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Escherichia coli K-12 substr. MG1655 Enzyme: bacterioferritin



Gene: bfr Accession Numbers: EG10113 (EcoCyc), b3336, ECK3323

Synonyms: cytochrome b1, cytochrome b557

Regulation Summary Diagram: ?

Subunit composition of bacterioferritin = [Bfr]24
         bacterioferritin monomer = Bfr

Summary:
The bfr gene encodes bacterioferritin, which is an iron storage protein [Andrews89]. Because a bfr mutant does not exhibit a defect in iron storage [AbdulTehrani99], and because bacterioferritin is observed under conditions of abundant iron [Matzanke89], the cellular role of bacterioferritin in E. coli is subject to debate. E. coli ferritin and bacterioferritin are distinct proteins that form complexes that store iron [Tsugita85, Hudson93].

Bacterioferritin exists as a 24-subunit Bfr homomultimer [Yariv81, Smith89a, Andrews89a, Andrews91a, Frolow94] that forms a sphere of 95 Å [Yariv81] or 119 to 128 Å [Smith89a] in diameter. Structural and physical characteristics of Bfr and Bfr complexes have been examined in detail [Smith91, Andrews89a, Andrews90, Andrews93, Cheesman93, Le93, Dautant98]. Bfr also forms a homodimer [Andrews91a, Andrews93]; this form is favored under low pH conditions [Andrews91a]. Bacterioferritin contains heme and binds non-heme iron [Andrews93, Cheesman93, Le93, Andrews95]. The heme attachment is an unusual bis-methionine axial ligation [Cheesman90, Frolow94]. The Bfr dinuclear-metal-ion-binding site/ferroxidase center and the mechanism by which iron is oxidized for storage within the structure of the bacterioferritin complex are discussed [Le93a, Le95, Keech97, Le97, Yang00c, BouAbdallah02].

Bacterioferritin interacts with the ferredoxin, Bfd [Garg96]. Bfr is soluble in the cytoplasm [Davis99].

A bfr mutant exhibits wild-type iron accumulation upon entering stationary phase in the presence of exogenous iron, in contrast to ftnA and ftnA bfr mutants, which show a defect in iron storage [AbdulTehrani99]. A fur ftnA or fur bfr double mutant exhibits a defect in resistance to hydroperoxides [AbdulTehrani99]. Mutation of residue Met52 results in a bacterioferritin complex that lacks the 12 hemes normally present in the wild-type complex [Andrews95], and mutation of residue Met52 causes the complex to bind more iron than the wild-type complex [Andrews95].

Bacterioferritins and ferritins share conserved amino acids within the ferroxidase center [Andrews91b].

Regulation has been described [Andrews89, Matzanke89, Masse02]. Gene expression is respessed by RyhB, which is a small RNA, and RyhB is subject to negative regulation by the Fur protein [Masse02]. Bacterioferritin is observed under conditions of abundant iron [Matzanke89]. bfr mRNA stability during glucose starvation is diminished in the absence of RNase III function [Freire06].

Reviews: [Andrews92, Moore91, Stiefel94, Thomson97, Andrews98, Andrews03]

Citations: [Smith88a, Yariv96, Yang00d, Jung01, Grady02]

Locations: membrane, cytosol

Map Position: [3,464,271 <- 3,464,747] (74.67 centisomes)
Length: 477 bp / 158 aa

Molecular Weight of Polypeptide: 18.495 kD (from nucleotide sequence), 15 kD (experimental)

Molecular Weight of Multimer: 452 kD (experimental)

Unification Links: ASAP:ABE-0010903 , CGSC:32528 , DIP:DIP-36167N , EchoBASE:EB0111 , EcoGene:EG10113 , EcoliWiki:b3336 , ModBase:P0ABD3 , OU-Microarray:b3336 , PortEco:bfr , PR:PRO_000022212 , Pride:P0ABD3 , Protein Model Portal:P0ABD3 , RefSeq:NP_417795 , RegulonDB:EG10113 , SMR:P0ABD3 , String:511145.b3336 , UniProt:P0ABD3

