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
MCRY_00550Hypothetical protein; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (270 aa)    
Predicted Functional Partners:
MCRY_17655
Glutamate synthase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.819
MCRY_06225
3-hydroxyacyl-CoA dehydrogenase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.797
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
       0.773
MCRY_06780
Short-chain dehydrogenase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
  
  0.669
MCRY_00540
Membrane protein; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.645
MCRY_10405
Short-chain dehydrogenase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.621
ctaB
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
 
      0.587
MCRY_12180
Peptide synthetase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.582
MCRY_08300
enoyl-CoA hydratase; Bacteria available from JCM 15447. Source DNA available from JCM 15447; catalyzes the ring cleavage reaction in phenylacetate degradation and the formation of 3-hydroxyacyl-CoA from crotonyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.569
MCRY_10275
Cytochrome P450; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cytochrome P450 family.
  
 0.537
Your Current Organism:
Marivita cryptomonadis
NCBI taxonomy Id: 505252
Other names: JCM 15447, KCCM 90070, M. cryptomonadis, Marivita cryptomonadis Hwang et al. 2009, Rhodobacteraceae bacterium CL-SK44, strain CL-SK44
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