STRINGSTRING
psd psd pssA pssA recA recA pgsA pgsA DVU_0724 DVU_0724 DVU_2978 DVU_2978 carA carA DVU_1386 DVU_1386 DVU_3308 DVU_3308 polA polA nnrD nnrD
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
psdPhosphatidylserine decarboxylase-related protein; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). (217 aa)    
Predicted Functional Partners:
pssA
CDP-diacylglycerol--serine O-phosphatidyltransferase; Identified by match to protein family HMM PF01066; match to protein family HMM TIGR00473; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
 
 0.995
recA
recA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
 
  
 0.780
pgsA
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Identified by match to protein family HMM PF01066; match to protein family HMM TIGR00560; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
 
 0.678
DVU_0724
Identified by match to protein family HMM PF01235; match to protein family HMM TIGR00835.
 
    0.645
DVU_2978
Hydrolase, haloacid dehalogenase-like family; Identified by similarity to OMNI:NTL02EC4785; match to protein family HMM PF00702.
   
 
 0.607
carA
Carbamoyl-phosphate synthase, small subunit; Identified by similarity to SP:P25993; match to protein family HMM PF00117; match to protein family HMM PF00988; match to protein family HMM TIGR01368.
   
    0.542
DVU_1386
Membrane protein, putative.
     
 0.495
DVU_3308
Identified by match to protein family HMM PF00753; Belongs to the UPF0173 family.
  
 
 0.485
polA
DNA polymerase I; Identified by similarity to SP:P00582; match to protein family HMM PF00476; match to protein family HMM PF01367; match to protein family HMM PF02739; match to protein family HMM TIGR00593.
  
  
 0.475
nnrD
YjeF-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...]
  
    0.474
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.