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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AKB64242.1Tetrahydromethanopterin S-methyltransferase subunit A 1. (172 aa)    
Predicted Functional Partners:
AKB64241.1
Tetrahydromethanopterin S-methyltransferase subunit H.
 
 0.999
mer
5,10-methylenetetrahydromethanopterin reductase; Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT; Belongs to the mer family.
 
  
 0.986
mtrE
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.967
mtrD
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.958
mtrB
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.958
mtrC
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.957
mtrH
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.951
mtrG
N5-methyltetrahydromethanopterin:coenzyme M 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.
 
 0.944
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.
     
 0.913
fae-hps
Formaldehyde activating enzyme; Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10- methylenetetrahydromethanopterin; In the N-terminal section; belongs to the formaldehyde- activating enzyme family.
     
 0.904
Your Current Organism:
Methanosarcina mazei
NCBI taxonomy Id: 213585
Other names: M. mazei S-6, Methanosarcina mazei S-6
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.