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
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Gene Fusion
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Coexpression
Experiments
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[Homology]
Score
pdxHPyridoxamine 5'-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (224 aa)    
Predicted Functional Partners:
pdxT
Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
    
 0.959
KIU17591.1
Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.875
pdxS
Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
    
 0.848
pdxS-2
Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
    
 0.848
KIU18709.1
MFS transporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.842
KIU14898.1
Phosphomethylpyrimidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.806
fgd
Glucose-6-phosphate dehydrogenase; Catalyzes the coenzyme F420-dependent oxidation of glucose 6- phosphate (G6P) to 6-phosphogluconolactone.
      
 0.787
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
     
 0.709
KIU18707.1
Citrate synthase 2; Forms citrate from oxaloacetate and acetyl-CoA; functions in TCA cycle; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the citrate synthase family.
 
   
 0.675
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 [...]
    
 0.650
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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