Relationship Links: InterPro:IN-FAMILY:IPR002024 , InterPro:IN-FAMILY:IPR008331 , InterPro:IN-FAMILY:IPR009040 , InterPro:IN-FAMILY:IPR009078 , InterPro:IN-FAMILY:IPR012347 , PDB:Structure:1BCF , PDB:Structure:1BFR , PDB:Structure:2HTN , PDB:Structure:2VXI , PDB:Structure:2Y3Q , PDB:Structure:3E1J , PDB:Structure:3E1L , PDB:Structure:3E1M , PDB:Structure:3E1N , PDB:Structure:3E1O , PDB:Structure:3E1P , PDB:Structure:3E1Q , PDB:Structure:3E2C , PDB:Structure:3GHQ , Pfam:IN-FAMILY:PF00210 , Prints:IN-FAMILY:PR00601 , Prosite:IN-FAMILY:PS00549 , Prosite:IN-FAMILY:PS50905

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006880 - intracellular sequestering of iron ion Inferred from experiment [Andrews93]
GO:0006826 - iron ion transport Inferred by computational analysis [GOA01]
GO:0006879 - cellular iron ion homeostasis Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005506 - iron ion binding Inferred from experiment [Andrews93]
GO:0020037 - heme binding Inferred from experiment [Yariv81]
GO:0042802 - identical protein binding Inferred from experiment [Yariv81]
GO:0004322 - ferroxidase activity Inferred by computational analysis [GOA01a]
GO:0008199 - ferric iron binding Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Author statement Inferred by computational analysis [UniProtGOA11, Andrews93]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]

MultiFun Terms: cell processes adaptations Fe aquisition

Essentiality data for bfr knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Enzymatic reaction of: ferroxidase (bacterioferritin)

EC Number: 1.16.3.1

4 Fe2+ + 4 H+ + oxygen <=> 4 Fe3+ + 2 H2O

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

The reaction is physiologically favored in the direction shown.


