Escherichia coli K-12 substr. MG1655 Enzyme: NAD(P)H nitroreductase NfsB

Gene: nfsB Accession Numbers: EG50005 (EcoCyc), b0578, ECK0570

Synonyms: ntr, dprA, nfnB

Regulation Summary Diagram: ?

Regulation summary diagram for nfsB

Subunit composition of NAD(P)H nitroreductase NfsB = [NfsB]2
         NAD(P)H nitroreductase NfsB = NfsB

The nfsB-encoded nitroreductase is the minor oxygen-insensitive nitroreductase present in E. coli K-12. NfsB reduces a broad range of nitroaromatic compounds [Zenno96, Zenno96a], including the antibiotics nitrofurazone and nitrofurantoin [McCalla78, Bryant81, Whiteway98].

NfsB is a flavin mononucleotide (FMN)-containing protein and uses both NADH and NADPH as a source of reducing equivalents [Bryant81, Zenno96]. FAD can substitute for FMN as an effective prosthetic group [Zenno96]. NfsB catalyzes the reduction of nitrocompounds using a ping-pong Bi-Bi mechanism [Zenno96]. The reduction of nitrosoaromatic compounds consists of two successive, two-electron transfer reactions to reduce nitrosoaromatics to their hydroxylamine derivatives [Race05]. NfsB can also act as a ferric reductase and catalyze a one-electron reduction of hydrogen peroxide, forming hydroxyl radicals [Takeda10].

An enzyme with dihyropteridine reductase (DHPR) activity [Vasudevan88, Vasudevan92], pterin-independent NAD(P)H oxidoreductase activity with potassium ferricyanide as the electron acceptor [Vasudevan88] and dihydrofolate reductase activity [Vasudevan92] has been purified from E. coli; its N-terminal amino acid sequence [Vasudevan88] is highly similar to that of NfsB.

Crystal structures of NfsB alone [Parkinson00], in complex with the substrate analog nicotinic acid [Lovering01] or with nitrofurazone [Race05], and of several mutant enzymes [Race07] have been solved.

Mutations in nfsB lead to increased resistance to nitrofurazone and furazolidone in an nfsA mutant background [McCalla78, Whiteway98]. Nitrofurantoin resistance due to nfsA/nfsB mutations carries a small fitness cost [Sandegren08]. An nfsA nfsB double mutant retains 30% of wt nitroreductase activity under aerobic conditions [Mercier13]. NfsB has been implicated in the ability to utilize 2,4,6-trinitrotoluene (TNT) as a source of nitrogen [GonzalezPerez07].

Bacterial nitroreductases such as NfsB have been used as prodrug activators for chemotherapy [Denny02, Christofferson09]. Mutants that increase its enzymatic activity against prodrugs (e.g. [Race07]) or to detoxify the anesthetic NBDZ [LinWu12] have been identified.

NfsB: "nitrofuran sensitivity B" [McCalla78]

Reviews: [Roldan08, LinWu10]

Citations: [Sastry84, Breeze83, Grove03, Jarrom09, Jaberipour10, Merkley10, Valle12, Li13a, Shen14, Bai15]

Locations: cytosol, membrane

Map Position: [603,994 <- 604,647] (13.02 centisomes, 47°)
Length: 654 bp / 217 aa

Molecular Weight of Polypeptide: 23.905 kD (from nucleotide sequence), 27.0 kD (experimental) [Zenno96 ]

Molecular Weight of Multimer: 43.0 kD (experimental) [Zenno96]

pI: 6.36

Unification Links: ASAP:ABE-0001981 , DIP:DIP-10330N , EchoBASE:EB4146 , EcoGene:EG20151 , EcoliWiki:b0578 , ModBase:P38489 , OU-Microarray:b0578 , PortEco:nfsB , PR:PRO_000023373 , Pride:P38489 , Protein Model Portal:P38489 , RefSeq:NP_415110 , RegulonDB:EG50005 , SMR:P38489 , String:511145.b0578 , UniProt:P38489

Relationship Links: InterPro:IN-FAMILY:IPR000415 , InterPro:IN-FAMILY:IPR029479 , PDB:Structure:1DS7 , PDB:Structure:1ICR , PDB:Structure:1ICU , PDB:Structure:1ICV , PDB:Structure:1IDT , PDB:Structure:1OO5 , PDB:Structure:1OO6 , PDB:Structure:1OON , PDB:Structure:1OOQ , PDB:Structure:1YKI , PDB:Structure:1YLR , PDB:Structure:1YLU , Pfam:IN-FAMILY:PF00881

In Paralogous Gene Group: 157 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for nfsB

GO Terms:

