|Gene:||narV||Accession Numbers: EG10644 (EcoCyc), b1465, ECK1459|
Component of: nitrate reductase Z (extended summary available)
narV encodes the γ subunit of nitrate reductase Z - it has 68% identity with narI (encoding the γ subunit of nitrate reductase A) but 87% similarity at the protein level; it is predicted to be the heme b binding subunit which transfers electrons from the quinone pool to the β subunit [Blasco90].
Gene Citations: [Bonnefoy94]
Locations: inner membrane
|Map Position: [1,533,961 <- 1,534,641] (33.06 centisomes, 119°)||Length: 681 bp / 226 aa|
Molecular Weight of Polypeptide: 26.018 kD (from nucleotide sequence)
Isozyme Sequence Similarity:
nitrate reductase A, γ subunit: YES
Unification Links: ASAP:ABE-0004889, CGSC:32136, EchoBASE:EB0638, EcoGene:EG10644, EcoliWiki:b1465, ModBase:P0AF32, OU-Microarray:b1465, PortEco:narV, PR:PRO_000023360, Protein Model Portal:P0AF32, RefSeq:NP_415982, RegulonDB:EG10644, SMR:P0AF32, String:511145.b1465, Swiss-Model:P0AF32, UniProt:P0AF32
|MultiFun Terms:||cell structure → membrane|
|metabolism → energy metabolism, carbon → anaerobic respiration|
|metabolism → energy production/transport → electron acceptors|
|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
Comment 2] |
Yes [Feist07, Comment 4]
Subunit of: nitrate reductase Z
Synonyms: NRZ, quinol:nitrate oxidoreductase
Subunit composition of
nitrate reductase Z = [NarY][NarZ][NarV]
nitrate reductase Z, β subunit = NarY (summary available)
nitrate reductase Z, α subunit = NarZ (summary available)
nitrate reductase Z, γ subunit = NarV (summary available)
Nitrate reductase Z (NRZ) is a membrane bound molybdoenzyme responsible for the weak nitrate reductase activity present when cells are grown aerobically in a nitrate containing medium [Iobbi87].
By homology whith nitrate reductase A, nitrate reductase Z is a heterotrimer composed of the α (NarZ), β (NarY) and γ (NarV) chains. A fourth polypeptide, encoded by narW, is required for the incorporation of the molybdenum cofactor into the α subunit [Blasco90, Blasco92].
NRZ is constitutively expressed in a strain which carries the operon on a multicopy plasmid [Iobbi87]; NRZ is repressed by Fnr in anaerobiosis; NRZ is only slightly induced by nitrate; NRZ may function during the aerobic to anaerobic transition when cells are growing in the presence of nitrate [IobbiNivol90]. During entry into stationary phase, transcription of the narZYWV operon is induced, and induction is mainly dependent on the alternative sigma factor RpoS [Chang99b].
Nitrate reductase Z also has tellurite reductase activity in wild-type E. coli [Avazeri97].
E. coli K-12 contains three nitrate reductases. Two of them, nitrate reductase A (NRA) and nitrate reductase Z (NRZ), are membrane bound and biochemically similar but differentially regulated (reviewed by [Bonnefoy94]. The third nitrate reductase, Nap is located in the periplasm.
Locations: inner membrane
Enzymatic reaction of: nitrate reductase
Synonyms: respiratory nitrate reductase, nitrite:(acceptor) oxidoreductase
EC Number: 220.127.116.11
Enzymatic reaction of: tellurite reductase (nitrate reductase Z)
EC Number: 1.97.1.-tellurite + an reduced unknown electron acceptor → Te0 + an oxidized unknown electron acceptor
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown.
Tellurite reductase activity was measured with benzyl viologen as an electron donor [Avazeri97].
|Transmembrane-Region||5 -> 30|
|Pfam PF02665||6 -> 225|
|Transmembrane-Region||49 -> 71|
|Transmembrane-Region||84 -> 113|
|Transmembrane-Region||126 -> 149|
|Transmembrane-Region||184 -> 199|
10/20/97 Gene b1465 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10644; confirmed by SwissProt match.
Avazeri97: Avazeri C, Turner RJ, Pommier J, Weiner JH, Giordano G, Vermeglio A (1997). "Tellurite reductase activity of nitrate reductase is responsible for the basal resistance of Escherichia coli to tellurite." Microbiology 143 ( Pt 4);1181-9. PMID: 9141681
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
Blasco90: Blasco F, Iobbi C, Ratouchniak J, Bonnefoy V, Chippaux M (1990). "Nitrate reductases of Escherichia coli: sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon." Mol Gen Genet 1990;222(1);104-11. PMID: 2233673
Blasco92: Blasco F, Pommier J, Augier V, Chippaux M, Giordano G (1992). "Involvement of the narJ or narW gene product in the formation of active nitrate reductase in Escherichia coli." Mol Microbiol 1992;6(2);221-30. PMID: 1545706
Chang99b: Chang L, Wei LI, Audia JP, Morton RA, Schellhorn HE (1999). "Expression of the Escherichia coli NRZ nitrate reductase is highly growth phase dependent and is controlled by RpoS, the alternative vegetative sigma factor." Mol Microbiol 34(4);756-66. PMID: 10564515
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
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
Guigliarelli92: Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P (1992). "EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism." Eur J Biochem 207(1);61-8. PMID: 1321049
Iobbi87: Iobbi C, Santini CL, Bonnefoy V, Giordano G (1987). "Biochemical and immunological evidence for a second nitrate reductase in Escherichia coli K12." Eur J Biochem 1987;168(2);451-9. PMID: 3311749
IobbiNivol90: Iobbi-Nivol C, Santini CL, Blasco F, Giordano G (1990). "Purification and further characterization of the second nitrate reductase of Escherichia coli K12." Eur J Biochem 188(3);679-87. PMID: 2139607
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
Park06a: Park YJ, Yoo CB, Choi SY, Lee HB (2006). "Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1." J Biochem Mol Biol 39(1);46-54. PMID: 16466637
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