Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: periplasmic nitrate reductase

Synonyms: Nap

Subunit composition of periplasmic nitrate reductase = [NapB][NapC][(NapG)(NapH)][NapA]
         subunit of periplasmic nitrate reductase, cytochrome c550 protein = NapB (summary available)
         periplasmic nitrate reductase, cytochrome c protein = NapC (summary available)
         NapGH, alternative quinol dehydrogenase = (NapG)(NapH) (summary available)
                 ferredoxin-type protein = NapG (summary available)
                 ferredoxin-type protein = NapH (summary available)
         large subunit of periplasmic nitrate reductase, molybdoprotein = NapA (summary available)

Summary:
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. The third nitrate reductase, Nap, is located in the periplasm. It is induced by anaerobiosis through the mediation of the transcription factor Fnr and low concentrations of nitrate through the mediation of NarP [McNicholas02]. Nap is not itself a coupling site for generating proton motive force; acting as a terminal electron acceptor, it does support anaerobic respiration of various carbon sources [Stewart02].

The physiological role of Nap is that of mediating anaerobic respiration at the expense of low concentrations of nitrate. Owing to the periplasmic location of Nap, the cost of pumping nitrate into the cell is avoided. In addition, Nap has a significantly higher affinity for nitrate than NRA and is thus able to exploit the low concentrations of nitrate occuring in the natural environment of E. coli [Potter99]. Notably, several pathogenic bacterial species, such as Haemophilus influenzae, only contain orthologs of the periplasmic nitrate reductase [Potter99]. During glucose fermentation in the absence of menaquinone, a very low level of Nap activity appears to substitute for the redox-balancing role of fumarate reductase, which is dependent on menaquinone [Brondijk04].

The nap operon encodes seven proteins. The catalytic portion of the protein, consisting of the periplasmic NapA and NapB polypeptides, receives electrons via the membrane-bound cytochrome NapC from NapGH or directly from the quinone pool. The NapD polypeptide is required for enzyme activity and is thought to be involved in the post-translational assembly of the molybdoprotein NapA. NapF, NapG and NapH are predicted to encode iron-sulfur proteins and are not required for Nap activity; they do, however, contribute to the maximum rate of nitrate reduction. NapG and NapH facilitate electron transfer from ubiquinol via NapC to NapAB. [Brondijk04, Brondijk02, Potter99a, Cole96, Grove96, Grove96a, IobbiNivol94]

nap: nitrate reductase in the periplasm [Grove96]

Locations: periplasmic space

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space


Enzymatic reaction of: nitrate reductase

EC Number: 1.7.99.4

Kinetic Parameters:

Substrate
Km (μM)
Citations
nitrate
200.0
[Garland75, BRENDA14]
nitrate
470.0
[Adams82, BRENDA14]


Subunit of periplasmic nitrate reductase: subunit of periplasmic nitrate reductase, cytochrome c550 protein

Synonyms: YejY, NapB, cytochrome c-type protein

Gene: napB Accession Numbers: EG12061 (EcoCyc), b2203, ECK2195

Locations: periplasmic space

Sequence Length: 149 AAs

Molecular Weight: 16.297 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Potter99a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProt-GOA, 2011]
Molecular Function: GO:0046872 - metal ion binding Inferred by computational analysis [UniProt-GOA, 2011]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [Diaz-Mejia et al., 2009, Grove96a]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProt-GOA, 2011]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers cytochromes
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Unification Links: EcoliWiki:b2203 , ModBase:P0ABL3 , PR:PRO_000023346 , Protein Model Portal:P0ABL3 , RefSeq:NP_416707 , SMR:P0ABL3 , String:511145.b2203 , Swiss-Model:P0ABL3 , UniProt:P0ABL3

Relationship Links: InterPro:IN-FAMILY:IPR005591 , InterPro:IN-FAMILY:IPR011031 , InterPro:IN-FAMILY:IPR027406 , Pfam:IN-FAMILY:PF03892 , Prosite:IN-FAMILY:PS51008

Summary:
The napB gene encodes the periplasmic diheme cytochrome c550 protein; it receives electrons from the membrane-bound proteins and passes them to NapA [IobbiNivol94, Grove96a, Grove96, Cole96]. E. coli NapA and NapB proteins do not purify as a heterodimeric complex [Jepson07].

