Escherichia coli K-12 substr. MG1655 Polypeptide: trimethylamine N-oxide reductase, TorZ subunit

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

Synonyms: bisZ

Regulation Summary Diagram

Regulation summary diagram for torZ

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

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. TorZ has 62% identity with the cytoplasmic BSO reductase and 42% identity with TorA [Gon00].

Locations: periplasmic space

Map Position: [1,954,578 <- 1,957,007] (42.11 centisomes, 152°)
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:PS00932, Prosite:IN-FAMILY:PS51318

In Paralogous Gene Group: 222 (14 members)

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

GO Terms:
Biological Process:
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0050626 - trimethylamine-N-oxide reductase (cytochrome c) activity [GOA01, Gon00]
Inferred by computational analysisGO:0003954 - NADH dehydrogenase activity [Gaudet10]
Inferred by computational analysisGO:0009055 - electron carrier activity [GOA01a]
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0030151 - molybdenum ion binding [GOA01a]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11a]
Cellular Component:
Inferred by computational analysisInferred from experimentGO:0030288 - outer membrane-bounded periplasmic space [Gon00, DiazMejia09]
Inferred by computational analysisGO:0042597 - periplasmic space [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: metabolismenergy metabolism, carbonanaerobic respiration
metabolismenergy production/transportelectron carriers

Essentiality data for torZ knockouts:

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

Last-Curated 27-Nov-2014 by Mackie A, Macquarie University

Subunit of: trimethylamine N-oxide reductase TorYZ

Synonyms: menaquinol:trimethylamine N-oxide oxidoreductase

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

torYZ encodes a trimethylamine N-oxide (TMAO) reductase complex in E. coli K-12. 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; dimethyl sulfoxide (DMSO) is a weak substrate in vitro; DMSO is a competitive inhibitor [Gon00]

Expression of torYZ is very low and not inducible by TMAO or dimethyl sulfoxide [Gon00].

GO Terms:
Molecular Function:
Inferred from experimentGO:0050626 - trimethylamine-N-oxide reductase (cytochrome c) activity [Gon00]

Last-Curated 27-Nov-2014 by Mackie A, Macquarie University

Enzymatic reaction of: trimethylamine N-oxide reductase

Inferred from experiment

Synonyms: TMAO reductase, biotin sulfoxide reductase

Transport reaction diagram for trimethylamine N-oxide reductase

Alternative Substrates for trimethylamine N-oxide: methionine S-oxide [Gon00], tetrahydrothiophene 1-oxide [Gon00], 4-methylmorpholine N-oxide [Gon00], d-biotin d-sulfoxide [Gon00]


Inhibitors (Competitive): dimethyl sulfoxide [Gon00]Kinetic Parameters:
Substrate Km (μM) Citations
trimethylamine N-oxide 1440.0 [Gon00, BRENDA14]
4-methylmorpholine N-oxide 1400.0 [Gon00]
tetrahydrothiophene 1-oxide 3370.0 [Gon00]
methionine S-oxide 800.0 [Gon00]
d-biotin d-sulfoxide 360.0 [Gon00]

Sequence Features

Protein sequence of trimethylamine N-oxide reductase, TorZ subunit with features indicated

Feature Class Location Citations Comment
Signal-Sequence 1 -> 31
Inferred from experimentAuthor statement[Gon00, Gon00, UniProt11, Gon00]
UniProt: Tat-type signal.
Chain 32 -> 809
Author statement[UniProt15]
UniProt: Trimethylamine-N-oxide reductase 2.
Sequence-Conflict 76
Inferred by curator[delCampillo96, UniProt15]
UniProt: (in Ref. 1; AAC44131).
Pfam PF00384 84 -> 550
Inferred by computational analysis[Finn14]
Molybdopterin : Molybdopterin oxidoreductase
Metal-Binding-Site 176
Inferred by computational analysis[UniProt15]
UniProt: Molybdenum.
Sequence-Conflict 291 -> 292
Inferred by curator[delCampillo96, UniProt15]
UniProt: (in Ref. 1; AAC44131).
Sequence-Conflict 299 -> 304
Inferred by curator[delCampillo96, UniProt15]
UniProt: (in Ref. 1; AAC44131).
Sequence-Conflict 406 -> 409
Inferred by curator[delCampillo96, UniProt15]
UniProt: (in Ref. 1; AAC44131).
Pfam PF01568 670 -> 779
Inferred by computational analysis[Finn14]
Molydop_binding : Molydopterin dinucleotide binding domain [More...]
Sequence-Conflict 801 -> 803
Inferred by curator[delCampillo96, UniProt15]
UniProt: (in Ref. 1; AAC44131).

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Transcription Unit

Transcription-unit diagram


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.


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.

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

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

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

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." 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."

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
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