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:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
proBGlutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (385 aa)    
Predicted Functional Partners:
proA
Gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.
 
 0.999
proC
Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
 
 0.960
putA
Transcriptional regulator; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
    
 0.943
argD
Acetylornithine aminotransferase; DapATase; functions in arginine biosynthetic pathway; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
   
 0.886
obgE
GTPase Obg; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
 
  
 0.789
nnrD
Bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-spec [...]
 
 
   0.698
argA
N-acetylglutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the acetyltransferase family. ArgA subfamily.
 
   
 0.666
ribB
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; Belongs to the DHBP synthase family.
     
 0.624
ALO39824.1
Competence protein ComEC; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.619
atpH
ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
    
 0.617
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Achromobacter sp. ATCC8750, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
Server load: low (8%) [HD]