STRINGSTRING
STRING protein interaction network
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
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sidCNonribosomal peptide synthase sidC; Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway. Arthroderma benhamiae produces 2 types of extracellular siderophores, ferrichrome C and ferricrocin. The biosynthesis of these siderophores depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase sidA. The structure of ferricrocin differs from ferrichrome C only by a serine for alanine substitution and the assembly of both siderophores is suggested to be performed by the nonribosomal peptide synthase (NRPS) sidC. (5087 aa)    
Predicted Functional Partners:
ARB_00034
Histidine biosynthesis trifunctional protein.
   
  
 0.711
ARB_01246
Carrier domain-containing protein.
  
 0.643
ARB_06687
Multifunctional tryptophan biosynthesis protein; Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
      
 0.521
sidA
L-ornithine N(5)-monooxygenase; L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway. Arthroderma benhamiae produces 2 types of extracellular siderophores, ferrichrome C and ferricrocin. The biosynthesis of these siderophores depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase sidA. The structure of ferricrocin differs from ferrichrome C only by a serine for alanine substitution and the assembly of both siderophores is suggested to be performed by the nonribosomal peptide synthase (NRPS) sidC.
      
 0.483
ARB_06708
Siderophore biosynthesis acetylase AceI, putative.
     
 0.481
ARB_04996
Uncharacterized protein; Belongs to the membrane-bound acyltransferase family.
  
  
 0.465
ARB_04804
Tryptophan synthase.
  
  
 0.461
Your Current Organism:
Trichophyton benhamiae
NCBI taxonomy Id: 663331
Other names: Arthroderma benhamiae CBS 112371, T. benhamiae CBS 112371, Trichophyton benhamiae CBS 112371
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