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hemE hemE hemN hemN hemG hemG hemC hemC hemD hemD hemY hemY cysG cysG hemF hemF hemA hemA hemH hemH cyoE cyoE hemB hemB hemL hemL
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa)
hemNO2-independent coproporphyrinogen III oxidase; Residues 1 to 459 of 459 are 99.78 pct identical to residues 1 to 459 of 459 from Escherichia coli K-12 Strain MG1655: B3867; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (459 aa)
hemGProtoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. (181 aa)
hemCPorphobilinogen deaminase = hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (320 aa)
hemDUroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. (246 aa)
hemYA late step of protoheme IX synthesis; Involved in a late step of protoheme IX synthesis. (398 aa)
cysGUroporphyrinogen III methylase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. (457 aa)
hemFCoproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. (299 aa)
hemAEnzyme in alternate path of synthesis of 5-aminolevulinate; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (418 aa)
hemHFerrochelatase: final enzyme of heme biosynthesis; Catalyzes the ferrous insertion into protoporphyrin IX. (320 aa)
cyoEProtoheme IX farnesyltransferase (haeme O biosynthesis); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (296 aa)
hemB5-aminolevulinate dehydratase = porphobilinogen synthase; Residues 1 to 335 of 335 are 99.10 pct identical to residues 1 to 335 of 335 from Escherichia coli K-12 Strain MG1655: B0369; Belongs to the ALAD family. (335 aa)
hemLGlutamate-1-semialdehyde aminotransferase (aminomutase); Residues 1 to 426 of 426 are 99.29 pct identical to residues 1 to 426 of 426 from Escherichia coli K-12 Strain MG1655: B0154. (426 aa)
Your Current Organism:
Escherichia coli O157H7 EDL933
NCBI taxonomy Id: 155864
Other names: E. coli O157:H7 str. EDL933, Escherichia coli O157:H7 EDL933, Escherichia coli O157:H7 str. EDL933, Escherichia coli O157:H7 strain EDL933
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