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
AKD99731.1LysR family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa)    
Predicted Functional Partners:
nuoC
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family.
   
 0.839
nuoI
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
   
 0.813
nuoD
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
  
 0.808
nqo6_2
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
   
 0.807
AKD97499.1
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
   
 0.800
AKD97500.1
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.
   
 0.782
AKD97501.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.743
AKD97493.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.729
nuoA
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family.
  
 0.718
nuoN
NADH-quinone oxidoreductase subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family.
  
 0.708
Your Current Organism:
Rhodococcus erythropolis
NCBI taxonomy Id: 1833
Other names: ATCC 4277, Arthrobacter hydrocarboglutamicus, Arthrobacter oxamicetus, Arthrobacter oxamicetus subsp. propiophenicolus, Arthrobacter paraffineus, Arthrobacter picolinophilus, Brevibacterium healii, Brevibacterium ketoglutamicum, Brevibacterium paraffinoliticum, CIP 104179, Corynebacterium alkanum, Corynebacterium aurantiacum, Corynebacterium humiferum, Corynebacterium sp. WS2071, Corynebacterium sp. WS2072, DSM 43066, IEGM 7, IFO 15567, JCM 20419, JCM 3201, LMG 5359, LMG:5359, Mycobacterium erythropolis, NBRC 15567, NCIB 11148, NCIB 9158, NCIB:11148, NCIB:9158, NCIMB 9158, NCTC 13021, NRRL B-16025, Nocardia calcarea, Nocardioides simplex ATCC 13260, Nocardioides simplex ATCC 19565, Nocardioides simplex ATCC 19566, R. erythropolis, Rhodococcus NI86/21, Rhodococcus sp. (strain NI86/21), Rhodococcus sp. ATCC 15108, Rhodococcus sp. ATCC 15961, Rhodococcus sp. ATCC 21035, Rhodococcus sp. BG43, Rhodococcus sp. BZ4, Rhodococcus sp. NCIB 9646, Rhodococcus sp. NI86/21, Rhodococcus sp. strain NI86/21, VKM Ac-858, strain N11
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