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
AFZ05387.1PFAM: Phosphoglycerate mutase family; COGs: COG0406 Fructose-2 6-bisphosphatase; InterPro IPR013078; KEGG: ter:Tery_2181 phosphoglycerate mutase; PFAM: Histidine phosphatase superfamily, clade-1; SMART: Histidine phosphatase superfamily, clade-1; SPTR: Phosphoglycerate mutase. (453 aa)    
Predicted Functional Partners:
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
    
 0.917
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
     
  0.900
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
     
  0.900
trpA
Tryptophan synthase, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
     
  0.900
AFZ08744.1
PFAM: Bacterial transferase hexapeptide (three repeats); COGs: COG1045 Serine acetyltransferase; InterPro IPR001451; KEGG: cyj:Cyan7822_3995 serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide repeat; SPTR: Bacterial transferase hexapeptide repeat protein.
     
  0.800
AFZ08746.1
Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (three repeats); COGs: COG1045 Serine acetyltransferase; InterPro IPR001451; KEGG: cyj:Cyan7822_1693 serine O-acetyltransferase; SPTR: Bacterial transferase hexapeptide repeat protein.
     
  0.800
AFZ08951.1
Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (three repeats); TIGRFAM: serine O-acetyltransferase; COGs: COG1045 Serine acetyltransferase; InterPro IPR001451:IPR005881; KEGG: ava:Ava_1668 serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide repeat; PRIAM: Serine O-acetyltransferase; SPTR: Serine O-acetyltransferase; TIGRFAM: Serine O-acetyltransferase.
     
  0.800
AFZ09632.1
Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (three repeats); TIGRFAM: serine O-acetyltransferase; COGs: COG1045 Serine acetyltransferase; InterPro IPR005881:IPR001451; KEGG: naz:Aazo_1129 serine O-acetyltransferase; PRIAM: Serine O-acetyltransferase; SPTR: Serine acetyltransferase; TIGRFAM: Serine O-acetyltransferase.
     
  0.800
AFZ05388.1
Dihydroorotase; PFAM: Amidohydrolase family; TIGRFAM: dihydroorotase, multifunctional complex type; COGs: COG0044 Dihydroorotase and related cyclic amidohydrolase; InterPro IPR006680:IPR004722; KEGG: ter:Tery_2179 dihydroorotase; PFAM: Amidohydrolase 1; SPTR: Dihydroorotase; TIGRFAM: Dihydroorotase.
       0.489
cobQ
Adenosylcobyric acid synthase (glutamine-hydrolysing); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
 
  
 0.460
Your Current Organism:
Oscillatoria nigroviridis
NCBI taxonomy Id: 179408
Other names: O. nigro-viridis PCC 7112, Oscillatoria nigro-viridis PCC 7112, Oscillatoria sp. PCC 7112
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