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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
ADL57715.1Predicted nitrogenase molybdenum-iron protein. (359 aa)    
Predicted Functional Partners:
murF
Predicted UDP-N-acetylmuramyl pentapeptide synthase.
 
  
 0.979
nifH2
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.
 
 0.978
nifH1
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.
 
 
 0.924
ADL57718.1
HypE-related protein.
 
     0.916
hisH
Predicted imidazole glycerol phosphate synthase, subunit H; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
       0.899
ADL57716.1
Predicted nucleotidyl transferase.
     
 0.868
ADL57719.1
Conserved hypothetical protein.
       0.779
mcrA
Methyl-coenzyme M reductase I, subunit alpha; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6- mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8- mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol compound such as CoA or CoM [...]
 
   
 0.769
mrtA
Methyl-coenzyme M reductase II, subunit alpha; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.
 
   
 0.768
mcrG
Methyl-coenzyme M reductase I, subunit gamma; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H- SOcoTP) nor any other thiol compound such as CoA or CoM [...]
 
   
 0.764
Your Current Organism:
Methanothermobacter marburgensis
NCBI taxonomy Id: 79929
Other names: M. marburgensis str. Marburg, Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133), Methanobacterium thermoautotrophicum str. Marburg, Methanothermobacter marburgensis str. Marburg, Methanothermobacter marburgensis strain Marburg
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