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
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Textmining
[Homology]
Score
queEOrganic radical activating enzyme; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (210 aa)    
Predicted Functional Partners:
ptsA
6-Pyruvoyl tetrahydrobiopterin synthase catalyses the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin is the cofactor for several aromatic amino acid monooxygenases. The enzyme is a homohexameric, composed of a dimer of trimers. A transition metal binding site formed by the three histidine residues is present in each subunit, and bound Zn(II) is responsible for the enzymatic activity; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.986
pts
6-Pyruvoyl tetrahydrobiopterin synthase is involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. It catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin. It forms a homohexamer formed of two homotrimers in a head to head fashion. Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.979
rnrB2
The small subunit of the ribonucleoside-diphosphate reductase is a part of a complex which is an heterotetramer of two large and two small subunits. The complex catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides; Contains a N- terminal evolutionarily mobile, ATP-binding regulatory domain (ATP cone domain) which binds either ATP (activating) or dATP (inhibitory). Substrate binding to the ATP cone domain is thought to alter the relative positions of the two subunits of ribonucleoside- diphosphate reductase; Binds two iron ions by subunit; Localized [...]
  
 
 0.910
CAZ95357.1
Hypothetical protein that contains a N-terminal LuxE domain; Localized in the cytoplasm.
  
     0.659
CAZ98252.1
Conserved hypothetical protein; Localized in the cytoplasm.
  
   
 0.604
CAZ96731.1
Possible ATPase; Belongs to the DUF (domain of unknown function) 853 family; Localized in the cytoplasm; Family membership.
       0.530
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
     
 0.473
CAZ96730.1
Conserved hypothetical lipoprotein; Signal peptide of lipoprotein cleaved between the residues 16 and 17; Putatively localized in the outer membrane; Conserved hypothetical protein.
       0.472
purF
Amidophosphoribosyltransferase catalyzes the first step in purine biosynthesis: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. PurF belongs to the Class-II glutamine amidotransferase family. It forms a homotetramer and binds one magnesium ion per subunit. Localized in the cytoplasm; High confidence in function and specificity.
  
  
 0.441
rlmH
Conserved hypothetical protein; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family.
   
    0.438
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.