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
KML36891.1Riboflavin synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. (217 aa)    
Predicted Functional Partners:
KML36890.1
5-amino-6-(5-phosphoribosylamino)uracil reductase; 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.
 
 0.999
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase; 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; Belongs to the DMRL synthase family.
 
 0.999
KML43717.1
Riboflavin biosynthesis protein RibF; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ribF family.
 
 
 0.884
hisI
phosphoribosyl-ATP pyrophosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
  
    0.816
KML43198.1
PTS beta-glucoside transporter subunit IIBC; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.746
KML39855.1
CoA-disulfide reductase; CoADR; specific for coenzyme A disulfide; requires NADH; involved in protecting cells against reactive oxygen species by recycling coenzyme A disulfide which can reduce hydrogen peroxide; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
    0.746
KML45402.1
Pyruvate kinase; Catalyzes the formation of phosphoenolpyruvate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.708
rpmE2
RpmE2; there appears to be two types of ribosomal proteins L31 in bacterial genomes; some contain a CxxC motif while others do not; Bacillus subtilis has both types; the proteins in this cluster do not have the CXXC motif; RpmE is found in exponentially growing Bacilli while YtiA was found after exponential growth; expression of ytiA is controlled by a zinc-specific transcriptional repressor; RpmE contains one zinc ion and a CxxC motif is responsible for this binding; forms an RNP particle along with proteins L5, L18, and L25 and 5S rRNA; found crosslinked to L2 and L25 and EF-G; may b [...]
   
    0.686
rpmE
50S ribosomal protein L31; Binds the 23S rRNA.
   
    0.686
Your Current Organism:
Bacillus firmus
NCBI taxonomy Id: 1399
Other names: ATCC 14575, B. firmus, BCRC 11730, Bacillaceae bacterium HQ2, Bacillus sp. JP44SK20, Bacillus sp. LK28, Bacillus sp. NCIM 2264, Bacillus sp. NCIM 2462, CCM 2213, CCRC 11730, CCRC:11730, CCUG 7418, CIP 52.70, DSM 12, IAM 12464, IFO 15306, JCM 2512, LMG 7125, LMG:7125, NBRC 15306, NCAIM B.01087, NCCB 48015, NCIB 9366, NCIMB 9366, NCTC 10335, NRRL B-14307, NRRL NRS-613, VKM B-498
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