Biological Process: GO:0046256 - 2,4,6-trinitrotoluene catabolic process Inferred from experiment [GonzalezPerez07]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004155 - 6,7-dihydropteridine reductase activity Inferred from experiment Inferred by computational analysis [GOA01, Vasudevan88]
GO:0010181 - FMN binding Inferred from experiment [Zenno96, Lovering01]
GO:0018545 - NAD(P)H nitroreductase activity Inferred from experiment [Zenno96, McCalla78, Bryant81, Breeze83a]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Lasserre06]
GO:0042803 - protein homodimerization activity Inferred from experiment [Zenno96]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]

MultiFun Terms: cell processes protection drug resistance/sensitivity
metabolism central intermediary metabolism unassigned reversible reactions

Essentiality data for nfsB 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]

Curated 22-Oct-2012 by Mackie A , Macquarie University
Last-Curated ? 29-Apr-2015 by Keseler I , SRI International

Enzymatic reaction of: NAD(P)H nitroreductase

EC Number: 1.7.1.-

an oxidized nitroaromatic compound + NAD(P)H <=> a reduced nitroaromatic compound + NAD(P)+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for an oxidized nitroaromatic compound: 7-nitrocoumarin-3-carboxylate [Mercier13 ] , nitrobenzodiazepine [Linwu09 ] , CB1954 [Race07 , Jarrom09 ] , nitrofurazone [Jarrom09 , Race07 , Valle12 ] , lawsone [Rau03 ] , 1,4-benzoquinone [Zenno96a ] , menadione [Zenno96a ] , ferricyanide [Zenno96a ]

Kinetic parameters [Race05]
Km for NADH varies from 3-8 µM depending on nitro-substrate.
Km for nitrofurazone 160-170 µM.
Km for nitrofurantoin 160-190 µM.
Km for 2-nitrofuran 450-470 µM.

FAD can effectively substitute for FMN [Zenno96]. NfsB does not reduce 3-nitrotyrosine [Lightfoot00].

Cofactors or Prosthetic Groups: FMN [Zenno96]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)

Enzymatic reaction of: dihydropteridine reductase (NAD(P)H nitroreductase NfsB)

Synonyms: NAD(P)H:6,7-dihydropteridine oxidoreductase, DHPR

EC Number:

a 5,6,7,8-tetrahydropteridine + NAD(P)+ <=> a 6,7-dihydropteridine + NAD(P)H + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Alternative Substrates for a 6,7-dihydropteridine [Vasudevan88 ]: cis-6-7-dimethyldihydro-(6H)-pterin , 6-methyldihydro-(6H)-pterin , dihydro-(6H)-monapterin , quinonoid dihydro-(6H)-biopterin , quinonoid dihydro-(6H)-neopterin

Monapterin is the major pterin present in extracts prepared from E. coli lysates - traces of biopterin were also identified [Vasudevan88]. The physiological relevance of dihydropteridine reductase (DHPR) activity in E. coli is not clear.

Cofactors or Prosthetic Groups: FAD [Vasudevan88]

Inhibitors (Competitive): methotrexate [Comment 4]

Sequence Features

Protein sequence of NAD(P)H nitroreductase NfsB with features indicated

Feature Class Location Attached Group Citations Comment
Sequence-Conflict 5  
[Vasudevan88, UniProt10a]
UniProt: (in Ref. 9; AA sequence);
Nucleotide-Phosphate-Binding-Region 10 -> 14 FMN
[Race05, Lovering01, Parkinson00, UniProt15]
UniProt: FMN.
Sequence-Conflict 10 -> 12  
[Vasudevan88, UniProt10a]
UniProt: (in Ref. 9; AA sequence);
Sequence-Conflict 19  
[Vasudevan88, UniProt10a]
UniProt: (in Ref. 9; AA sequence);
Sequence-Conflict 21  
[Anlezark92, UniProt10a]
UniProt: (in Ref. 7; AA sequence);
Sequence-Conflict 28  
[Anlezark92, UniProt10a]
UniProt: (in Ref. 7; AA sequence);
Amino-Acid-Sites-That-Bind 41  
UniProt: NAD or NADP; via amide nitrogen.
Amino-Acid-Sites-That-Bind 71  
[Race05, Lovering01, Parkinson00, UniProt15]
UniProt: FMN.
Nucleotide-Phosphate-Binding-Region 153 -> 158  
UniProt: NAD or NADP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 165 -> 166 FMN
[Race05, Lovering01, Parkinson00, UniProt15]
UniProt: FMN.
Sequence-Conflict 180  
[Anlezark92, UniProt10a]
UniProt: (in Ref. 7; AA sequence);
Nucleotide-Phosphate-Binding-Region 205 -> 207 FMN
[Race05, Lovering01, Parkinson00, UniProt15]
UniProt: FMN.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


7/10/1998 (pkarp) Merged genes G557/b0578 and EG50005/nfnB
3/2/1998 (pkarp) Merged genes EG20151/nfnB and EG50005/EG20151
10/20/97 Gene b0578 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG20151; confirmed by SwissProt match.


