. PMID: 3528139

Other References Related to Gene Regulation

Iuchi87: Iuchi S, Lin EC (1987). "The narL gene product activates the nitrate reductase operon and represses the fumarate reductase and trimethylamine N-oxide reductase operons in Escherichia coli." Proc Natl Acad Sci U S A 1987;84(11);3901-5. PMID: 3035558

Simon95: Simon G, Jourlin C, Ansaldi M, Pascal MC, Chippaux M, Mejean V (1995). "Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression." Mol Microbiol 1995;17(5);971-80. PMID: 8596446


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc14.