Essentiality data for napB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes et al., 2003, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba et al., 2006, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce et al., 2006, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba et al., 2006, Comment 2]
Yes [Feist07, Comment 4]

Subunit of periplasmic nitrate reductase: periplasmic nitrate reductase, cytochrome c protein

Synonyms: YejX, NapC, cytochrome c-type protein

Gene: napC Accession Numbers: EG12060 (EcoCyc), b2202, ECK2194

Locations: inner membrane

Sequence Length: 200 AAs

Molecular Weight: 23.101 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Potter99a]
GO:0019333 - denitrification pathway Inferred by computational analysis [GOA et al., 2001]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProt-GOA, 2011]
Molecular Function: GO:0020037 - heme binding Inferred by computational analysis [GOA et al., 2001]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProt-GOA, 2011]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProt-GOA, 2011]
GO:0016020 - membrane Inferred by computational analysis [UniProt-GOA, 2011, Grove96a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProt-GOA, 2011, GOA et al., 2001]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers cytochromes
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Unification Links: EcoliWiki:b2202 , ModBase:P0ABL5 , PR:PRO_000023347 , Pride:P0ABL5 , Protein Model Portal:P0ABL5 , RefSeq:NP_416706 , SMR:P0ABL5 , String:511145.b2202 , UniProt:P0ABL5

Relationship Links: InterPro:IN-FAMILY:IPR005126 , InterPro:IN-FAMILY:IPR011031 , InterPro:IN-FAMILY:IPR011885 , InterPro:IN-FAMILY:IPR024717 , Pfam:IN-FAMILY:PF03264 , Prosite:IN-FAMILY:PS51008

Summary:
The napC gene encodes a membrane-bound tetraheme cytochrome c protein, which passes electrons either from NapGH or directly from the quinone pool to NapB [IobbiNivol94, Grove96a, Grove96, Cole96, Brondijk04].

NapC is homologous to CymA in the dissimilatory iron(III)-reducing (DIR) bacterium Shewanella oneidensis MR-1. Heterologous expression of CymA in E. coli enabled growth as a DIR bacterium using Fe(III) NTA as the terminal electron acceptor [Gescher08].

Essentiality data for napC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes et al., 2003, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba et al., 2006, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce et al., 2006, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba et al., 2006, Comment 2]
Yes [Feist07, Comment 4]

Subunit of periplasmic nitrate reductase: NapGH, alternative quinol dehydrogenase

Summary:
Both NapG and NapH are required for efficient electron transfer from ubiquinol, but not menaquinol, via NapC to the NapAB complex. NapGH acts as an alternative quinol dehydrogenase to NapC, which can utilize menaquinol directly [Brondijk02, Brondijk04].

No direct evidence for the formation of a NapGH complex has been obtained yet, but the available experimental data is consistent with its existence [Brondijk04].


Subunit of NapGH, alternative quinol dehydrogenase: ferredoxin-type protein

Synonyms: YojB, YojA, NapG

Gene: napG Accession Numbers: EG12064 (EcoCyc), b2205, ECK2197

Locations: periplasmic space

Sequence Length: 231 AAs

Molecular Weight: 24.925 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProt-GOA, 2011]
Molecular Function: GO:0046872 - metal ion binding Inferred by computational analysis [UniProt-GOA, 2011]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProt-GOA, 2011, GOA et al., 2001]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProt-GOA, 2011]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [Diaz-Mejia et al., 2009, Brondijk04]

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

Unification Links: EcoliWiki:b2205 , ModBase:P0AAL3 , PR:PRO_000023349 , Pride:P0AAL3 , Protein Model Portal:P0AAL3 , RefSeq:NP_416709 , SMR:P0AAL3 , String:511145.b2205 , UniProt:P0AAL3

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR004494 , InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF00037 , Pfam:IN-FAMILY:PF12800 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51379

Summary:
The napG gene encodes a non-haem iron-sulfur protein. [Grove96a, Grove96, Cole96]

NapG together with NapH is required for electron transfer from ubiquinol, but not menaquinol, via NapC to the NapAB complex [Brondijk02, Brondijk04]. NapG contains a twin-arginine sequence which is essential for its function, and some evidence for periplasmic localization of the protein has been obtained [Brondijk04].