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 1 -> 145
[UniProt09]
UniProt: Ferritin-like diiron;
Extrinsic-Sequence-Variant 5 -> 7
[UniProt10a]
Alternate sequence: TKV → VKI; UniProt: (in strain: ECOR 30);
Mutagenesis-Variant 18
[Baaghil03, UniProt12a]
Alternate sequence: E → A; UniProt: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core.
Metal-Binding-Site 18
[UniProt10a]
UniProt: Iron 1;
Mutagenesis-Variant 31
[Andrews95, UniProt12a]
Alternate sequence: M → L; UniProt: No loss of heme binding.
Alternate sequence: M → H; UniProt: No loss of heme binding.
Extrinsic-Sequence-Variant 38
[UniProt10a]
Alternate sequence: K → M; UniProt: (in strain: ECOR 30);
Mutagenesis-Variant 46
[Crow09, UniProt12a]
Alternate sequence: H → A; UniProt: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired.
Metal-Binding-Site 46
[UniProt12a]
UniProt: Iron 3.
Mutagenesis-Variant 50
[Crow09, UniProt12a]
Alternate sequence: D → A; UniProt: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired.
Metal-Binding-Site 50
[UniProt12a]
UniProt: Iron 3.
Metal-Binding-Site 51
[UniProt10a]
UniProt: Iron 1;
Mutagenesis-Variant 52
[Andrews95, UniProt12a]
Alternate sequence: M → L; UniProt: Loss of heme binding. Is still capable of accumulating iron.
Alternate sequence: M → H; UniProt: Loss of heme binding. Is still capable of accumulating iron.
Metal-Binding-Site 52
[UniProt10a]
UniProt: Iron (heme axial ligand);
Sequence-Conflict 53
[Andrews89a, UniProt10a]
Alternate sequence: K → M; UniProt: (in Ref. 5; AA sequence);
Metal-Binding-Site 54
[UniProt10a]
UniProt: Iron 1;
Extrinsic-Sequence-Variant 57
[UniProt10a]
Alternate sequence: R → K; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 68
[UniProt10a]
Alternate sequence: L → I; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 78
[UniProt10a]
Alternate sequence: N → G; UniProt: (in strain: ECOR 30);
Mutagenesis-Variant 86
[Andrews95, UniProt12a]
Alternate sequence: M → L; UniProt: No loss of heme binding.
Extrinsic-Sequence-Variant 88
[UniProt10a]
Alternate sequence: R → Q; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 92
[UniProt10a]
Alternate sequence: A → R; UniProt: (in strain: ECOR 30);
Metal-Binding-Site 94
[UniProt10a]
UniProt: Iron 2;
Extrinsic-Sequence-Variant 96
[UniProt10a]
Alternate sequence: D → E; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 100
[UniProt10a]
Alternate sequence: N → D; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 106
[UniProt10a]
Alternate sequence: G → A; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 125
[UniProt10a]
Alternate sequence: R → A; UniProt: (in strain: ECOR 30);
Mutagenesis-Variant 127
[Baaghil03, UniProt12a]
Alternate sequence: E → Q; UniProt: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core.
Metal-Binding-Site 127
[UniProt10a]
UniProt: Iron 1;
Mutagenesis-Variant 130
[Baaghil03, UniProt12a]
Alternate sequence: H → E; UniProt: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core.
Metal-Binding-Site 130
[UniProt10a]
UniProt: Iron 2;
Extrinsic-Sequence-Variant 142 -> 144
[UniProt10a]
Alternate sequence: QKM → GKI; UniProt: (in strain: ECOR 30);
Extrinsic-Sequence-Variant 152 -> 158
[UniProt10a]
Alternate sequence: AQIREEG → SQIKVKD; UniProt: (in strain: ECOR 30);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3336 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10113; confirmed by SwissProt match.


References

AbdulTehrani99: Abdul-Tehrani H, Hudson AJ, Chang YS, Timms AR, Hawkins C, Williams JM, Harrison PM, Guest JR, Andrews SC (1999). "Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient." J Bacteriol 181(5);1415-28. PMID: 10049371

Andrews03: Andrews SC, Robinson AK, Rodriguez-Quinones F (2003). "Bacterial iron homeostasis." FEMS Microbiol Rev 27(2-3);215-37. PMID: 12829269

Andrews89: Andrews SC, Harrison PM, Guest JR (1989). "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12." J Bacteriol 171(7);3940-7. PMID: 2661540

Andrews89a: Andrews SC, Smith JM, Guest JR, Harrison PM (1989). "Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia coli-K12." Biochem Biophys Res Commun 158(2);489-96. PMID: 2644932

Andrews90: Andrews SC, Smith JM, Guest JR, Harrison PM (1990). "Genetic and structural characterization of the bacterioferritin of Escherichia coli." Biochem Soc Trans 18(4);658-9. PMID: 2276500

Andrews91a: Andrews SC, Findlay JB, Guest JR, Harrison PM, Keen JN, Smith JM (1991). "Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vinelandii." Biochim Biophys Acta 1078(1);111-6. PMID: 1904771

Andrews91b: Andrews SC, Smith JM, Yewdall SJ, Guest JR, Harrison PM (1991). "Bacterioferritins and ferritins are distantly related in evolution. Conservation of ferroxidase-centre residues." FEBS Lett 293(1-2);164-8. PMID: 1959654

Andrews92: Andrews SC, Arosio P, Bottke W, Briat JF, von Darl M, Harrison PM, Laulhere JP, Levi S, Lobreaux S, Yewdall SJ (1992). "Structure, function, and evolution of ferritins." J Inorg Biochem 47(3-4);161-74. PMID: 1431878

Andrews93: Andrews SC, Smith JM, Hawkins C, Williams JM, Harrison PM, Guest JR (1993). "Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C-terminally extended variant." Eur J Biochem 213(1);329-38. PMID: 8477705

