2.02012-05-31 14:48:35 -06002015-06-03 17:20:08 -0600ECMDB20516M2MDB001325Ferric coprogenFerric coprogen belongs to the class of Fatty Acid Esters. These are carboxylic ester derivatives of a fatty acid. (inferred from compound structure)Coprogen is involved in iron transportation. The FhuE protein of Escherichia coli functions as the receptor for ferric coprogen and ferric-rhodotorulic acid. (PMID 3032906) The fhuE gene of Escherichia coli encodes the FhuE protein, which is a receptor protein in the coprogen-mediated siderophore iron-transport system. (PMID 16502288) Removal of iron from coprogen, ferrichrome, and ferrioxamine B was significantly lower in fhuF mutants compared to the corresponding parental strains, which suggested that FhuF is involved in iron removal from these hydroxamate-type siderophores. (PMID 14756576) Insertional inactivation and gene replacement of both genes showed that while FhuD2 is involved in the transport of iron(III) in complex with ferrichrome, ferrioxamine B, aerobactin, and coprogen, FhuD1 shows a more limited substrate range, capable of only iron(III)-ferrichrome and iron(III)-ferrioxamine B transport in S. (PMID 11489851)CoprogenC35H53FeN6O13821.673821.302002945iron(3+) ion N-(1-{[(3Z)-4-{[3-(3,6-dihydroxy-5-{3-[(2Z)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]propyl}-2,5-dihydropyrazin-2-yl)propyl](oxido)carbamoyl}-3-methylbut-3-en-1-yl]oxy}-5-[(2E)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]-1-oxopentan-2-yl)ethanimidic acidiron(3+) ion N-(1-{[(3Z)-4-{[3-(3,6-dihydroxy-5-{3-[(2Z)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]propyl}-2,5-dihydropyrazin-2-yl)propyl](oxido)carbamoyl}-3-methylbut-3-en-1-yl]oxy}-5-[(2E)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]-1-oxopentan-2-yl)ethanimidic acid31418-71-0[Fe+3].[H]\C(=C(\C)CCO)C(=O)N([O-])CCCC(N=C(C)O)C(=O)OCC\C(C)=C(\[H])C(=O)N([O-])CCCC1N=C(O)C(CCCN([O-])C(=O)C(\[H])=C(\C)CCO)N=C1OInChI=1S/C35H53N6O13.Fe/c1-23(11-17-42)20-30(45)39(51)14-5-8-27-33(48)38-28(34(49)37-27)9-6-15-40(52)32(47)22-25(3)13-19-54-35(50)29(36-26(4)44)10-7-16-41(53)31(46)21-24(2)12-18-43;/h20-22,27-29,42-43H,5-19H2,1-4H3,(H,36,44)(H,37,49)(H,38,48);/q-3;+3/b23-20-,24-21+,25-22-;FQIVLXIUJLOKPL-QYOPVWIVSA-NCytosolExtra-organismPeriplasmlogp2.31logs-4.51solubility2.85e-02 g/llogp-0.32pka_strongest_acidic5.29pka_strongest_basic3.6iupaciron(3+) ion N-(1-{[(3Z)-4-{[3-(3,6-dihydroxy-5-{3-[(2Z)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]propyl}-2,5-dihydropyrazin-2-yl)propyl](oxido)carbamoyl}-3-methylbut-3-en-1-yl]oxy}-5-[(2E)-5-hydroxy-3-methyl-N-oxidopent-2-enamido]-1-oxopentan-2-yl)ethanimidic acidaverage_mass821.673mono_mass821.302002945smiles[Fe+3].