Essentiality data for napG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes et al., 2003, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba et al., 2006, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce et al., 2006, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba et al., 2006, Comment 2]
Yes [Feist07, Comment 4]

Subunit of NapGH, alternative quinol dehydrogenase: ferredoxin-type protein

Synonyms: YejZ, NapH

Gene: napH Accession Numbers: EG12062 (EcoCyc), b2204, ECK2196

Locations: inner membrane

Sequence Length: 287 AAs

Molecular Weight: 31.873 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProt-GOA, 2011]
Molecular Function: GO:0005506 - iron ion binding Inferred by computational analysis [GOA et al., 2001]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProt-GOA, 2011]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProt-GOA, 2011, GOA et al., 2001]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProt-GOA, 2011]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProt-GOA, 2011, Diaz-Mejia et al., 2009, Daley05]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProt-GOA, 2011, Brondijk04]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProt-GOA, 2011]

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

Unification Links: DIP:DIP-10310N , EcoliWiki:b2204 , Mint:MINT-1276100 , ModBase:P33934 , PR:PRO_000023350 , Protein Model Portal:P33934 , RefSeq:NP_416708 , SMR:P33934 , String:511145.b2204 , UniProt:P33934

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR011886 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF12801 , Pfam:IN-FAMILY:PF12837 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

Summary:
The napH gene encodes a non-haem iron-sulfur protein. [Grove96a, Grove96, Cole96]

NapH together with NapG is required for electron transfer from ubiquinol, but not menaquinol, via NapC to the NapAB complex [Brondijk02, Brondijk04]. NapH is an integral membrane protein with four membrane-spanning domains; the C-terminal domain with its two predicted [4Fe-4S] clusters is located in the cytoplasm [Brondijk04]. Using two-hybrid assays, it has been shown that NapH interacts strongly with NapC [Brondijk04].

Essentiality data for napH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes et al., 2003, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba et al., 2006, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce et al., 2006, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba et al., 2006, Comment 2]
Yes [Feist07, Comment 4]

Subunit of periplasmic nitrate reductase: large subunit of periplasmic nitrate reductase, molybdoprotein

Synonyms: YojE, YojC, YojD, NapA

Gene: napA Accession Numbers: EG12067 (EcoCyc), b2206, ECK2198

Locations: periplasmic space

Sequence Length: 828 AAs

Molecular Weight: 93.042 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Stewart02]
GO:0006777 - Mo-molybdopterin cofactor biosynthetic process Inferred by computational analysis [GOA06]
GO:0042128 - nitrate assimilation Inferred by computational analysis [UniProt-GOA, 2011, GOA06, GOA et al., 2001]
GO:0045333 - cellular respiration Inferred by computational analysis [Gaudet10]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProt-GOA, 2011, GOA06, GOA et al., 2001]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala et al., 2014, Dow14, Chan10a, Chan09]
GO:0008940 - nitrate reductase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA et al., 2001, Thomas99a, Stewart02, Grove96]
GO:0030151 - molybdenum ion binding Inferred from experiment Inferred by computational analysis [GOA et al., 2001, Jepson07]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProt-GOA, 2011, GOA06, GOA et al., 2001, Jepson07]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA06]
GO:0009055 - electron carrier activity Inferred by computational analysis [GOA06]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProt-GOA, 2011, GOA et al., 2001]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [Gaudet10]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProt-GOA, 2011]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProt-GOA, 2011]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [Diaz-Mejia et al., 2009, Han13, Thomas99a]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProt-GOA, 2011, GOA06, GOA et al., 2001, Grove96]

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

Unification Links: DIP:DIP-10304N , EcoliWiki:b2206 , Mint:MINT-1243254 , ModBase:P33937 , PR:PRO_000023345 , Pride:P33937 , Protein Model Portal:P33937 , RefSeq:NP_416710 , SMR:P33937 , String:511145.b2206 , UniProt:P33937

Relationship Links: InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR010051 , InterPro:IN-FAMILY:IPR019546 , InterPro:IN-FAMILY:IPR027467 , PDB:Structure:2NYA , PDB:Structure:2PQ4 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Prosite:IN-FAMILY:PS00490 , Prosite:IN-FAMILY:PS00551 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926

Summary:
The napA gene encodes the periplasmic nitrate reductase molybdoprotein with an Fe-S center [Grove96, Cole96]. NapA binds a [4Fe-4S] cluster and bis-molybdopterin guanine dinucleotide [Jepson07]. NapA is synthesized as a precursor with a 36 residue signal peptide that is removed upon export to the periplasm [Thomas99a]. Prior to export the the signal peptide of NapA is bound to the NapD chaperone which may act to protect NapD from translocation until cofactor loading is complete [Maillard07]. A NapD binding epitope is located towards the N-terminus of the NapA signal peptide and partially overlaps with the twin arginine motif [Grahl12]. An NMR structure of the NapD-NapA signal peptide complex has been reported [Grahl12].

