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
Ping_1973PFAM: short-chain dehydrogenase/reductase SDR; KEGG: son:SO2935 short chain dehydrogenase. (245 aa)    
Predicted Functional Partners:
pfaC
Polyunsaturated fatty acid synthase PfaC; PFAM: beta-ketoacyl synthase; Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase, FabA/FabZ; KEGG: cps:CPS_3102 polyunsaturated fatty acid synthase PfaC; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
  
 
 0.843
Ping_0213
cob(I)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
 
    0.629
Ping_2837
PFAM: Carbamoyl-phosphate synthase L chain, ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; KEGG: son:SO0840 acetyl-CoA carboxylase multifunctional enzyme accADC, carboxyl transferase subunit alpha/carboxyl transferase subunit beta/biotin carboxylase.
  
 
 0.614
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
 
 
 
 0.609
Ping_1972
Inner membrane peptidase, Serine peptidase, MEROPS family S49; PFAM: peptidase S49; Peptidase S49, N-terminal domain protein; KEGG: cps:CPS_1193 SohB protein, peptidase U7 family.
       0.596
Ping_3552
1-phosphofructokinase; PFAM: PfkB domain protein; KEGG: ppr:PBPRA1574 putative 1-phosphofructokinase; Belongs to the carbohydrate kinase PfkB family.
   
  
 0.592
Ping_0398
PFAM: RDD domain containing protein; KEGG: ppr:PBPRA0490 hypothetical protein.
  
     0.585
lacZ
Beta-galactosidase; PFAM: glycoside hydrolase, family 42, domain 5, loop region; glycoside hydrolase family 2, immunoglobulin domain protein beta-sandwich; glycoside hydrolase family 2, TIM barrel; glycoside hydrolase family 2, sugar binding; KEGG: vvy:VVA0165 beta-galactosidase; Belongs to the glycosyl hydrolase 2 family.
  
  
 0.551
Ping_2604
PFAM: Enoyl-CoA hydratase/isomerase; 3-hydroxyacyl-CoA dehydrogenase domain protein; 3-hydroxyacyl-CoA dehydrogenase, NAD-binding; KEGG: bba:Bd1836 fatty oxidation complex, alpha subunit.
 
 0.536
paaN
TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: aldehyde dehydrogenase; MaoC domain protein dehydratase; KEGG: ecj:JW1382 fused aldehyde dehydrogenase and enoyl-CoA hydratase.
  
 0.514
Your Current Organism:
Psychromonas ingrahamii
NCBI taxonomy Id: 357804
Other names: P. ingrahamii 37, Psychromonas ingrahamii 37, Psychromonas ingrahamii str. 37, Psychromonas ingrahamii strain 37, gas vacuolate str. 37
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