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:
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Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
ADO48520.1PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG: cro:ROD_35211 hypothetical protein. (150 aa)    
Predicted Functional Partners:
ADO48687.1
KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein.
  
  
 0.643
ADO48521.1
Methyltransferase type 12; KEGG: spe:Spro_1013 methyltransferase; PFAM: Methyltransferase type 12; SMART: Ribosomal RNA adenine methylase transferase-like.
       0.584
nuoC
NADH dehydrogenase I, D subunit; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
  
 0.540
ADO49351.1
KEGG: kva:Kvar_3643 succinate dehydrogenase, cytochrome b556 subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit; PFAM: succinate dehydrogenase cytochrome b subunit.
   
    0.509
birA
Bifunctional BirA, biotin operon repressor/biotin--acetyl-CoA-carboxylase ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.490
ADO47259.1
KEGG: ses:SARI_00124 formate hydrogenlyase complex iron-sulfur subunit.
   
    0.445
ADO47452.1
KEGG: kva:Kvar_1176 4Fe-4S ferredoxin iron-sulfur binding domain protein.
   
    0.445
nuoI
NADH-quinone oxidoreductase, chain I; 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.
   
    0.445
ADO47854.1
KEGG: ebi:EbC_44610 conserved uncharacterized protein.
  
    0.430
ADO48614.1
KEGG: pfs:PFLU2487 hypothetical protein.
  
    0.427
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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