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hemL hemL hemH hemH cyoE cyoE hemB hemB phpB phpB CAR16833.1 CAR16833.1 cobU cobU cobS cobS cobT cobT uidA uidA hemA hemA btuR btuR gltX gltX hemF hemF eutT eutT hemC hemC hemD hemD hemX hemX hemN hemN hemG hemG bfr bfr cysG cysG hemE hemE
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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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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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hemLGlutamate-1-semialdehyde aminotransferase (aminomutase); Function experimentally demonstrated in the studied species; enzyme. (426 aa)
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. (320 aa)
cyoEProtoheme IX farnesyltransferase; 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)
hemBPorphobilinogen synthase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the ALAD family. (324 aa)
phpBPutative phosphatase with phosphoglycerate mutase domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the phosphoglycerate mutase family. (203 aa)
CAR16833.1Cob(I)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. (200 aa)
cobUBifunctional cobinamide kinase and cobinamide phosphate guanylyltransferase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate. (181 aa)
cobSCobalamin 5'-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. (247 aa)
cobTNicotinate-nucleotide dimethylbenzimidazole-P phophoribosyl transferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). Belongs to the CobT family. (359 aa)
uidAbeta-D-glucuronidase; Function experimentally demonstrated in the studied species; enzyme; Belongs to the glycosyl hydrolase 2 family. (603 aa)
hemAGlutamyl tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (418 aa)
btuRcob(I)alamin adenolsyltransferase/cobinamide ATP-dependent adenolsyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. (196 aa)
gltXglutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (471 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)
eutTPutative cobalamin adenosyltransferase in ethanolamine utilization; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (267 aa)
hemCHydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (313 aa)
hemDUroporphyrinogen III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. (246 aa)
hemXPutative uroporphyrinogen III methylase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (393 aa)
hemNCoproporphyrinogen III oxidase, SAM and NAD(P)H dependent, oxygen-independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
hemGProtoporphyrin oxidase, flavoprotein; Function experimentally demonstrated in the studied species; carrier. (181 aa)
bfrBacterioferritin, iron storage and detoxification protein; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (158 aa)
cysGFused siroheme synthase 1, 3-dimethyluroporphyriongen III dehydrogenase and siroheme ferrochelatase; 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)
hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (354 aa)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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