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
ACV24014.1KEGG: dat:HRM2_45740 GlnA2; TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp. (448 aa)    
Predicted Functional Partners:
carA
TIGRFAM: carbamoyl-phosphate synthase, small subunit; PFAM: Carbamoyl-phosphate synthase small chain; glutamine amidotransferase class-I; KEGG: sfu:Sfum_0009 carbamoyl phosphate synthase small subunit; Belongs to the CarA family.
  
 
 0.973
nifH
Nitrogenase iron protein; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein; Belongs to the NifH/BchL/ChlL family.
  
 
 0.967
ACV24138.1
TIGRFAM: asparagine synthase (glutamine-hydrolyzing); PFAM: asparagine synthase; glutamine amidotransferase class-II; KEGG: wbr:WGLp587 asparagine synthetase B.
  
  
 0.961
ACV23847.1
PFAM: MGS domain protein; Carbamoyl-phosphate synthase L chain ATP-binding; ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; protein of unknown function DUF201; phosphoribosylglycinamide synthetase; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; KEGG: dal:Dalk_3481 carbamoyl-phosphate synthase, large subunit.
  
 0.956
ACV23848.1
PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; KEGG: dal:Dalk_3481 carbamoyl-phosphate synthase, large subunit.
  
 0.956
glmS
Glucosamine/fructose-6-phosphate aminotransferase, isomerizing; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
 
 
 0.944
ACV24428.1
PFAM: nitrogen regulatory protein P-II; KEGG: abu:Abu_0198 nitrogen regulatory protein PII; Belongs to the P(II) protein family.
  
 
 0.944
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
  
 
 0.931
purQ
Phosphoribosylformylglycinamidine synthase I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist i [...]
 
  
 0.926
hcp
Hybrid cluster protein; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
    
 0.919
Your Current Organism:
Methanocaldococcus fervens
NCBI taxonomy Id: 573064
Other names: M. fervens AG86, Methanocaldococcus fervens AG86, Methanocaldococcus fervens DSM 4213, Methanocaldococcus fervens str. AG86, Methanocaldococcus fervens strain AG86
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.