2.0 2012-05-31 13:00:23 -0600 2015-09-13 12:56:08 -0600 ECMDB00692 M2MDB000172 Iron Iron is a chemical element with the symbol Fe and atomic number 26. Iron makes up 5% of the Earth's crust and is second in abundance to aluminium among the metals and fourth in abundance among the elements. Iron (as Fe2+, ferrous ion) is a necessary trace element used by all known living organisms. Iron-containing enzymes, usually containing heme prosthetic groups, participate in catalysis of oxidation reactions in biology, and in transport of a number of soluble gases. Its chief functions are in the transport of oxygen to tissue (hemoglobin) and in cellular oxidation mechanisms. Inorganic iron involved in redox reactions is also found in the iron-sulfur clusters of many enzymes, such as nitrogenase (involved in the synthesis of ammonia from nitrogen and hydrogen) and hydrogenase. A class of non-heme iron proteins is responsible for a wide range of functions such as ribonucleotide reductase (reduces ribose to deoxyribose; DNA biosynthesis) and purple acid phosphatase (hydrolysis of phosphate esters). When the body is fighting a bacterial infection, the body sequesters iron inside of cells (mostly stored in the storage molecule ferritin) so that it cannot be used by bacteria. Iron may promote both growth of E. coli. (PMID: 16151163) Armco iron Carbonyl iron FE Fe(ii) Fe++ Fe+2 Fe2+ Fe++ Fe+2 Ferrous ion Ferrous iron Ferrovac e Hematite Infed Limonite LOHA Magnetite Malleable iron Metopirone Metyrapone Pzh2M PZHO Remko Suy-B 2 Taconite Venofer Wrought iron Fe 55.845 55.934942133 lambda2-iron(2+) ion lambda2-iron(2+) ion 7439-89-6 [Fe++] InChI=1S/Fe/q+2 CWYNVVGOOAEACU-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm melting_point 1538 oC logp -0.77 ChemAxon pka_strongest_acidic 4.58 ChemAxon iupac lambda2-iron(2+) ion ChemAxon average_mass 55.845 ChemAxon mono_mass 55.934942133 ChemAxon smiles [Fe++] ChemAxon formula Fe ChemAxon inchi InChI=1S/Fe/q+2 ChemAxon inchikey CWYNVVGOOAEACU-UHFFFAOYSA-N ChemAxon polar_surface_area 0 ChemAxon refractivity 0 ChemAxon polarizability 1.78 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 0 ChemAxon donor_count 0 ChemAxon physiological_charge 2 ChemAxon formal_charge 2 ChemAxon Pyrimidine metabolism The metabolism of pyrimidines begins with L-glutamine interacting with water molecule and a hydrogen carbonate through an ATP driven carbamoyl phosphate synthetase resulting in a hydrogen ion, an ADP, a phosphate, an L-glutamic acid and a carbamoyl phosphate. The latter compound interacts with an L-aspartic acid through a aspartate transcarbamylase resulting in a phosphate, a hydrogen ion and a N-carbamoyl-L-aspartate. The latter compound interacts with a hydrogen ion through a dihydroorotase resulting in the release of a water molecule and a 4,5-dihydroorotic acid. This compound interacts with an ubiquinone-1 through a dihydroorotate dehydrogenase, type 2 resulting in a release of an ubiquinol-1 and an orotic acid. The orotic acid then interacts with a phosphoribosyl pyrophosphate through a orotate phosphoribosyltransferase resulting in a pyrophosphate and an orotidylic acid. The latter compound then interacts with a hydrogen ion through an orotidine-5 '-phosphate decarboxylase, resulting in an release of carbon dioxide and an Uridine 5' monophosphate. The Uridine 5' monophosphate process to get phosphorylated by an ATP driven UMP kinase resulting in the release of an ADP and an Uridine 5--diphosphate. Uridine 5-diphosphate can be metabolized in multiple ways in order to produce a Deoxyuridine triphosphate. 1.-Uridine 5-diphosphate interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in the release of a water molecule and an oxidized thioredoxin and an dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate. 2.-Uridine 5-diphosphate interacts with a reduced NrdH glutaredoxin-like protein through a Ribonucleoside-diphosphate reductase 1 resulting in a release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate. 3.