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
KIU16530.1NUDIX hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa)    
Predicted Functional Partners:
nnrE
Membrane protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers [...]
  
 0.981
KIU16529.1
F420-0--gamma-glutamyl ligase; Catalyzes the addition of gamma linked glutamate to 7,8-didemethyl-8-hydroxy-5-deazariboflavin coenzyme F420-0); Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.944
KIU16528.1
2-phospho-L-lactate transferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.893
KIU17326.1
DEAD/DEAH box helicase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the DEAD box helicase family.
    
 0.885
KIU16046.1
DEAD/DEAH box helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.885
deaD
Cold-shock protein; DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.
    
 0.885
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
   
 0.806
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
    
 0.790
nadE
NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
   
 0.757
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan.
   
 
 0.751
Your Current Organism:
Mycolicibacterium llatzerense
NCBI taxonomy Id: 280871
Other names: CCUG 54744, CECT 7273, DSM 45343, JCM 16229, M. llatzerense, Mycobacterium llatzerense, Mycobacterium llatzerense Gomila et al. 2008, Mycobacterium sp. 13-009-09768, Mycobacterium sp. MG12, Mycobacterium sp. MG13, Mycobacterium sp. MG14, Mycobacterium sp. MG15, Mycobacterium sp. MG16, Mycobacterium sp. MG18, Mycolicibacterium llatzerense (Gomila et al. 2008) Gupta et al. 2018, strain MG13
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