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
moaDSimilar to Escherichia coli molybdopterin converting factor subunit 1 MoaD or ChlA4 or ChlM or b0784 SWALL:MOAD_ECOLI (SWALL:P30748) (81 aa) fasta scores: E(): 3.2e-19, 67.9% id in 81 aa. (81 aa)    
Predicted Functional Partners:
moaE
Similar to Escherichia coli molybdopterin converting factor subunit 2 MoaE or ChlA5 or b0785 SWALL:MOAE_ECOLI (SWALL:P30749) (149 aa) fasta scores: E(): 6.1e-45, 76.51% id in 149 aa.
 
 0.999
moeB
Similar to Escherichia coli molybdopterin biosynthesis protein MoeB or ChlN or b0826 SWALL:MOEB_ECOLI (SWALL:P12282) (249 aa) fasta scores: E(): 1.1e-66, 71.37% id in 248 aa.
  
 0.988
moaC
Molybdenum cofactor biosynthesis protein C; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family.
 
  
 0.987
moaB
Molybdenum cofactor biosynthesis protein B; May be involved in the biosynthesis of molybdopterin. Belongs to the MoaB/Mog family.
 
  
 0.927
moaA
Molybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate.
 
  
 0.916
moeA
Molybdopterin biosynthesis protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.
 
  
 0.822
thiG
Thiazole biosynthesis protein; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
   
 
 0.789
thiF
Thiamine biosynthesis adenylyltransferase; Similar to Escherichia coli adenylyltransferase ThiF or b3992 SWALL:THIF_ECOLI (SWALL:P30138) (251 aa) fasta scores: E(): 7e-59, 60.56% id in 246 aa.
  
 
 0.697
mog
Molybdopterin biosynthesis protein; Similar to Escherichia coli, Escherichia coli O157:H7, and Shigella flexneri molybdopterin biosynthesis Mog protein Mog or MogA or ChlG or b0009 or z0009 or ecs0009 or sf0010 SWALL:MOG_ECOLI (SWALL:P28694) (195 aa) fasta scores: E(): 2e-61, 85.12% id in 195 aa.
 
  
 0.640
gcvP
Putative glycine cleavage system P protein (glycine dehydrogenase [decarboxylating]); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
    0.615
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.