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate. The latter compound interacts with a reduced flavodoxin through ribonucleoside-triphosphate reductase resulting in the release of an oxidized flavodoxin, a water molecule and a Deoxyuridine triphosphate 4.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in the release of a water molecule, an oxidized flavodoxin and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. 5.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP then interacts with a reduced NrdH glutaredoxin-like protein through a ribonucleoside-diphosphate reductase 2 resulting in the release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. 6.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate. The deoxyuridine triphosphate then interacts with a water molecule through a nucleoside triphosphate pyrophosphohydrolase resulting in a release of a hydrogen ion, a phosphate and a dUMP. The dUMP then interacts with a methenyltetrahydrofolate through a thymidylate synthase resulting in a dihydrofolic acid and a 5-thymidylic acid. Then 5-thymidylic acid is then phosphorylated through a nucleoside diphosphate kinase resulting in the release of an ADP and thymidine 5'-triphosphate. PW000942 ec00240 Metabolic Biosynthesis of siderophore group nonribosomal peptides 2,3-dihydroxybenzoate is synthesized from chorismate via isochorismate and 2,3-dihydroxy-2,3-dihydrobenzoate. The biosynthesis of 2,3-dihydroxybenzoate starts from chorismate being synthesized into isochorismate through isochorismate synthase entC. EntC catalyzes the conversion of chorismate to isochorismate. The N-terminal isochorismate lyase domain of EntB hydrolyzes the pyruvate group of isochorismate to produce 2,3-dihydro-2,3-dihydroxybenzoate. The conversion of this latter compound to 2,3-dihydroxybenzoate is catalyzed by the EntA dehydrogenase.This compound then interacts with L-serine and ATP through enterobactin synthase protein complex resulting in the production of enterobactin. Enterobactin is exported into the periplasmic space through the enterobactin exporter entS. The compound is the export to the environment through the outer membrane protein TolC. In the environment enterobactin reacts with iron to produce Ferric enterobactin. This compound is imported into the periplasmic space through a ferric enterobactin outermembrane transport complex. The compound then enters the cytoplasm through a ferric enterobactin ABC transporter.Once inside the cytoplasm, ferric enterobactin spontaneously releases the iron ion from the enterobactin. PW000760 ec01053 Metabolic Two-component system ec02020 2-Oxopent-4-enoate metabolism The pathway starts with trans-cinnamate interacting with a hydrogen ion, an oxygen molecule, and a NADH through a cinnamate dioxygenase resulting in a NAD and a cis-3-(3-Carboxyethenyl)-3,5-cyclohexadiene-1,2-diol which then interact together through a 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase resulting in the release of a hydrogen ion, an NADH molecule and a 2,3 dihydroxy-trans-cinnamate. The second way by which the 2,3 dihydroxy-trans-cinnamate is acquired is through a 3-hydroxy-trans-cinnamate interacting with a hydrogen ion, a NADH and an oxygen molecule through a 3-(3-hydroxyphenyl)propionate 2-hydroxylase resulting in the release of a NAD molecule, a water molecule and a 2,3-dihydroxy-trans-cinnamate. The compound 2,3 dihydroxy-trans-cinnamate then interacts with an oxygen molecule through a 2,3-dihydroxyphenylpropionate 1,2-dioxygenase resulting in a hydrogen ion and a 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. The latter compound then interacts with a water molecule through a 2-hydroxy-6-oxononatrienedioate hydrolase resulting in a release of a hydrogen ion, a fumarate molecule and (2Z)-2-hydroxypenta-2,4-dienoate. The latter compound reacts spontaneously to isomerize into a 2-oxopent-4-enoate. This compound is then hydrated through a 2-oxopent-4-enoate hydratase resulting in a 4-hydroxy-2-oxopentanoate. This compound then interacts with a 4-hydroxy-2-ketovalerate aldolase resulting in the release of a pyruvate, and an acetaldehyde. The acetaldehyde then interacts with a coenzyme A and a NAD molecule through a acetaldehyde dehydrogenase resulting in a hydrogen ion, a NADH and an acetyl-coa which can be incorporated into the TCA cycle PW001890 Metabolic Collection of Reactions without pathways PW001891 Metabolic Porphyrin metabolism The metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter . L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate. This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane. Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III. Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III. Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+ uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway. Uroporphyrinogen III can be processed in anaerobic or aerobic condition. Anaerobic: Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX Aerobic: Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX. The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway. PW000936 Metabolic threonine biosynthesis The biosynthesis of threonine starts with oxalacetic acid interacting with an L-glutamic acid through an aspartate aminotransferase resulting in a oxoglutaric acid and an L-aspartic acid. The latter compound is then phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000817 Metabolic 2-Oxopent-4-enoate metabolism 2 The pathway starts with trans-cinnamate interacting with a hydrogen ion, an oxygen molecule, and a NADH through a cinnamate dioxygenase resulting in a NAD and a Cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol which then interact together through a 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase resulting in the release of a hydrogen ion, an NADH molecule and a 2,3 dihydroxy-trans-cinnamate. The second way by which the 2,3 dihydroxy-trans-cinnamate is acquired is through a 3-hydroxy-trans-cinnamate interacting with a hydrogen ion, a NADH and an oxygen molecule through a 3-(3-hydroxyphenyl)propionate 2-hydroxylase resulting in the release of a NAD molecule, a water molecule and a 2,3-dihydroxy-trans-cinnamate. The compound 2,3 dihydroxy-trans-cinnamate then interacts with an oxygen molecule through a 2,3-dihydroxyphenylpropionate 1,2-dioxygenase resulting in a hydrogen ion and a 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. The latter compound then interacts with a water molecule through a 2-hydroxy-6-oxononatrienedioate hydrolase resulting in a release of a hydrogen ion, a fumarate molecule and (2Z)-2-hydroxypenta-2,4-dienoate. The latter compound reacts spontaneously to isomerize into a 2-oxopent-4-enoate. This compound is then hydrated through a 2-oxopent-4-enoate hydratase resulting in a 4-hydroxy-2-oxopentanoate. This compound then interacts with a 4-hydroxy-2-ketovalerate aldolase resulting in the release of a pyruvate, and an acetaldehyde. The acetaldehyde then interacts with a coenzyme A and a NAD molecule through a acetaldehyde dehydrogenase resulting in a hydrogen ion, a NADH and an acetyl-coa which can be incorporated into the TCA cycle PW002035 Metabolic L-threonine degradation to methylglyoxal L-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways. PW002106 Metabolic Specdb::MsMs 62010 Specdb::MsMs 62011 Specdb::MsMs 62012 Specdb::MsMs 118659 Specdb::MsMs 118660 Specdb::MsMs 118661 HMDB00692 23925 25394 C00023 18248 FE+2 FE2 Iron Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. 21097882 Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 Appenzeller, B. M., Yanez, C., Jorand, F., Block, J. C. (2005). "Advantage provided by iron for Escherichia coli growth and cultivability in drinking water." Appl Environ Microbiol 71:5621-5623. 16151163 Gal S, Fridkin M, Amit T, Zheng H, Youdim MB: M30, a novel multifunctional neuroprotective drug with potent iron chelating and brain selective monoamine oxidase-ab inhibitory activity for Parkinson's disease. J Neural Transm Suppl. 2006;(70):447-56. 17017567 Piga A, Galanello R, Forni GL, Cappellini MD, Origa R, Zappu A, Donato G, Bordone E, Lavagetto A, Zanaboni L, Sechaud R, Hewson N, Ford JM, Opitz H, Alberti D: Randomized phase II trial of deferasirox (Exjade, ICL670), a once-daily, orally-administered iron chelator, in comparison to deferoxamine in thalassemia patients with transfusional iron overload. Haematologica. 