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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

Bai15: Bai J, Zhou Y, Chen Q, Yang Q, Yang J (2015). "Altering the Regioselectivity of a Nitroreductase in the Synthesis of Arylhydroxylamines by Structure-Based Engineering." Chembiochem. PMID: 25917861

Breeze83: Breeze AS, Obaseiki-Ebor EE (1983). "Mutations to nitrofurantoin and nitrofurazone resistance in Escherichia coli K12." J Gen Microbiol 129(1);99-103. PMID: 6339681

Breeze83a: Breeze AS, Obaseiki-Ebor EE (1983). "Nitrofuran reductase activity in nitrofurantoin-resistant strains of Escherichia coli K12: some with chromosomally determined resistance and others carrying R-plasmids." J Antimicrob Chemother 12(6);543-7. PMID: 6363380

Bryant81: Bryant DW, McCalla DR, Leeksma M, Laneuville P (1981). "Type I nitroreductases of Escherichia coli." Can J Microbiol 27(1);81-6. PMID: 7011517

Christofferson09: Christofferson A, Wilkie J (2009). "Mechanism of CB1954 reduction by Escherichia coli nitroreductase." Biochem Soc Trans 37(Pt 2);413-8. PMID: 19290872

Denny02: Denny WA (2002). "Nitroreductase-based GDEPT." Curr Pharm Des 8(15);1349-61. PMID: 12052212

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."

GonzalezPerez07: Gonzalez-Perez MM, van Dillewijn P, Wittich RM, Ramos JL (2007). "Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth." Environ Microbiol 9(6);1535-40. PMID: 17504490

Grove03: Grove JI, Lovering AL, Guise C, Race PR, Wrighton CJ, White SA, Hyde EI, Searle PF (2003). "Generation of Escherichia coli nitroreductase mutants conferring improved cell sensitization to the prodrug CB1954." Cancer Res 63(17);5532-7. PMID: 14500391

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jaberipour10: Jaberipour M, Vass SO, Guise CP, Grove JI, Knox RJ, Hu L, Hyde EI, Searle PF (2010). "Testing double mutants of the enzyme nitroreductase for enhanced cell sensitisation to prodrugs: effects of combining beneficial single mutations." Biochem Pharmacol 79(2);102-11. PMID: 19665450

Jarrom09: Jarrom D, Jaberipour M, Guise CP, Daff S, White SA, Searle PF, Hyde EI (2009). "Steady-state and stopped-flow kinetic studies of three Escherichia coli NfsB mutants with enhanced activity for the prodrug CB1954." Biochemistry 48(32);7665-72. PMID: 19580253

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

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Li13a: Li Z, Gao X, Shi W, Li X, Ma H (2013). "7-((5-Nitrothiophen-2-yl)methoxy)-3H-phenoxazin-3-one as a spectroscopic off-on probe for highly sensitive and selective detection of nitroreductase." Chem Commun (Camb) 49(52);5859-61. PMID: 23698620

Lightfoot00: Lightfoot RT, Shuman D, Ischiropoulos H (2000). "Oxygen-insensitive nitroreductases of Escherichia coli do not reduce 3-nitrotyrosine." Free Radic Biol Med 28(7);1132-6. PMID: 10832075

Linwu09: Linwu SW, Syu CJ, Chen YL, Wang AH, Peng FC (2009). "Characterization of Escherichia coli nitroreductase NfsB in the metabolism of nitrobenzodiazepines." Biochem Pharmacol 78(1);96-103. PMID: 19447228

LinWu10: LinWu SW, Wang AH, Peng FC (2010). "Flavin-containing reductase: new perspective on the detoxification of nitrobenzodiazepine." Expert Opin Drug Metab Toxicol 6(8);967-81. PMID: 20504108

LinWu12: LinWu SW, Wu CA, Peng FC, Wang AH (2012). "Structure-based development of bacterial nitroreductase against nitrobenzodiazepine-induced hypnosis." Biochem Pharmacol 83(12);1690-9. PMID: 22445794

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lovering01: Lovering AL, Hyde EI, Searle PF, White SA (2001). "The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution." J Mol Biol 309(1);203-13. PMID: 11491290

McCalla78: McCalla DR, Kaiser C, Green MH (1978). "Genetics of nitrofurazone resistance in Escherichia coli." J Bacteriol 133(1);10-6. PMID: 338576

