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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
CYA_1380Conserved hypothetical protein; Identified by similarity to GB:BAC09114.1. (174 aa)    
Predicted Functional Partners:
ubiA
4-hydroxybenzoate polyprenyl transferase; Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of plastoquinone-9 (PQ-9) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 4-hydroxy-3-solanesylbenzoate. Belongs to the UbiA prenyltransferase family.
    
 0.912
CYA_2455
Isochorismate synthase; Identified by match to protein family HMM PF00425; match to protein family HMM TIGR00543.
     
 0.906
trpE
Anthranilate synthase component I; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...]
    
 0.827
tyrA
Prephenate dehydrogenase; Identified by similarity to SP:P20692; match to protein family HMM PF02153; match to protein family HMM PF02254; match to protein family HMM PF02558; match to protein family HMM PF03446; match to protein family HMM PF03807.
     
 0.806
trpG
Anthranilate synthase component II; Identified by match to protein family HMM PF00117; match to protein family HMM TIGR00566.
    
 0.803
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
     
 0.802
aspC
Aspartate aminotransferase; Identified by similarity to SP:Q56232; match to protein family HMM PF00155.
     
  0.800
aroH
Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
     
  0.800
hisC
Histidinol-phosphate aminotransferase; Identified by match to protein family HMM PF00155; match to protein family HMM TIGR01141; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
     
  0.800
CYA_1384
Conserved hypothetical protein; Identified by similarity to GB:BAC09596.1.
 
     0.747
Your Current Organism:
Synechococcus sp. JA33Ab
NCBI taxonomy Id: 321327
Other names: Cyanobacteria bacterium Yellowstone A-Prime, S. sp. JA-3-3Ab, Synechococcus sp. JA-3-3Ab, Synechococcus sp. OS-type A str. JA-3-3Ab, Synechococcus sp. OS-type A strain JA-3-3Ab
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.