[H]\C(=C(\C)CCO)C(=O)N([O-])CCCC(N=C(C)O)C(=O)OCC\C(C)=C(\[H])C(=O)N([O-])CCCC1N=C(O)C(CCCN([O-])C(=O)C(\[H])=C(\C)CCO)N=C1OformulaC35H53FeN6O13inchiInChI=1S/C35H53N6O13.Fe/c1-23(11-17-42)20-30(45)39(51)14-5-8-27-33(48)38-28(34(49)37-27)9-6-15-40(52)32(47)22-25(3)13-19-54-35(50)29(36-26(4)44)10-7-16-41(53)31(46)21-24(2)12-18-43;/h20-22,27-29,42-43H,5-19H2,1-4H3,(H,36,44)(H,37,49)(H,38,48);/q-3;+3/b23-20-,24-21+,25-22-;inchikeyFQIVLXIUJLOKPL-QYOPVWIVSA-Npolar_surface_area294.64refractivity194.4polarizability78.37rotatable_bond_count25acceptor_count15donor_count5physiological_charge1formal_charge0Specdb::NmrOneD287935Specdb::NmrOneD287936Specdb::NmrOneD287937Specdb::NmrOneD287938Specdb::NmrOneD287939Specdb::NmrOneD287940Specdb::NmrOneD287941Specdb::NmrOneD287942Specdb::NmrOneD287943Specdb::NmrOneD287944Specdb::NmrOneD287945Specdb::NmrOneD287946Specdb::NmrOneD287947Specdb::NmrOneD287948Specdb::NmrOneD287949Specdb::NmrOneD287950Specdb::NmrOneD287951Specdb::NmrOneD287952Specdb::NmrOneD287953Specdb::NmrOneD287954Specdb::MsMs1233772Specdb::MsMs1233773Specdb::MsMs1233774Specdb::MsMs1349272Specdb::MsMs1349273Specdb::MsMs134927464498894952560CPD0-621Keseler, 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-D590.21097882Matzanke, B. F., Anemuller, S., Schunemann, V., Trautwein, A. X., Hantke, K. (2004). "FhuF, part of a siderophore-reductase system." Biochemistry 43:1386-1392.14756576Cui, Y., Tu, R., Guan, Y., Ma, L., Chen, S. (2006). "Cloning, sequencing, and characterization of the Azospirillum brasilense fhuE gene." Curr Microbiol 52:169-177.16502288Sebulsky, M. T., Heinrichs, D. E. (2001). "Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus." J Bacteriol 183:4994-5000.11489851Yurtsever D. (2007). Fatty acid methyl ester profiling of Enterococcus and Esherichia coli for microbial source tracking. M.sc. Thesis. Villanova University: U.S.AIron(3+)-hydroxamate import ATP-binding protein fhuCP07821FHUC_ECOLIfhuChttp://ecmdb.ca/proteins/P07821.xmlIron(3+)-hydroxamate import system permease protein fhuBP06972FHUB_ECOLIfhuBhttp://ecmdb.ca/proteins/P06972.xmlIron(3+)-hydroxamate-binding protein fhuDP07822FHUD_ECOLIfhuDhttp://ecmdb.ca/proteins/P07822.xmlIron(3+)-hydroxamate import ATP-binding protein fhuCP07821FHUC_ECOLIfhuChttp://ecmdb.ca/proteins/P07821.xmlIron(3+)-hydroxamate import system permease protein fhuBP06972FHUB_ECOLIfhuBhttp://ecmdb.ca/proteins/P06972.xmlFhuE receptorP16869FHUE_ECOLIfhuEhttp://ecmdb.ca/proteins/P16869.xmlBiopolymer transport protein exbBP0ABU7EXBB_ECOLIexbBhttp://ecmdb.ca/proteins/P0ABU7.xmlBiopolymer transport protein exbDP0ABV2EXBD_ECOLIexbDhttp://ecmdb.ca/proteins/P0ABV2.xmlProtein tonBP02929TONB_ECOLItonBhttp://ecmdb.ca/proteins/P02929.xmlIron(3+)-hydroxamate-binding protein fhuDP07822FHUD_ECOLIfhuDhttp://ecmdb.ca/proteins/P07822.xmlAdenosine triphosphate + Water + Ferric coprogen > ADP + Ferric coprogen + Hydrogen ion + PhosphateAdenosine triphosphate + Water + Ferric coprogen > ADP + Ferric coprogen + Hydrogen ion + Phosphatecoprogen unloaded (no Fe(III)) + Fe3+ > Ferric coprogen