STRINGSTRING
entD entD entF entF entC entC entE entE entB entB entA entA ybdB ybdB menF menF
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
entDEnterobactin synthetase component D; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-fo [...] (209 aa)
entFATP-dependent serine activating enzyme (may be part of enterobactin synthase as component F); Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE) (By similarity); Belongs to the ATP-dependent AMP-binding enzyme f [...] (1293 aa)
entCIsochorismate hydroxymutase 2, enterochelin biosynthesis; Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate. (391 aa)
entE2,3-dihydroxybenzoate-AMP ligase; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate excha [...] (536 aa)
entB2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase; Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntB is a bifunctional protein that serves as an isochorismate lyase and an aryl carrier protein (ArCP). Catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), the precursor o [...] (285 aa)
entA2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase, enterochelin biosynthesis; Residues 1 to 248 of 248 are 99.19 pct identical to residues 1 to 248 of 248 from Escherichia coli K-12 Strain MG1655: B0596. (248 aa)
ybdBOrf, hypothetical protein; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Belongs to the thioesterase PaaI family. (137 aa)
menFIsochorismate hydroxymutase 2, menaquinone biosynthesis; Catalyzes the conversion of chorismate to isochorismate. (356 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
Server load: low (14%) [HD]