2006 Jul;91(7):873-80. 16818273 Nasolodin VV, Zaitseva IP, Gladkikh IP, Voronin SM: [Correction of iron and immune deficiencies in students from a higher humanitarian educational establishment] Gig Sanit. 2005 Sep-Oct;(5):64-7. 16277000 Custodio PJ, Carvalho ML, Nunes F, Pedroso S, Campos A: Direct analysis of human blood (mothers and newborns) by energy dispersive X-ray fluorescence. J Trace Elem Med Biol. 2005;19(2-3):151-8. Epub 2005 Oct 24. 16325530 Agarwal MB: Exjade (ICL 670): A new oral iron chelator. J Assoc Physicians India. 2006 Mar;54:214-7. 16800349 Cortese S, Konofal E, Lecendreux M, Mouren MC, Bernardina BD: Restless legs syndrome triggered by heart surgery. Pediatr Neurol. 2006 Sep;35(3):223-6. 16939866 Barkova EN, Nazarenko EV, Zhdanova EV: Diurnal variations in qualitative composition of breast milk in women with iron deficiency. Bull Exp Biol Med. 2005 Oct;140(4):394-6. 16671562 Christoforidis A, Haritandi A, Tsitouridis I, Tsatra I, Tsantali H, Karyda S, Dimitriadis AS, Athanassiou-Metaxa M: Correlative study of iron accumulation in liver, myocardium, and pituitary assessed with MRI in young thalassemic patients. J Pediatr Hematol Oncol. 2006 May;28(5):311-5. 16772883 Kom GD, Schwedhelm E, Nielsen P, Boger RH: Increased urinary excretion of 8-iso-prostaglandin F2alpha in patients with HFE-related hemochromatosis: a case-control study. Free Radic Biol Med. 2006 Apr 1;40(7):1194-200. Epub 2005 Dec 13. 16545687 Gerlach M, Double KL, Youdim MB, Riederer P: Potential sources of increased iron in the substantia nigra of parkinsonian patients. J Neural Transm Suppl. 2006;(70):133-42. 17017520 Jost PJ, Stengel SM, Huber W, Sarbia M, Peschel C, Duyster J: Very severe iron-deficiency anemia in a patient with celiac disease and bulimia nervosa: a case report. 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Acta Haematol. 2006;115(1-2):106-8. 16424659 Matinaho S, Karhumaki P, Parkkinen J: Bicarbonate inhibits the growth of Staphylococcus epidermidis in platelet concentrates by lowering the level of non-transferrin-bound iron. Transfusion. 2005 Nov;45(11):1768-73. 16271102 Blanck HM, Cogswell ME, Gillespie C, Reyes M: Iron supplement use and iron status among US adults: results from the third National Health and Nutrition Examination Survey. Am J Clin Nutr. 2005 Nov;82(5):1024-31. 16280434 Yarali N, Fisgin T, Duru F, Kara A, Ecin N, Fitoz S, Erden I: Subcutaneous bolus injection of deferoxamine is an alternative method to subcutaneous continuous infusion. J Pediatr Hematol Oncol. 2006 Jan;28(1):11-6. 16394886 Walter PB, Fung EB, Killilea DW, Jiang Q, Hudes M, Madden J, Porter J, Evans P, Vichinsky E, Harmatz P: Oxidative stress and inflammation in iron-overloaded patients with beta-thalassaemia or sickle cell disease. 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Curr Med Chem. 2005;12(23):2695-709. 16305466 http://hmdb.ca/system/metabolites/msds/000/000/611/original/IRON_msds.pdf?1368649641 Cysteine desulfurase P0A6B7 ISCS_ECOLI iscS http://ecmdb.ca/proteins/P0A6B7.xml Siroheme synthase P0AEA8 CYSG_ECOLI cysG http://ecmdb.ca/proteins/P0AEA8.xml NAD(P)H-flavin reductase P0AEN1 FRE_ECOLI fre http://ecmdb.ca/proteins/P0AEN1.xml Ferrochelatase P23871 HEMH_ECOLI hemH http://ecmdb.ca/proteins/P23871.xml Blue copper oxidase cueO P36649 CUEO_ECOLI cueO http://ecmdb.ca/proteins/P36649.xml Ferric iron reductase protein fhuF P39405 FHUF_ECOLI fhuF http://ecmdb.ca/proteins/P39405.xml Lipoyl synthase P60716 LIPA_ECOLI lipA http://ecmdb.ca/proteins/P60716.xml Cysteine desulfurase_ P77444 SUFS_ECOLI sufS http://ecmdb.ca/proteins/P77444.xml Probable ATP-dependent transporter sufC P77499 SUFC_ECOLI sufC http://ecmdb.ca/proteins/P77499.xml Ferrous iron transport protein B P33650 FEOB_ECOLI feoB http://ecmdb.ca/proteins/P33650.xml FeS cluster assembly protein sufB P77522 SUFB_ECOLI sufB http://ecmdb.ca/proteins/P77522.xml Protein cyaY P27838 CYAY_ECOLI cyaY http://ecmdb.ca/proteins/P27838.xml NifU-like