Essentiality data for napA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes et al., 2003, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba et al., 2006, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce et al., 2006, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba et al., 2006, Comment 2]
Yes [Feist07, Comment 4]

References

Adams82: Adams MW, Mortenson LE (1982). "The effect of cyanide and ferricyanide on the activity of the dissimilatory nitrate reductase of Escherichia coli." J Biol Chem 257(4);1791-9. PMID: 7035454

Baba et al., 2006: 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.

Brondijk02: Brondijk TH, Fiegen D, Richardson DJ, Cole JA (2002). "Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation." Mol Microbiol 44(1);245-55. PMID: 11967083

Brondijk04: Brondijk TH, Nilavongse A, Filenko N, Richardson DJ, Cole JA (2004). "NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing." Biochem J 379(Pt 1);47-55. PMID: 14674886

Chan09: Chan CS, Chang L, Rommens KL, Turner RJ (2009). "Differential interactions between Tat-specific redox enzyme peptides and their chaperones." J Bacteriol 191(7):2091-101. PMID: 19151138

Chan10a: Chan CS, Chang L, Winstone TM, Turner RJ (2010). "Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates." FEBS Lett 584(22);4553-8. PMID: 20974141

Cole96: Cole J (1996). "Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation?." FEMS Microbiol Lett 1996;136(1);1-11. PMID: 8919448

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Diaz-Mejia et al., 2009: 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

Dow14: Dow JM, Grahl S, Ward R, Evans R, Byron O, Norman DG, Palmer T, Sargent F (2014). "Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone." FEBS J 281(1);246-60. PMID: 24314029

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

Garland75: Garland PB, Downie JA, Haddock BA (1975). "Proton translocation and the respiratory nitrate reductase of Escherichia coli." Biochem J 152(3);547-59. PMID: 5996

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

Gerdes et al., 2003: 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

Gescher08: Gescher JS, Cordova CD, Spormann AM (2008). "Dissimilatory iron reduction in Escherichia coli: identification of CymA of Shewanella oneidensis and NapC of E. coli as ferric reductases." Mol Microbiol 68(3);706-19. PMID: 18394146

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Grahl12: Grahl S, Maillard J, Spronk CA, Vuister GW, Sargent F (2012). "Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide." Mol Microbiol 83(6);1254-67. PMID: 22329966

Grove96: Grove J, Tanapongpipat S, Thomas G, Griffiths L, Crooke H, Cole J (1996). "Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm." Mol Microbiol 1996;19(3);467-81. PMID: 8830238

Grove96a: Grove J, Busby S, Cole J (1996). "The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli." Mol Gen Genet 1996;252(3);332-41. PMID: 8842153

Han13: Han MJ, Kim JY, Kim JA (2013). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng. PMID: 24140104

IobbiNivol94: Iobbi-Nivol C, Crooke H, Griffiths L, Grove J, Hussain H, Pommier J, Mejean V, Cole JA (1994). "A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12." FEMS Microbiol Lett 1994;119(1-2);89-94. PMID: 8039676

Jepson07: Jepson BJ, Mohan S, Clarke TA, Gates AJ, Cole JA, Butler CS, Butt JN, Hemmings AM, Richardson DJ (2007). "Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli." J Biol Chem 282(9);6425-37. PMID: 17130127

Joyce et al., 2006: 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

Maillard07: Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F (2007). "Structural diversity in twin-arginine signal peptide-binding proteins." Proc Natl Acad Sci U S A 104(40);15641-6. PMID: 17901208

McNicholas02: McNicholas PM, Gunsalus RP (2002). "The molybdate-responsive Escherichia coli ModE transcriptional regulator coordinates periplasmic nitrate reductase (napFDAGHBC) operon expression with nitrate and molybdate availability." J Bacteriol 184(12);3253-9. PMID: 12029041

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

Potter99: Potter LC, Millington P, Griffiths L, Thomas GH, Cole JA (1999). "Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?." Biochem J 344 Pt 1;77-84. PMID: 10548536

Potter99a: Potter LC, Cole JA (1999). "Essential roles for the products of the napABCD genes, but not napFGH, in periplasmic nitrate reduction by Escherichia coli K-12." Biochem J 1999;344 Pt 1;69-76. PMID: 10548535

Rajagopala et al., 2014: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Stewart02: Stewart V, Lu Y, Darwin AJ (2002). "Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12." J Bacteriol 184(5);1314-23. PMID: 11844760

Thomas99a: Thomas G, Potter L, Cole JA (1999). "The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site." FEMS Microbiol Lett 1999;174(1);167-71. PMID: 10234835

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

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms 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
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, biocyc11.