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
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[Homology]
Score
paaEPhenylacetic acid degradation NADH oxidoreductase; The protein PaaE is involved in the phenylacetic acid aerobic catabolism. It is likely part of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. It is activated by cAMP receptor protein (CRP) and the integration host factor (IHF). Contains a N-terminal FAD-binding domain, a central feredoxin-like NAD-binding domain and a C-terminal 2Fe-2S iron-sulfur cluster binding domain; Localized in the cytoplasm; High confidence in function and specificity. (349 aa)    
Predicted Functional Partners:
paaK
Phenylacetate-coenzyme A ligase catalyzes the activation of phenylacetic acid to phenylacetyl-CoA. It is the first step of the Phenylacetic acid aerobic catabolism; Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds; Activated by cAMP receptor protein (CRP); Contains an AMP binding motif; Localized in the cytoplasm; High confidence in function and specificity.
 
 
 0.949
CAZ95173.1
Coenzyme A ligase; Protein putatively involved in the exopolysaccharide biosynthesis; Localized in the cytoplasm; Function unclear.
 
 
 0.946
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.
  
 
 0.921
fdx
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. It binds two 4Fe-4S clusters; Localized in the cytoplasm; Function unclear.
  
 
 0.856
gltB
Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...]
   
 0.827
CAZ94684.1
This protein belongs to the MOSC (MOCO sulfurase C-terminal) family which encompasses beta-strand-rich domains identified in the molybdenum cofactor sulfurase. These MOSC domains contain an absolutely conserved cysteine and are predicted to be sulfur-carrier domains that receive sulfur abstracted by the pyridoxal phosphate- dependent NifS-like enzymes, on their conserved cysteine, and deliver it for the formation of diverse sulfur-metal clusters. Localized in the cytoplasm; Family membership.
    
 0.776
iscS
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules as thio-nucleosides in tRNA, thiamine, biotin, lipoate, molybdopterin and Fe-S cluster; Uses the Pyridoxal phosphate as prosthetic group linked to a lysine residue; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.773
cypA
Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics; P450 enzymes usually act as terminal oxidases in multicomponent electron transfer chains, called P450-containing monooxygenase systems; Acts with the ferredoxin and the ferredoxin reductase; Localized in the cytoplasm; Specificity unclear.
  
 0.719
CAZ95821.1
Transcriptional regulator belonging to the PadR family. Features a helix-turn-helix DNA binding motif. Localized in the cytoplasm; Specificity unclear.
     
 0.705
narB/nirB
Respiratory nitrate/nitrite reductase; Bifunctional enzyme involved in the denitrification processes (nitrate respiration). It contains in its N-terminal part a nitrate reductase module required for nitrate assimilation (reducing nitrate to nitrite) using molybdopterin and 1 4Fe-4S cluster as cofactors and in its C-terminal part a nitrite reductase module required for nitrite assimilation (reducing nitrite to ammonia) using FAD, 4Fe-4S cluster and siroheme as cofactors; Belongs to Belongs to the prokaryotic molybdopterin-containing oxidoreductase family and to the nitrite and sulfite r [...]
  
  
 0.681
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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