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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
pheAPrephenate dehydratase catalyzes the decarboxylation of prephenate to phenylpyruvate. PheA is involved in L-phenylalanine biosynthesis. It features a C- terminal ACT domain. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Localized in the cytoplasm; High confidence in function and specificity. (275 aa)    
Predicted Functional Partners:
aroGH
Bifunctional enzyme including 3-deoxy-7-phosphoheptulonate synthase (DAHP synthase) in N-terminus and chorismate mutase in C-terminus. DAHP synthase catalyzes the first step in the common pathway leading to the biosynthesis of aromatic compounds, the stereospecific condensation of phosphoenolpyruvate and D-erythrose-4-phosphate giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Chorismate mutase catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. Localized in the cytoplasm; High confidence in function and speci [...]
 
 0.998
aatA-2
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.990
tyrA
Prephenate dehydrogenase is involved in tyrosine biosynthesis. It catalyzes the reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH. It uses NAD as a cofactor. Localized in the cytoplam; High confidence in function and specificity.
 
 
 0.988
hisC
The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.929
hisC2
The histidinol-phosphate aminotransferase catalyses the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily; Possibly exported in the periplasmic space by a twin-arginine signal peptide (cleavage site between 32 and 33); High confidence in function and specificity.
  
 
 0.919
aatB
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.912
CAZ94893.1
Aminotransferases use the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; Specificity unclear.
  
 0.910
phhA
Phenylalanine 4-monooxygenase, also known as phenylalanine-4-hydroxylase, is involved in L-phenylalanine biodegradation. It catalyzes the reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin. It binds Fe(2+) ion as a cofactor. PhhA belongs to the biopterin-dependent aromatic amino acid hydroxylase family. Localized in the cytoplasm; High confidence in function and specificity.
     
 0.908
tyrDC
Tyrosine decarboxylase catalyzes the reaction : L-tyrosine = tyramine + CO2. This enzyme covalently binds the cofactor pyridoxal-phosphate (PLP) on a conserved lysine. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.805
kdsB
The 3-Deoxy-manno-octulosonate cytidylyltransferase, also known as CMP-KDO synthetase, activates KDO (a 8-carbon sugar) required for incorporation into bacterial lipopolysaccharide in Gram- negative bacteria; It binds one magnesium ion as cofactor; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the KdsB family.
      0.783
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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