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
nudBNUDIX pyrophosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (147 aa)    
Predicted Functional Partners:
ARA75244.1
6-carboxytetrahydropterin synthase QueD; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
  0.915
folE
GTP cyclohydrolase I FolE; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.911
ARA74644.1
Alkaline phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the alkaline phosphatase family.
     
 0.903
folX
Dihydroneopterin triphosphate 2'-epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.901
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
   0.901
ARA76670.1
YebC/PmpR family DNA-binding transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.882
nnrD
Bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase; 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 [...]
  
 0.796
ruvC
Crossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
  
  
 0.617
birA
Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
   
    0.570
rnr
Ribonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. Belongs to the RNR ribonuclease family. RNase R subfamily.
   
 0.498
Your Current Organism:
Pectobacterium brasiliense
NCBI taxonomy Id: 180957
Other names: CFBP 6617, Erwinia carotovora subsp. brasiliensis, LMG 21371, LMG:21371, NCPPB 4609, P. brasiliense, Pectobacterium brasiliense Portier et al. 2019, Pectobacterium brasiliensis, Pectobacterium carotovorum subsp. brasiliense, Pectobacterium carotovorum subsp. brasiliensis, strain 212
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