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.
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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
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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plsYProtein of unknown function DUF205; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. (220 aa)    
Predicted Functional Partners:
plsX
Fatty acid/phospholipid synthesis protein PlsX; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
 
  
 0.983
gpsA
PFAM: NAD-dependent glycerol-3-phosphate dehydrogenase domain protein; Ketopantoate reductase ApbA/PanE domain protein; KEGG: gbm:Gbem_0008 NAD-dependent glycerol-3- phosphate dehydrogenase domain protein.
 
 
 0.959
glpK
Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family.
    
 0.922
Plim_3130
Phospholipid/glycerol acyltransferase.
  
 
 0.918
secY
Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
      
 0.618
Plim_0719
PFAM: phospholipid/glycerol acyltransferase; SMART: phospholipid/glycerol acyltransferase; KEGG: pst:PSPTO_5540 acyltransferase, putative.
  
 
 0.590
Plim_0830
PFAM: protein of unknown function UPF0153; KEGG: bba:Bd0554 hypothetical protein.
       0.503
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 [...]
     
 0.475
Plim_1537
TIGRFAM: CDP-diacylglycerol/glycerol-3-phosphate 3- phosphatidyltransferase; PFAM: CDP-alcohol phosphatidyltransferase; KEGG: gur:Gura_2485 CDP-diacylglycerol--glycerol-3- phosphate 3-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
   
 0.456
Plim_2369
PFAM: AMP-dependent synthetase and ligase; phospholipid/glycerol acyltransferase; major facilitator superfamily MFS_1; SMART: phospholipid/glycerol acyltransferase; KEGG: aba:Acid345_4052 2-acyl-glycerophospho- ethanolamine acyltransferase.
  
  
 0.452
Your Current Organism:
Planctopirus limnophila
NCBI taxonomy Id: 521674
Other names: P. limnophila DSM 3776, Planctomyces limnophilus ATCC 43296, Planctomyces limnophilus DSM 3776, Planctomyces limnophilus str. DSM 3776, Planctomyces limnophilus strain DSM 3776, Planctopirus limnophila DSM 3776, Planctopirus limnophilus DSM 3776
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