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
ADZ08737.1PFAM: 4Fe-4S binding domain; KEGG: mth:MTH1736 formate hydrogenlyase, iron-sulfur subunit 2. (143 aa)    
Predicted Functional Partners:
ADZ08738.1
PFAM: 4Fe-4S binding domain; KEGG: mmg:MTBMA_c03120 HycB-related protein.
 
 
 
0.998
ADZ08739.1
KEGG: mth:MTH1738 pyruvate ferredoxin oxidoreductase subunit beta; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
  
 
 0.998
ADZ08740.1
KEGG: mmg:MTBMA_c03140 pyruvate synthase, subunit A; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal.
  
 
 0.997
ADZ08741.1
KEGG: mmg:MTBMA_c03150 pyruvate synthase, subunit D; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate; PFAM: 4Fe-4S binding domain.
  
 
  0.982
ADZ08742.1
TIGRFAM: 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate; KEGG: mth:MTH1740 pyruvate ferredoxin oxidoreductase subunit gamma/delta; PFAM: Pyruvate/ketoisovalerate oxidoreductase, catalytic domain.
  
 
  0.975
ADZ10728.1
TIGRFAM: Formate dehydrogenase, alpha subunit; PFAM: Molybdopterin oxidoreductase; Molybdopterin oxidoreductase, Fe4S4 domain; NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; Ferredoxin; 4Fe-4S binding domain; Molydopterin dinucleotide-binding domain; KEGG: mth:MTH1552 formate dehydrogenase, alpha subunit-like protein; SMART: Molybdopterin oxidoreductase, Fe4S4 domain; NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding.
 
  
 0.939
cdhC
CO dehydrogenase/acetyl-CoA synthase complex, beta subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex); Belongs to the CdhC family.
  
 
 0.926
cdhD
CO dehydrogenase/acetyl-CoA synthase, delta subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains the overall quaternary structure of the ACDS complex. Belongs to the CdhD family.
  
 
  0.922
cdhE
CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).
  
 
  0.922
cdhB
Acetyl-CoA decarbonylase/synthase complex subunit epsilon; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation. Belongs to the CdhB family.
  
 
  0.919
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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