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
cutDPutative pyruvate formate-lyase activating enzyme; Catalyzes activation of the choline trimethylamine-lyase CutC under anaerobic conditions by generation of an organic free radical on a glycine residue, via an homolytic cleavage of S-adenosyl-L-methionine (SAM). (316 aa)    
Predicted Functional Partners:
nuoC
NADH-quinone oxidoreductase chain C/D; 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 N-terminal section; belongs to the complex I 30 kDa subunit family.
  
 0.998
cutC-2
Putative formate acetyltransferase; Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde. Belongs to the glycyl radical enzyme (GRE) family. CutC subfamily.
 
  
 0.976
ECA0824
Similar to Rhodospirillum rubrum pyruvate-flavodoxin oxidoreductase NifJ SWALL:NIFJ_RHORU (SWALL:Q53046) (1191 aa) fasta scores: E(): 0, 54.73% id in 1182 aa, and to Escherichia coli probable pyruvate-flavodoxin oxidoreductase ydbk or b1378 SWALL:NIFJ_ECOLI (SWALL:P52647) (1174 aa) fasta scores: E(): 0, 78.79% id in 1174 aa. Also similar to ECA2957 (47.377% id. in 1182 aa overlap).
  
 
 0.967
hyfG
Similar to Escherichia coli hydrogenase-4 component G HyfG or b2487 SWALL:HYFG_ECOLI (SWALL:P77329) (555 aa) fasta scores: E(): 3.1e-128, 78.03% id in 569 aa.
  
 
 0.954
pflB
Similar to Escherichia coli formate acetyltransferase 1 PflB or Pfl or b0903 SWALL:PFLB_ECOLI (SWALL:P09373) (759 aa) fasta scores: E(): 0, 91.3% id in 759 aa.
 
  
 0.950
cfa6
Similar to Pseudomonas syringae type I polyketide synthase Cfa6 SWALL:Q9Z3T9 (EMBL:AF098795) (2731 aa) fasta scores: E(): 0, 60.14% id in 2725 aa, and to Polyangium cellulosum Soraphen polyketide synthase A SorA SWALL:Q9ADL6 (EMBL:U24241) (6315 aa) fasta scores: E(): 0, 43.21% id in 2277 aa.
  
 0.926
nuoE
NADH-quinone oxidoreductase chain E; Similar to Escherichia coli, Escherichia coli O6, and Shigella flexneri NADH-quinone oxidoreductase chain E NuoE or b2285 or c2826 or sf2361 SWALL:NUOE_ECOLI (SWALL:P33601) (166 aa) fasta scores: E(): 2.7e-53, 84.27% id in 159 aa.
  
 0.891
adhE
Aldehyde-alcohol dehydrogenase; Similar to Escherichia coli, and Escherichia coli O157:H7 aldehyde-alcohol dehydrogenase [includes: alcohol dehydrogenase, acetaldehyde dehydrogenase, and pyruvate-formate-lyase deactivase AdhE or Ana or b1241 or z2016 or ecs1741 SWALL:ADHE_ECOLI (SWALL:P17547) (890 aa) fasta scores: E(): 0, 89.1% id in 890 aa; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
 
  
 0.888
nuoF
NADH-quinone oxidoreductase chain F; 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.
  
 0.887
nuoB
NADH-quinone oxidoreductase chain B; 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.
  
 0.883
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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