protein P0ACD4 NIFU_ECOLI nifU http://ecmdb.ca/proteins/P0ACD4.xml Cysteine desulfuration protein sufE P76194 SUFE_ECOLI sufE http://ecmdb.ca/proteins/P76194.xml FeS cluster assembly protein sufD P77689 SUFD_ECOLI sufD http://ecmdb.ca/proteins/P77689.xml Regulator of cell morphogenesis and NO signaling P69506 RCMNS_ECOLI ytfE http://ecmdb.ca/proteins/P69506.xml ferritin iron storage protein (cytoplasmic) P0A998 ftnA http://ecmdb.ca/proteins/P0A998.xml Bacterioferritin P0ABD3 BFR_ECOLI bfr http://ecmdb.ca/proteins/P0ABD3.xml Uncharacterized protein yqjH Q46871 YQJH_ECOLI yqjH http://ecmdb.ca/proteins/Q46871.xml Probable ATP-dependent transporter sufC P77499 SUFC_ECOLI sufC http://ecmdb.ca/proteins/P77499.xml Zinc transporter zupT P0A8H3 ZUPT_ECOLI zupT http://ecmdb.ca/proteins/P0A8H3.xml Putative ferrous iron permease efeU P75901 EFEU_ECOLI efeU http://ecmdb.ca/proteins/P75901.xml Ferrous iron transport protein B P33650 FEOB_ECOLI feoB http://ecmdb.ca/proteins/P33650.xml Manganese transport protein mntH P0A769 MNTH_ECOLI mntH http://ecmdb.ca/proteins/P0A769.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Ferrous-iron efflux pump fieF P69380 FIEF_ECOLI fieF http://ecmdb.ca/proteins/P69380.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD scaffold complex + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with bound [2Fe-2S] cluster +2 SufSE sulfur acceptor complex Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD with bound [2Fe-2S] cluster + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with two bound [2Fe-2S] clusters +2 SufSE sulfur acceptor complex FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU scaffold protein > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with bound [2Fe-2S] cluster FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU with bound [2Fe-2S] cluster > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with two bound [2Fe-2S] clusters 4 Iron + 4 Hydrogen ion + Oxygen >4 Fe3+ +2 Water Iron + Protoporphyrin IX >2 Hydrogen ion + Heme PROTOHEMEFERROCHELAT-RXN [4Fe-4S] iron-sulfur cluster + 2 S-Adenosylmethionine + Hydrogen ion + NAD + octanoate (protein bound) > [2Fe-2S] iron-sulfur cluster +2 5'-Deoxyadenosine +2 Iron + lipoate (protein bound) +2 L-Methionine + NADH Iron + Sirohydrochlorin >3 Hydrogen ion + Siroheme SIROHEME-FERROCHELAT-RXN Adenosine triphosphate + Water + Iron > ADP + Iron + Hydrogen ion + Phosphate Adenosine triphosphate + Water + Iron > ADP + Iron + Hydrogen ion + Phosphate FADH2 + 2 Fe3+ > FAD +2 Iron +2 Hydrogen ion [3Fe-4S] damaged iron-sulfur cluster + Iron > [4Fe-4S] iron-sulfur cluster FADH2 + 2 Ferroxamine > FAD +2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion 2 Ferroxamine + FMNH >2 Iron +2 ferroxamine minus Fe(3) + Flavin Mononucleotide +2 Hydrogen ion 2 Ferroxamine + Reduced riboflavin >2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion + Riboflavin Hydrogen ion + Hydrogen peroxide + Iron > hydroxyl radical + OH- + Fe3+ RXN-12540 Oxygen + Iron > Superoxide anion + Fe3+ RXN-12541 Hydrogen ion + Heme Protoporphyrin IX + Iron RXN0-6258 Iron + Protoporphyrin IX > Heme + Hydrogen ion PROTOHEMEFERROCHELAT-RXN Iron + Hydrogen ion + Oxygen > Fe3+ + Water RXN0-1483 Iron + a siderophore + NADP < an Fe(III)-siderophore + NADPH + Hydrogen ion RXN0-6555 Iron + (2,3-dihydroxybenzoylserine)3 + NADP < ferric 2,3-dihydroxybenzoylserine + NADPH + Hydrogen ion RXN0-6941 Sirohydrochlorin + Iron <> Hydrogen ion + Siroheme SIROHEME-FERROCHELAT-RXN Siroheme + 2 Hydrogen ion > Sirohydrochlorin + Iron 2 Iron + Hydrogen peroxide + 2 Hydrogen ion >2 Fe3+ +2 Water Heme + 2 Hydrogen ion > Protoporphyrin IX + Iron 2 Iron + 2 an apo-siderophore + NADP + Hydrogen ion >2 an Fe(III)-siderophore + NADPH Protoporphyrin IX + Iron >2 Hydrogen ion + ferroheme b PW_R003486 Sirohydrochlorin + Iron >2 Hydrogen ion + Siroheme PW_R003492 18000.0 uM 0.0 K-12 72000000 0 1. Cybercell Database: <a href='http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi'>http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi</a> 2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.