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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Escherichia coli K-12 substr. MG1655 Polypeptide: trimethylamine N-oxide reductase III, TorZ subunit



Gene: torZ Accession Numbers: G7022 (EcoCyc), b1872, ECK1873

Synonyms: bisZ

Regulation Summary Diagram: ?

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

Summary:
TorZ is the catalytic subunit of TMAO reductase III. The TorZ protein was first identified as a biotin sulfoxide (BSO) reductase, and the gene was named bisZ [delCampillo96]. Recent work has shown that the reductase is more efficient with TMAO as a substrate than BSO. TorZ is exported to the periplasm via the Tat pathway [Gon00].

Locations: periplasmic space, membrane

Map Position: [1,952,602 <- 1,955,031] (42.08 centisomes)
Length: 2430 bp / 809 aa

Molecular Weight of Polypeptide: 88.964 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006244 , DIP:DIP-9226N , EchoBASE:EB3061 , EcoGene:EG13276 , EcoliWiki:b1872 , ModBase:P46923 , OU-Microarray:b1872 , PortEco:torZ , PR:PRO_000024093 , Pride:P46923 , Protein Model Portal:P46923 , RefSeq:NP_416386 , RegulonDB:G7022 , SMR:P46923 , String:511145.b1872 , Swiss-Model:P46923 , UniProt:P46923

Relationship Links: InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR006655 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006658 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR019546 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Prosite:IN-FAMILY:PS00490 , Prosite:IN-FAMILY:PS00551 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318

In Paralogous Gene Group: 222 (14 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0045333 - cellular respiration Inferred by computational analysis [Gaudet10]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0009055 - electron carrier activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0030151 - molybdenum ion binding Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0050626 - trimethylamine-N-oxide reductase (cytochrome c) activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0016020 - membrane Inferred by computational analysis [Gaudet10]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09, Gon00]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron carriers

Essentiality data for torZ 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]

Subunit of: trimethylamine N-oxide reductase III

Subunit composition of trimethylamine N-oxide reductase III = [TorZ][TorY]
         trimethylamine N-oxide reductase III, TorZ subunit = TorZ (summary available)
         trimethylamine N-oxide reductase III, c-type cytochrome subunit = TorY (summary available)

Summary:
The torYZ-encoded trimethylamine N-oxide (TMAO) reductase III represents a third TMAO respiratory system in E. coli. TorZ is the catalytic subunit and TorY the pentahemic c-type cytochrome subunit. The enzyme has broad substrate specificity; it is able to reduce N- and S-oxide compounds. TMAO is the best substrate for the enzyme. [Gon00]

Expression of torYZ is very low and not inducible by TMAO, DMSO or BSO [Gon00].


Enzymatic reaction of: trimethylamine N-oxide reductase

Synonyms: TMAO reductase, biotin sulfoxide reductase

Alternative Substrates for trimethylamine N-oxide: DL-Methionine sulfoxide , tetrahydrothiophene 1-oxide , 4-methylmorpholine N-Oxide , dimethyl sulfoxide [Gon00 ] , d-biotin d-sulfoxide

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

Summary:
Trimethylamine N-oxide reductase III has broad substrate specificity; it is capable of reducing N- and S-oxide compounds. TMAO is the best substrate for the enzyme [Gon00].

The representation of the TMAO redutase 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.

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
trimethylamine N-oxide
670.0, 950.0
[Yamamoto86, BRENDA14]
trimethylamine N-oxide
1440.0
[Gon00, 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
Signal-Sequence 1 -> 31
[Gon00, UniProt11]
UniProt: Tat-type signal.
Signal-Sequence 1 -> 37
Signal sequence cleavage was confirmed by N-terminal sequencing of the processed product [Gon00].
Chain 32 -> 809
[UniProt09]
UniProt: Trimethylamine-N-oxide reductase 2;
Sequence-Conflict 76
[delCampillo96, UniProt10]
Alternate sequence: A → T; UniProt: (in Ref. 1; AAC44131);
Metal-Binding-Site 176
[UniProt13]
UniProt: Molybdenum; Non-Experimental Qualifier: by similarity.
Sequence-Conflict 291 -> 292
[delCampillo96, UniProt10]
Alternate sequence: HD → TI; UniProt: (in Ref. 1; AAC44131);
Sequence-Conflict 299 -> 304
[delCampillo96, UniProt10]
Alternate sequence: YTTGYP → TLPGIR; UniProt: (in Ref. 1; AAC44131);
Sequence-Conflict 406 -> 409
[delCampillo96, UniProt10]
Alternate sequence: EMSA → DFSGP; UniProt: (in Ref. 1; AAC44131);
Sequence-Conflict 801 -> 803
[delCampillo96, UniProt10]
Alternate sequence: AFD → GFG; UniProt: (in Ref. 1; AAC44131);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

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

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

delCampillo96: del Campillo Campbell A, Campbell A (1996). "Alternative gene for biotin sulfoxide reduction in Escherichia coli K-12." J Mol Evol 42(2);85-90. PMID: 8919859

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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

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

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

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

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: 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.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords 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


Report Errors or Provide Feedback
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, BIOCYC14B.