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
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Gene Fusion
Cooccurrence
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[Homology]
Score
prsRibose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily. (317 aa)    
Predicted Functional Partners:
Rmag_0062
Transketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
   
 
 0.953
Rmag_0962
PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: ftl:FTL_0310 pyruvate dehydrogenase, E2 component.
   
 0.951
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
 0.941
rpiA
Ribose-5-phosphate isomerase; Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
  
 
 0.936
Rmag_0456
Phosphomannomutase; PFAM: phosphoglucomutase/phosphomannomutase C terminal; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II; phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain III; KEGG: noc:Noc_2994 phosphomannomutase.
  
 0.918
Rmag_0101
PFAM: NUDIX hydrolase; KEGG: noc:Noc_2420 NUDIX hydrolase.
     
  0.900
pyrE
Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
  
 
 0.875
hisG
ATP phosphoribosyltransferase (homohexameric); Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
  
 
 0.847
glmU
UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.
 
  
 0.819
hisZ
ATP phosphoribosyltransferase regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
    
 0.807
Your Current Organism:
Ruthia magnifica
NCBI taxonomy Id: 413404
Other names: C. Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica str. Cm (Calyptogena magnifica), Candidatus Ruthia magnifica strain Cm (Calyptogena magnifica), Ruthia magnifica str. Cm (Calyptogena magnifica)
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