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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
eifTranslation initiation factor eIF-2B alpha subunit; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). (358 aa)    
Predicted Functional Partners:
fucA
L-fuculose phosphate aldolase(L-fuculose-1-phosphate aldolase). Involved in the fucose metabolism catalyzing the third step of the pathway, L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. 41% Aldolase_II_N.IPR004782; FucA. Pfam:PF00596; Aldolase_II; 1. TIGRFAMs:TIGR01086; fucA; 1; High confidence in function and specificity.
 
 
 0.984
azo1998
Purine-nucleoside phosphorylase; Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.
 
 
 0.979
metH
Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
   
  
 0.812
speE2
Probable spermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine; Belongs to the spermidine/spermine synthase family.
 
  
 0.734
rpe
Ribulose-phosphate 3-epimerase(also known as pentose-5-phosphate 3-epimerase, PPE or Rpe), is the enzyme that converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. 71%Ribul_P_3_epim. Pfam:PF00834; Ribul_P_3_epim; 1. TIGRFAMs:TIGR01163; rpe; 1; High confidence in function and specificity.
  
   0.697
ybdL
Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to trembl|Q8XXV2 (58%) and to sprot|YBDL_ECOLI (52%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding [...]
 
  
 0.671
azo1995
Conserved hypothetical protein; 41% Aldolase_II_N. Class II Aldolase and Adducin N-terminal domain Pfam: PF00596; Aldolase_II; 1. fucA: L-fuculose phosphate aldolase; High confidence in function and specificity.
  
 
 0.621
azo2608
Conserved hypothetical protein; 42% Aldolase_II_N.Class II Aldolase and Adducin N-terminal domain. Pfam: PF00596; Aldolase_II; 1. TIGR: PP2871; High confidence in function and specificity.
  
 
 0.621
pheA
Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity.
     
 0.577
ribH
Riboflavin synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
  
    0.532
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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