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
phhAPhenylalanine 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. (587 aa)    
Predicted Functional Partners:
pcbD
Pterin-4-alpha-carbinolamine dehydratase is involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. It catalyzes the the dehydration of 4a-hydroxytetrahydrobiopterins. Localized in the cytoplasm; High confidence in function and specificity.
  
 0.980
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.
   
 0.914
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.
     
 0.908
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.
     
 0.908
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.
   
 
 0.908
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.
   
 
 0.908
pheA
Prephenate 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.
     
 0.908
dfrA
Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
     
 0.900
hmgA
Catalytic activity: Homogentisate + O2 = 4-maleylacetoacetate. Tyrosine metabolism and Styrene degradation; High confidence in function and specificity.
 
  
 0.858
menF
The isochorismate synthase, called also isochorismate mutase catalyses the conversion of chorismate to isochorismate, the first step in the biosynthesis of both respiratory chain components: menaquinone (MK, vitamin K2) and phylloquinone (vitamin K1); Localized in the cytoplasm; High confidence in function and specificity.
     
  0.800
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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