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
CAZ98522.1Type III polyketide synthases are homodimeric enzymes that iteratively carry out the polyketide synthesis at one single active site; Belongs to the chalcone/stilbene synthase family; Localized in the cytoplasm; Specificity unclear. (351 aa)    
Predicted Functional Partners:
CAZ98524.1
Aromatic-ring hydroxylase, FAD-dependent oxidoreductase family; Aromatic-ring hydroxylases (or monooxygenases) catalyze the incorporation of one atom of dioxygen into an aromatic compound and the reduction of the other oxygen atom to water. These oxidoreductases are FAD-dependent and adopt a Rossmann fold; Belongs to the pyridine nucleotide-disulphide reductases superfamily; Localized in the cytoplasm; Specificity unclear.
 
  
 0.951
CAZ94457.1
Type I polyketide synthases are modular enzymes involved in the synthesis of various polyketides. This enzyme encompasses five modules: beta-ketoacyl synthase (KS), acyltransferase (AC), dehydratase (DH), enoyl reductase (ER) and acyl carrier protein (ACP). This modular enzyme is homologous to mycocerosic acid synthase (EC 2.3.1.111). Binds 1 phosphopantetheine group covalently. Localized in the cytoplasmic membrane; Specificity unclear.
 
 
 0.943
CAZ98523.1
Conserved hypothetical protein; Localized in the cytoplasm.
 
     0.940
acpP4
Acyl carrier protein (ACP) is the carrier of the growing fatty acid chain in fatty acid biosynthesis. ACP is produced as an apoprotein and is converted to its active form by [ACP]synthase (AcpS); Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.923
CAZ98521.1
Belongs to the short-chain dehydrogenases/reductases (SDR) family, Glucose/ribitol dehydrogenase subfamily; Most dehydrogenases possess at least 2 domains, the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis; Localized in the cytoplasm; Family membership.
 
 
 
 0.909
fabB7
3-oxoacyl-[acyl-carrier-protein] synthase, also known as beta-ketoacyl synthase, catalyzes the condensation reaction of fatty acid synthesis by the addition of two carbons from malonyl-ACP to an acyl acceptor. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids; Belongs to the Beta-ketoacyl synthase family; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
  
 0.889
CAZ96747.1
Metallo-beta-lactamase superfamily protein; Protein with a N-terminal metallo beta-lactamase domain and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site Cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue; binds two zinc ions per molecule as cofactor; Localized in the cytoplasm; Function unclear.
    
   0.871
CAZ94370.1
Conserved protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. contains various metallo-hydrolases including beta-lactamases, but also glyoxylases and arylsulfatases. The active site is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear.
    
   0.871
CAZ98563.1
Protein with a N-terminal domain belonging to the metallo-beta-lactamase superfamily and two rhodanese (thiosulfate sulfurtransferase) domains: one where the active-site cysteine residue is replaced by another aminoacid whereas the C-terminal domain displays the catalytic cysteine residue. The active site of the metallo-beta-lactamase domain is characterized by several conserved histidines binding the catalytic zinc ions. The enzymes can bind one or two zinc ions; Localized in the cytoplasm; Function unclear.
    
   0.871
CAZ95265.1
FAD-dependent amine oxidoreductase of unknown substrate specificity; Belongs to the amine oxydase family; Localized in the cytoplasm; Specificity unclear.
    
 
 0.839
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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