Mercier13: Mercier C, Chalansonnet V, Orenga S, Gilbert C (2013). "Characteristics of major Escherichia coli reductases involved in aerobic nitro and azo reduction." J Appl Microbiol 115(4);1012-22. PMID: 23795903

Merkley10: Merkley ED, Parson WW, Daggett V (2010). "Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold." Protein Eng Des Sel 23(5);327-36. PMID: 20083491

Parkinson00: Parkinson GN, Skelly JV, Neidle S (2000). "Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme." J Med Chem 43(20);3624-31. PMID: 11020276

Race05: Race PR, Lovering AL, Green RM, Ossor A, White SA, Searle PF, Wrighton CJ, Hyde EI (2005). "Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme." J Biol Chem 280(14);13256-64. PMID: 15684426

Race07: Race PR, Lovering AL, White SA, Grove JI, Searle PF, Wrighton CW, Hyde EI (2007). "Kinetic and structural characterisation of Escherichia coli nitroreductase mutants showing improved efficacy for the prodrug substrate CB1954." J Mol Biol 368(2);481-92. PMID: 17350040

Rajagopala14: 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

Rau03: Rau J, Stolz A (2003). "Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent Azo reductases." Appl Environ Microbiol 69(6);3448-55. PMID: 12788749

Roldan08: Roldan MD, Perez-Reinado E, Castillo F, Moreno-Vivian C (2008). "Reduction of polynitroaromatic compounds: the bacterial nitroreductases." FEMS Microbiol Rev 32(3);474-500. PMID: 18355273

Sandegren08: Sandegren L, Lindqvist A, Kahlmeter G, Andersson DI (2008). "Nitrofurantoin resistance mechanism and fitness cost in Escherichia coli." J Antimicrob Chemother 62(3);495-503. PMID: 18544599

Sastry84: Sastry SS, Jayaraman R (1984). "Nitrofurantoin-resistant mutants of Escherichia coli: isolation and mapping." Mol Gen Genet 196(2);379-80. PMID: 6387400

Shen14: Shen L, Schroeder M, Ogorzalek TL, Yang P, Wu FG, Marsh EN, Chen Z (2014). "Surface orientation control of site-specifically immobilized nitro-reductase (NfsB)." Langmuir 30(20);5930-8. PMID: 24807676

Takeda10: Takeda K, Sato J, Goto K, Fujita T, Watanabe T, Abo M, Yoshimura E, Nakagawa J, Abe A, Kawasaki S, Niimura Y (2010). "Escherichia coli ferredoxin-NADP+ reductase and oxygen-insensitive nitroreductase are capable of functioning as ferric reductase and of driving the Fenton reaction." Biometals 23(4);727-37. PMID: 20407804

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.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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

Valle12: Valle A, Le Borgne S, Bolivar J, Cabrera G, Cantero D (2012). "Study of the role played by NfsA, NfsB nitroreductase and NemA flavin reductase from Escherichia coli in the conversion of ethyl 2-(2'-nitrophenoxy)acetate to 4-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one (D-DIBOA), a benzohydroxamic acid with interesting biological properties." Appl Microbiol Biotechnol 94(1);163-71. PMID: 22173483

Vasudevan88: Vasudevan SG, Shaw DC, Armarego WL (1988). "Dihydropteridine reductase from Escherichia coli." Biochem J 1988;255(2);581-8. PMID: 3060113

Vasudevan92: Vasudevan SG, Paal B, Armarego WL (1992). "Dihydropteridine reductase from Escherichia coli exhibits dihydrofolate reductase activity." Biol Chem Hoppe Seyler 373(10);1067-73. PMID: 1418677

Whiteway98: Whiteway J, Koziarz P, Veall J, Sandhu N, Kumar P, Hoecher B, Lambert IB (1998). "Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli." J Bacteriol 180(21);5529-39. PMID: 9791100

Zenno96: Zenno S, Koike H, Tanokura M, Saigo K (1996). "Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri." J Biochem 120(4);736-44. PMID: 8947835

Zenno96a: Zenno S, Koike H, Tanokura M, Saigo K (1996). "Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution." J Bacteriol 178(15);4731-3. PMID: 8755909

Other References Related to Gene Regulation

Barbosa02c: Barbosa TM, Levy SB (2002). "Activation of the Escherichia coli nfnB gene by MarA through a highly divergent marbox in a class II promoter." Mol Microbiol 45(1);191-202. PMID: 12100559

Martin02: Martin RG, Rosner JL (2002). "Genomics of the marA/soxS/rob regulon of Escherichia coli: identification of directly activated promoters by application of molecular genetics and informatics to microarray data." Mol Microbiol 44(6);1611-24. PMID: 12067348

Martin11: Martin RG, Rosner JL (2011). "Promoter discrimination at class I MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli." J Bacteriol 193(2);506-15. PMID: 21097628

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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