Andrews95: Andrews SC, Le Brun NE, Barynin V, Thomson AJ, Moore GR, Guest JR, Harrison PM (1995). "Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants." J Biol Chem 270(40);23268-74. PMID: 7559480

Andrews98: Andrews SC (1998). "Iron storage in bacteria." Adv Microb Physiol 40;281-351. PMID: 9889981

Baaghil03: Baaghil S, Lewin A, Moore GR, Le Brun NE (2003). "Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center." Biochemistry 42(47);14047-56. PMID: 14636073

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

BouAbdallah02: Bou-Abdallah F, Lewin AC, Le Brun NE, Moore GR, Chasteen ND (2002). "Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry." J Biol Chem 277(40);37064-9. PMID: 12124394

Cheesman90: Cheesman MR, Thomson AJ, Greenwood C, Moore GR, Kadir F (1990). "Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa." Nature 346(6286);771-3. PMID: 2167456

Cheesman93: Cheesman MR, le Brun NE, Kadir FH, Thomson AJ, Moore GR, Andrews SC, Guest JR, Harrison PM, Smith JM, Yewdall SJ (1993). "Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies." Biochem J 292 ( Pt 1);47-56. PMID: 8389131

Crow09: Crow A, Lawson TL, Lewin A, Moore GR, Le Brun NE (2009). "Structural basis for iron mineralization by bacterioferritin." J Am Chem Soc 131(19);6808-13. PMID: 19391621

Dautant98: Dautant A, Meyer JB, Yariv J, Precigoux G, Sweet RM, Kalb AJ, Frolow F (1998). "Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli." Acta Crystallogr D Biol Crystallogr 54 ( Pt 1);16-24. PMID: 9867433

Davis99: Davis GD, Elisee C, Newham DM, Harrison RG (1999). "New fusion protein systems designed to give soluble expression in Escherichia coli." Biotechnol Bioeng 65(4);382-8. PMID: 10506413

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

Freire06: Freire P, Amaral JD, Santos JM, Arraiano CM (2006). "Adaptation to carbon starvation: RNase III ensures normal expression levels of bolA1p mRNA and sigma(S)." Biochimie 88(3-4);341-6. PMID: 16309817

Frolow94: Frolow F, Kalb AJ, Yariv J (1994). "Structure of a unique twofold symmetric haem-binding site." Nat Struct Biol 1(7);453-60. PMID: 7664064

Garg96: Garg RP, Vargo CJ, Cui X, Kurtz DM (1996). "A [2Fe-2S] protein encoded by an open reading frame upstream of the Escherichia coli bacterioferritin gene." Biochemistry 35(20);6297-301. PMID: 8639572

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.

Grady02: Grady JK, Zang J, Laue TM, Arosio P, Chasteen ND (2002). "Characterization of the H- and L-subunit ratios of ferritins by sodium dodecyl sulfate-capillary gel electrophoresis." Anal Biochem 302(2);263-8. PMID: 11878806

Hudson93: Hudson AJ, Andrews SC, Hawkins C, Williams JM, Izuhara M, Meldrum FC, Mann S, Harrison PM, Guest JR (1993). "Overproduction, purification and characterization of the Escherichia coli ferritin." Eur J Biochem 218(3);985-95. PMID: 8281950

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

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

Jung01: Jung Y, Kwak J, Lee Y (2001). "High-level production of heme-containing holoproteins in Escherichia coli." Appl Microbiol Biotechnol 55(2);187-91. PMID: 11330712

Keech97: Keech AM, Le Brun NE, Wilson MT, Andrews SC, Moore GR, Thomson AJ (1997). "Spectroscopic studies of cobalt(II) binding to Escherichia coli bacterioferritin." J Biol Chem 272(1);422-9. PMID: 8995278

