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
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[Homology]
Score
CAZ96431.1N-formylkynurenine (aryl-) formamidase is an enzyme involved in the tryptophan metabolism. It hydrolyses the N-formyl-L-kynurenine to L-kynurenine and formate; belongs to the cyclase family; Localized in the cytoplasm; High confidence in function and specificity. (250 aa)    
Predicted Functional Partners:
kynU
Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively.
 
 
 0.986
tdoA2
Tryptophan 2,3-dioxygenase is Involved in L-kynurenine metabolism from L-tryptophan,incorporating oxygen into the indole moiety of tryptophan. It has a broad specificity towards tryptamine and derivatives including D-and L-tryptophan, 5-hydroxytryptophan and serotonin; This enzyme forms a tetramer and binds 2 hemes per subunit; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.973
tdoA1
Tryptophan 2,3-dioxygenase is Involved in L-kynurenine metabolism from L-tryptophan,incorporating oxygen into the indole moiety of tryptophan. It has a broad specificity towards tryptamine and derivatives including D-and L-tryptophan, 5-hydroxytryptophan and serotonin; This enzyme forms a tetramer and binds 2 hemes per subunit; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.972
kmoA
Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid; Belongs to the aromatic-ring hydroxylase family. KMO subfamily.
 
  
 0.955
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.
     
  0.900
pycA
Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
     
 0.802
pckA2
Phosphoenolpyruvate carboxykinase [ATP]; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
     
  0.800
pckA1
Phosphoenolpyruvate carboxykinase [ATP]; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
     
  0.800
CAZ96433.1
Conserved hypothetical protein; Protein with an uncleaved signal peptide; Seems localized in the cytoplasmic membrane.
       0.800
maeB
Bifunctional protein: Malic enzyme (N-terminal domain, 1 to 550) and Phosphate acetyl/butaryl transferase (C-terminal domain, 550 to 765); 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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