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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[Homology]
Score
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (424 aa)    
Predicted Functional Partners:
hemL
Similar to Escherichia coli glutamate-1-semialdehyde 2,1-aminomutase HemL or Gsa or PopC or B0154 SW:GSA_ECOLI (P23893) (426 aa) fasta scores: E(): 6.9e-94, 60.094% id in 426 aa, and to Neisseria meningitidis glutamate-1-semialdehyde 2,1-aminomutase HemL or Nma0592 SW:GSA_NEIMA (Q9JW10) (427 aa) fasta scores: E(): 3.1e-105, 65.808% id in 427 aa.
 
 0.989
HemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.
  
 0.980
gltX
glutamyl-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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
     
 0.934
hemB
Similar to Pseudomonas aeruginosa delta-aminolevulinic acid dehydratase HemB or Pa5243 SW:HEM2_PSEAE (Q59643) (337 aa) fasta scores: E(): 1.2e-78, 65.15% id in 330 aa, and to Neisseria meningitidis delta-aminolevulinic acid dehydratase NMB0801 TR:Q9K025 (EMBL:AE002433) (333 aa) fasta scores: E(): 2.1e-86, 71.77% id in 326 aa; Belongs to the ALAD family.
 
  
 0.883
cysG
Siroheme synthase; 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.
 
  
 0.878
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
  
 0.817
hemK
Heme biosynthesis protein; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.
     
 0.729
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
  
 0.723
atpE
ATP synthase c chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
 
   
 0.722
glnB
Similar to many nitrogen regulatory proteins e.g. Rhodobacter sphaeroides P-II SW:GLNB_RHOSH () (112 aa) fasta scores: E(): 8.4e-31, 76.78% id in 112 aa; Belongs to the P(II) protein family.
   
  
 0.691
Your Current Organism:
Bordetella pertussis
NCBI taxonomy Id: 257313
Other names: B. pertussis Tohama I, Bordetella pertussis Tohama I
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