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

Le93: Le Brun NE, Cheesman MR, Thomson AJ, Moore GR, Andrews SC, Guest JR, Harrison PM (1993). "An EPR investigation of non-haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate. A study using nitric oxide as a spin probe." FEBS Lett 323(3);261-6. PMID: 8388809

Le93a: Le Brun NE, Wilson MT, Andrews SC, Guest JR, Harrison PM, Thomson AJ, Moore GR (1993). "Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin." FEBS Lett 333(1-2);197-202. PMID: 8224163

Le95: Le Brun NE, Andrews SC, Guest JR, Harrison PM, Moore GR, Thomson AJ (1995). "Identification of the ferroxidase centre of Escherichia coli bacterioferritin." Biochem J 312 ( Pt 2);385-92. PMID: 8526846

Le97: Le Brun NE, Andrews SC, Moore GR, Thomson AJ (1997). "Interaction of nitric oxide with non-haem iron sites of Escherichia coli bacterioferritin: reduction of nitric oxide to nitrous oxide and oxidation of iron(II) to iron(III)." Biochem J 326 ( Pt 1);173-9. PMID: 9337865

Masse02: Masse E, Gottesman S (2002). "A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli." Proc Natl Acad Sci U S A 99(7);4620-5. PMID: 11917098

Matzanke89: Matzanke BF, Muller GI, Bill E, Trautwein AX (1989). "Iron metabolism of Escherichia coli studied by Mossbauer spectroscopy and biochemical methods." Eur J Biochem 183(2);371-9. PMID: 2667998

Moore91: Moore GR (1991). "Bacterial 4-alpha-helical bundle cytochromes." Biochim Biophys Acta 1058(1);38-41. PMID: 1646016

Smith88a: Smith JM, Quirk AV, Plank RW, Diffin FM, Ford GC, Harrison PM (1988). "The identity of Escherichia coli bacterioferritin and cytochrome b1." Biochem J 255(2);737-40. PMID: 3060115

Smith89a: Smith JM, Ford GC, Harrison PM, Yariv J, Kalb AJ (1989). "Molecular size and symmetry of the bacterioferritin of Escherichia coli. X-ray crystallographic characterization of four crystal forms." J Mol Biol 205(2);465-7. PMID: 2648005

Smith91: Smith JM (1991). "Bacterioferritin: structural modelling and molecular symmetry of Escherichia coli BFR." Biochem Soc Trans 19(3);337S. PMID: 1783168

Stiefel94: Stiefel EI, Grossman MJ, Hinton SM, Minak-Bernero V, George GN, Prince RC, Bare RE, Watt GD (1994). "Bacterioferritin: a hemoprotein member of the ferritin family." Adv Exp Med Biol 356;157-64. PMID: 7887220

Thomson97: Thomson AJ, Le Brun NE, Keech A, Andrews SC, Moore GR (1997). "Pumping iron: does bacterioferritin contain a redox-driven iron pump?." Biochem Soc Trans 25(1);96-101. PMID: 9056851

Tsugita85: Tsugita A, Yariv J (1985). "Preliminary results for the primary structure of bacterioferritin of Escherichia coli." Biochem J 231(1);209-12. PMID: 3904732

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

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

Yang00c: Yang X, Le Brun NE, Thomson AJ, Moore GR, Chasteen ND (2000). "The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin." Biochemistry 39(16);4915-23. PMID: 10769150

Yang00d: Yang X, Chiancone E, Stefanini S, Ilari A, Chasteen ND (2000). "Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua." Biochem J 349 Pt 3;783-6. PMID: 10903139

Yariv81: Yariv J, Kalb AJ, Sperling R, Bauminger ER, Cohen SG, Ofer S (1981). "The composition and the structure of bacterioferritin of Escherichia coli." Biochem J 197(1);171-5. PMID: 7032515

Yariv96: Yariv J (1996). "Circumstantial evidence for cytochrome b1 involvement in the functioning of lac-permease in respiring Escherichia coli." J Theor Biol 182(4);459-62. PMID: 8944892


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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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