STRINGSTRING
ispDF protein (Maritimibacter alkaliphilus) - STRING interaction network
"ispDF" - Bifunctional enzyme IspD/IspF in Maritimibacter alkaliphilus
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ispDFBifunctional enzyme IspD/IspF ; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF) (376 aa)    
Predicted Functional Partners:
dxr
2-C-methyl-D-erythritol 4-phosphate synthase ; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) (399 aa)
 
  0.998
ispE
4-(cytidine-5’-diphospho)-2-C-methyl-D-erythritol kinase ; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (265 aa)
 
 
  0.993
ispG
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase ; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (377 aa)
 
 
  0.987
RB2654_12999
Uroporphyrin-III C-methyltransferase-like ; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD- dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme (476 aa)
         
  0.961
RB2654_03194
Putative competence-damaged inducible protein (156 aa)
   
   
  0.937
RB2654_03199
Phosphatidylglycerolphosphate phosphatase A ; Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (163 aa)
         
  0.928
ispH
4-hydroxy-3-methylbut-2-enyl diphosphate reductase ; Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) (322 aa)
 
   
  0.926
RB2654_10393
DNA polymerase I (932 aa)
   
   
  0.918
murC
UDP-N-acetylmuramoyl-L-alanine synthetase ; Cell wall formation (467 aa)
     
 
  0.916
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 [...] (846 aa)
         
  0.913
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
Server load: low (6%) [HD]