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:
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Cooccurrence
Coexpression
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[Homology]
Score
mtrATetrahydromethanopterin S-methyltransferase subunit A; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step; Belongs to the MtrA family. (239 aa)    
Predicted Functional Partners:
ADZ08470.1
TIGRFAM: Coenzyme F420 hydrogenase, subunit alpha; KEGG: mth:MTH1300 coenzyme F420-reducing hydrogenase, alpha subunit; PFAM: Nickel-dependent hydrogenase, large subunit; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.
  
   
 0.999
ADZ08472.1
TIGRFAM: Coenzyme F420 hydrogenase, subunit gamma; KEGG: mmg:MTBMA_c16840 F420-reducing hydrogenase, subunit gamma; PFAM: NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 4Fe-4S binding domain.
  
  
 0.999
ADZ08570.1
TIGRFAM: Sulfopyruvate decarboxylase, beta subunit; KEGG: mmg:MTBMA_c15850 sulfopyruvate decarboxylase, beta subunit; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
      
 0.999
mtrE
Tetrahydromethanopterin S-methyltransferase subunit E; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 0.999
mtrD
Tetrahydromethanopterin S-methyltransferase subunit D; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 0.999
mtrC
Tetrahydromethanopterin S-methyltransferase, subunit C; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 0.999
mtrF
Tetrahydromethanopterin S-methyltransferase, F subunit; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
   
 0.999
mtrG
Tetrahydromethanopterin S-methyltransferase, subunit G; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 0.999
mtrH
Tetrahydromethanopterin S-methyltransferase subunit H; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. MtrH catalyzes the transfer of the methyl group from methyl-tetrahydromethanopterin to the corrinoid prosthetic group of MtrA.
 
 0.999
ADZ10722.1
KEGG: mru:mru_0344 tungsten formylmethanofuran dehydrogenase subunit A FwdA; TIGRFAM: Formylmethanofuran dehydrogenase, subunit A; PFAM: Amidohydrolase 3.
     
 0.999
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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