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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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ribHRiboflavin synthase beta chain (ribH); 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. (141 aa)    
Predicted Functional Partners:
ribB
GTP cyclohydrolase II (ribA); Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
 
 
 0.999
ribC
Riboflavin synthase (ribC); Similar to GP:1419079 percent identity: 68.00; identified by sequence similarity; putative; Belongs to the DMRL synthase family.
 
  
 0.985
arfC
Riboflavin-specific deaminase (ribG); Catalyzes an early step in riboflavin biosynthesis, the NAD(P)H-dependent reduction of the ribose side chain of 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6- ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the authentic substrate, and the alpha anomer can serve as substrate subsequent to spontaneous anomerization. NADPH and NADH function equally well as the reductants. Does not catalyze the reduction of 5- amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D- ribitylamino)uracil; [...]
 
 
 0.953
hisE
phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphohydrolase (hisIE); Similar to SP:P06989 GB:D43637 GB:U02072 GB:X03974 PID:41700 percent identity: 30.43; identified by sequence similarity; putative.
  
    0.916
ribL
Glycerol-3-phosphate cytidyltransferase (taqD); Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3- phosphate cytidylyltransferase, as previously annotated in the complete gen [...]
     
 0.911
pyrD
Dihydroorotase dehydrogenase (pyrD); Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor; Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
  
  
 0.815
pyrB
Aspartate carbamoyltransferase catalytic chain (pyrB); Similar to GP:1572497 percent identity: 59.12; identified by sequence similarity; putative.
  
    0.792
rpl13
LSU ribosomal protein L13P (rplM); This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
    0.761
MJ_0959
Aspartate aminotransferase (aspC); Similar to PID:704449 GB:AE000666 percent identity: 54.69; identified by sequence similarity; putative.
     
 0.740
purE
Phosphoribosylaminoimidazole carboxylase, (purE); Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
     
 0.730
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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