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
AFZ46196.1Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. (360 aa)    
Predicted Functional Partners:
AFZ46033.1
PFAM: Lumazine binding domain; TIGRFAM: riboflavin synthase, alpha subunit; COGs: COG0307 Riboflavin synthase alpha chain; InterPro IPR001783; KEGG: cyc:PCC7424_0243 riboflavin synthase subunit alpha; PFAM: Lumazine-binding protein; PRIAM: Riboflavin synthase; SPTR: Similar to A3IMV7_9CHRO Riboflavin synthase subunit alpha; TIGRFAM: riboflavin synthase, alpha subunit.
  
 0.999
ribBA
GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
 0.999
ribH
6,7-dimethyl-8-ribityllumazine 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.
 
 
 0.989
AFZ46938.1
FMN adenylyltransferase; PFAM: Riboflavin kinase; FAD synthetase; TIGRFAM: riboflavin kinase/FMN adenylyltransferase; COGs: COG0196 FAD synthase; InterPro IPR002606:IPR015864:IPR015865; KEGG: cyh:Cyan8802_2123 riboflavin biosynthesis protein RibF; PFAM: Riboflavin kinase; FAD synthetase; SPTR: Riboflavin biosynthesis protein RibF; TIGRFAM: riboflavin biosynthesis protein RibF; Belongs to the ribF family.
  
  
 0.858
AFZ47998.1
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.839
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
     
 0.833
nadE
NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
  
  
 0.823
moaA
GTP cyclohydrolase subunit MoaA; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate.
    
 0.711
AFZ47307.1
PFAM: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK); TIGRFAM: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; COGs: COG0801 7 8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; InterPro IPR000550; KEGG: cyt:cce_2591 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; PFAM: 78-dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; PRIAM:2-amino-4-hydroxy-6-hydroxymethyldihydropteri dinediphosphokinase; SPTR:2-amino-4-hydroxy-6-hydroxymethyldihydropterid inepyrophosphokinase; TIGRFAM:2-amino-4-hydroxy-6-hydroxymethyldihydropte ridinepyrop [...]
  
  
 0.681
AFZ48641.1
Dihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin.
  
  
 0.679
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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