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
nudLNUDIX hydrolase; Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. (192 aa)    
Predicted Functional Partners:
ADO48236.1
KEGG: kpe:KPK_1965 aminodeoxychorismate synthase, component I; TIGRFAM: para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding-like; Anthranilate synthase component I domain protein.
     
 0.839
birA
Bifunctional BirA, biotin operon repressor/biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.608
nnrE
Carbohydrate kinase, YjeF related protein; 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-specific NAD(P)H-hydrate dehydratase to allow t [...]
  
 0.582
ADO48237.1
PFAM: protein of unknown function UPF0181; KEGG: sdy:SDY_1717 hypothetical protein; Belongs to the UPF0181 family.
       0.558
ADO48234.1
TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
    0.538
nudC
NAD(+) diphosphatase; KEGG: ssn:SSON_4169 NADH pyrophosphatase; PFAM: NUDIX hydrolase; NADH pyrophosphatase-like; Zinc ribbon NADH pyrophosphatase; Belongs to the Nudix hydrolase family. NudC subfamily.
 
   
 0.451
nudJ
PFAM: NUDIX hydrolase; KEGG: enc:ECL_02500 NUDIX hydrolase; Belongs to the Nudix hydrolase family. NudJ subfamily.
 
  
 0.446
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
Server load: low (14%) [HD]