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
Your Input:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
glmMPhosphoglucosamine mutase (glmM/femD); Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family. (452 aa)    
Predicted Functional Partners:
glmU
UDP-N-acetylglucosamine pyrophosphorylase (glmU); 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.
 
  
 0.978
glmS
Glucosamine--fructose-6-phosphate aminotransferase (glmS); Psort: bacterial inner membrane --- Certainty= 0.200(Affirmative); COG0449 GlmS glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains.
 
 
 0.971
lipB
Lipoate-protein ligase B (lipB); Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
       0.664
murC
UDP-N-acetylmuramate-alanine ligase (murC); Cell wall formation; Belongs to the MurCDEF family.
   
 
 0.641
guaB
Inosine monophosphate dehydrogenase (guaB); Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
    
 0.631
folP
Dihydropteroate synthase (folP); Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
  
  
 0.609
groEL
60 kD chaperonin (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
     
 0.578
ftsH
Cell division protein (ftsH); Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
  
  
 0.574
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase (murA); Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily.
  
  
 0.572
nifS-2
Putative cystine defulfurase (nifS-like protein); Duplicated gene; Similar to AMF_489; psort: bacterial inner membrane --- Certainty= 0.119(Affirmative); COG1104 cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes.
     
 0.556
Your Current Organism:
Anaplasma marginale
NCBI taxonomy Id: 320483
Other names: A. marginale str. Florida, Anaplasma marginale str. Florida, Anaplasma marginale strain Florida
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