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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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. (241 aa)    
Predicted Functional Partners:
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
mtrB
Tetrahydromethanopterin S-methyltransferase subunit B; 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
ADI74852.1
TIGRFAM: tetrahydromethanopterin S-methyltransferase, MtrH subunit; KEGG: mbu:Mbur_1518 putative methyltransferase; PFAM: Tetrahydromethanopterin S-methyltransferase MtrH subunit.
 
 0.999
ADI74242.1
TIGRFAM: tetrahydromethanopterin S-methyltransferase, MtrH subunit; KEGG: mba:Mbar_A2072 putative methyltransferase; PFAM: Tetrahydromethanopterin S-methyltransferase MtrH subunit.
 
 0.997
mer
5,10-methylenetetrahydromethanopterin reductase; Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT; Belongs to the mer family.
 
  
 0.985
ftr
Formylmethanofuran/tetrahydromethanopterin N-formyltransferase; Catalyzes the reversible transfer of a formyl group from formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) so as to produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and methanofuran (MFR); Belongs to the FTR family.
     
 0.975
Your Current Organism:
Methanohalobium evestigatum
NCBI taxonomy Id: 644295
Other names: M. evestigatum Z-7303, Methanohalobium evestigatum Z-7303, Methanohalobium evestigatum str. Z-7303, Methanohalobium evestigatum strain Z-7303
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.