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
sthAPyridine nucleotide transhydrogenase; Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (466 aa)    
Predicted Functional Partners:
AMG69221.1
Dihydrolipoamide succinyltransferase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 0.944
aceF
Pyruvate dehydrogenase complex dihydrolipoyllysine-residue acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 0.940
nadE
NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
    
 0.919
pntA
NAD(P) transhydrogenase subunit alpha; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the AlaDH/PNT family.
     
 0.915
pntB
NAD(P) transhydrogenase subunit beta; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the PNT beta subunit family.
     
 0.914
cobB
NAD-dependent deacylase; Modulates the activities of several enzymes which are inactive in their acetylated form; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sirtuin family. Class III subfamily.
  
 0.912
mazG
Nucleoside triphosphate hydrolase; Functions in degradation of stringent response intracellular messenger ppGpp; in Escherichia coli this gene is co-transcribed with the toxin/antitoxin genes mazEF; activity of MazG is inhibited by MazEF in vitro; ppGpp inhibits mazEF expression; MazG thus works in limiting the toxic activity of the MazF toxin induced during starvation; MazG also interacts with the GTPase protein Era; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.906
ppnK
NAD(+) kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
     
 0.906
nudC
NADH pyrophosphatase; Can catalyze hydrolysis of broad range of dinucleotide pyrophosphates but prefers reduced form of NADH; requires divalent metal ions such as magnesium and manganese and produces two mononucleoside 5'-phosphates; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Nudix hydrolase family. NudC subfamily.
     
 0.902
nadD
Nicotinate-nicotinamide nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
     
 0.900
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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