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
ddhNAD-dependent 2-hydroxyacid dehydrogenases are enzymes which seem to be specific for the D-isomer of their substrate. these enzymes are composed of a substrate-binding domain and a NAD-binding domain (Rossman fold); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity. (329 aa)    
Predicted Functional Partners:
ppsA
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family.
    
 0.967
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.
  
 0.940
pykA
Pyruvate kinase (PK) catalyzes the final step in glycolysis (Embden-Meyerhof pathway), the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP. PK forms a homotetramer and requires both magnesium and potassium ions for its activity. PK helps control the rate of glycolysis, along with phosphofructokinase and hexokinase. PK possesses allosteric sites for numerous effectors; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.932
lldD1
L-lactate dehydrogenase is involved in L-lactate degradation converting the L-lactate to pyruvate; Uses flavin mononucleotide (FMN) as prosthetic group; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.920
lldD2
L-lactate dehydrogenase is involved in L-lactate degradation converting the L-lactate to pyruvate; Uses flavin mononucleotide (FMN) as prosthetic group; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.920
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.
  
 0.915
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.
  
 0.915
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.
  
 0.915
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.
   
 
 0.908
gpmA
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.
    
 0.906
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
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.