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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ADZ09300.1TIGRFAM: Bacterial carbamate kinase; KEGG: mem:Memar_0247 carbamate kinase; PFAM: Aspartate/glutamate/uridylate kinase; Belongs to the carbamate kinase family. (325 aa)    
Predicted Functional Partners:
ADZ08343.1
PFAM: Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain; Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding; TIGRFAM: Ornithine carbamoyltransferase; HAMAP: Ornithine carbamoyltransferase; KEGG: mfv:Mfer_0050 ornithine carbamoyltransferase; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
 
  
 0.958
ADZ10077.1
KEGG: cyj:Cyan7822_0613 glutamate--ammonia ligase; PFAM: Glutamine synthetase, catalytic domain.
     
 0.917
ADZ10697.1
TIGRFAM: Glutamine synthetase type I; KEGG: mth:MTH1570 glutamine synthetase; PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp.
     
 0.917
purQ
Phosphoribosylformylglycinamidine synthase 1; 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 [...]
    
  0.902
pyrB
PFAM: Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding; Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain; TIGRFAM: Aspartate carbamoyltransferase, eukaryotic; HAMAP: Aspartate carbamoyltransferase, eukaryotic; KEGG: mmg:MTBMA_c00020 aspartate carbamoyltransferase.
 
  
 0.894
carA
TIGRFAM: Carbamoyl-phosphate synthase, small subunit; KEGG: mmg:MTBMA_c13800 carbamoyl-phosphate synthase, small subunit; PFAM: Carbamoyl-phosphate synthase, small subunit, N-terminal; Glutamine amidotransferase class-I, C-terminal; Belongs to the CarA family.
    
 0.824
carB
SMART: Methylglyoxal synthase-like domain; TIGRFAM: Carbamoyl-phosphate synthase, large subunit; KEGG: mmg:MTBMA_c13790 carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthetase, large subunit, ATP-binding; Carbamoyl-phosphate synthase, large subunit, N-terminal; Carbamoyl-phosphate synthetase, large subunit, oligomerisation; Methylglyoxal synthase-like domain; Belongs to the CarB family.
    
 0.821
pyrI
Aspartate carbamoyltransferase regulatory chain; Involved in allosteric regulation of aspartate carbamoyltransferase.
    
 0.820
ADZ09301.1
KEGG: mfv:Mfer_1029 radical sam domain protein; PFAM: Radical SAM; SMART: Elongator protein 3/MiaB/NifB.
  
    0.503
argS
KEGG: mth:MTH1447 arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; HAMAP: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family.
     
 0.414
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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