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
AMG69400.1Formate dehydrogenase subunit alpha; Selenocysteine-containing polypeptide; hydrogen linked formate dehydrogenase which catalyzes the oxidation of formate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (722 aa)    
Predicted Functional Partners:
hycE
Hydrogenase 3 large subunit; Formate hydrogenlyase subunit 5; HycBCDEFG is part of the formate hydrogenlyase system which is involved in the cleaving of formate to dihydrogen and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.961
cysJ
Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
    
 0.903
AMG70393.1
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
 
 
 0.802
AMG72174.1
Sulfite reductase; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
    
 0.796
nuoE
NADH dehydrogenase; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.794
AMG68914.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.790
mobA
Molybdenum cofactor guanylyltransferase; Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor; Belongs to the MobA family.
 
  
 0.767
AMG68924.1
With YgfM and YgfN forms a selenate reductase, which seems to catalyze the reduction of selenate to selenite; YgfK mutants are unable to reduce selenate; involved in purine salvage process; seems to act as an oxidoreductase, but sequence similarity suggests it is a dihydrothymine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.765
fdhD
Sufurtransferase FdhD; Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. Belongs to the FdhD family.
 
 
 0.758
nuoB-2
Hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.713
Your Current Organism:
Morganella morganii
NCBI taxonomy Id: 582
Other names: ATCC 25830, ATCC 8076H, Bacillus morgani, CCUG 6328, CIP 103763, CIP A231, DSM 30164, IFO 3848, LMG 7874, LMG:7874, M. morganii, NBRC 3848, NCCB 73065, NCIB 235, NCIB:235, NCTC 235, Organism N 1, Proteus morganii, Salmonella morgani
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