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
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[Homology]
Score
gltBFerredoxin-dependent glutamate synthase,; Specificity unclear. (1557 aa)    
Predicted Functional Partners:
gltD
Glutamate synthase (small chain) oxidoreductase; Glutamate synthase [NADPH] precursor (EC 1.4.1.13) (NADPH-GOGAT)small chain. TREMBL:Q8XV67-77% identity, 87% similarity InterPro:IPR006005- One pathway for the assimilation of ammonia and glutamate biosynthesis involves glutamate synthase (EC: 1.4.1.13) which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ gid: gid protein Pfam:FAD binding domain,Thi family, 4Fe-4S binding domain,KTN-NAD binding domain, DUF127; High confidence [...]
 0.999
glxD
Glutamate synthase, large subunit. Similar to sprot|GLXD_RHIME (87%). Glutamate synthase (GltS) is a complex iron-sulphur flavoprotein that catalyses the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the bacterial, yeast and plant pathways for ammonia assimilation. Pfam: Conserved region in glutamate synthase; Specificity unclear.
  
 0.982
boxA
Benzoyl-CoA oxygenase component A. 84% 4Fe4S_ferredoxin. IPR001709; FPN_cyt_redctse. IPR001433; Oxred_FAD/NAD(P). Pfam:PF00037; Fer4; 2. PF00175; NAD_binding_1; 1; High confidence in function and specificity.
  
 
 0.975
glxC
Probable protein GlxC. Similar to sprot|GLXC_RHIME (59%) and to pir|A96211 (51%). Pfam (PF01493): GXGXG; Family membership.
  
 0.968
carB
Carbamoyl-phosphate synthase (glutamine-hydrolyzing) large chain InterPro: Carbamoyl-phosphate synthase; High confidence in function and specificity; Belongs to the CarB family.
  
 
 0.964
azo2695
Conserved hypothetical protein. Homology to BF2580 of Bacteroides fragilis of 47% (gnl|keqq|bfr:BF2580(KEGG)). No domains predicted. No TMHs. No signal peptide.
  
 
 0.964
glnA
Glutamine synthetase I (GS) plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam (PF00120): Glutamine synthetase, catalytic domain Pfam (PF03951): Glutamine synthetase, beta-Grasp domain; High confidence in function and specificity.
  
 
 0.963
glnT
Glutamine synthetase III plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to trembl|Q98A06 (58%) and to sprot|GLN3_RHILP (38%). Pfam (PF03951): Glutamine synthetase, beta-Grasp domain Pfam(PF00120): Glutamine synthetase, catalytic domain; High confidence in function and specificity.
  
 
 0.963
argG
ArgG protein; Argininosuccinate synthase, argG. Similar to SWISSPROT:ASSY_NITEU (81%). Argininosuccinate synthase is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. InterPro (PF00764): Argininosuccinate synthase InterPro (TIGR00032): Argininosuccinate synthase; High confidence in function and specificity.
  
 
 0.960
nadE
NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
    
 0.959
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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