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
APA96176.1Prolyl aminopeptidase; KEGG: alu:BB31_19135 proline iminopeptidase. (142 aa)    
Predicted Functional Partners:
APA98505.1
F420H(2)-dependent quinone reductase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of menadione to menadio; since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidat [...]
  
     0.724
APA97135.1
Prolyl aminopeptidase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. Since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be the endogenous menaquinone found in the memb [...]
  
     0.718
APB01446.1
Prolyl aminopeptidase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of both benzoquinone and naphthoquinone analog; since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2 [...]
  
     0.709
APA97021.1
F420H(2)-dependent quinone reductase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of menadione to menadio; since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidat [...]
  
     0.649
APA97129.1
Prolyl aminopeptidase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. Since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidation is therefore likely to be the endogenous menaquinone found in the memb [...]
  
     0.642
APA94526.1
Hypothetical protein.
  
     0.564
cofD
2-phospho-L-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.
 
   
 0.529
APA97480.1
F420H(2)-dependent quinone reductase; Involved in a F420-dependent anti-oxidant mechanism that protects M. tuberculosis against oxidative stress and bactericidal agents. Catalyzes the F420H(2)-dependent two-electron reduction of quinones to dihydroquinones, thereby preventing the formation of cytotoxic semiquinones obtained by the one-electron reduction pathway. In vitro, catalyzes the reduction of menadione to menadio; since menaquinone is the sole quinone electron carrier in the respiratory chain in M. tuberculosis, the physiological electron acceptor for Fqr-mediated F420H(2) oxidat [...]
  
     0.520
APB01042.1
KEGG: ype:YPO0589 2,4-dienoyl-CoA reductase (NADPH2).
  
 0.500
cofE
Coenzyme F420-0:L-glutamate ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0.
 
   
 0.486
Your Current Organism:
Nocardia seriolae
NCBI taxonomy Id: 37332
Other names: ATCC 43993, CCUG 46828, CIP 104778, DSM 44129, IFO 15557, JCM 3360, N. seriolae, NBRC 15557
Server load: low (20%) [HD]