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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
betBBetaine aldehyde dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. (490 aa)    
Predicted Functional Partners:
betA
Choline dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate.
 
 
 0.984
betI
Transcriptional regulator, TetR family; Repressor involved in the biosynthesis of the osmoprotectant glycine betaine. It represses transcription of the choline transporter BetT and the genes of BetAB involved in the synthesis of glycine betaine (By similarity).
  
 0.894
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
    
 0.859
PC1_0578
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; phosphopantetheine-binding; condensation domain protein; KEGG: rso:RS05859 peptide synthetase protein; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.534
PC1_0698
TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: eca:ECA0824 pyruvate-flavodoxin oxidoreductase.
  
 
 0.511
PC1_2163
KEGG: eca:ECA2142 UreA amidolyase; TIGRFAM: urea carboxylase; urea amidolyase related protein; PFAM: Allophanate hydrolase subunit 2; Carbamoyl-phosphate synthase L chain ATP-binding; biotin carboxylase domain protein; Allophanate hydrolase subunit 1; biotin/lipoyl attachment domain-containing protein; Carbamoyl-phosphate synthetase large chain domain protein; SMART: Allophanate hydrolase subunit 2; Allophanate hydrolase subunit 1.
  
  
 0.460
PC1_2553
PFAM: protein of unknown function DUF533; KEGG: eca:ECA1747 hypothetical protein.
       0.452
acs
acetate/CoA ligase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
  
 
 0.451
PC1_0299
PFAM: ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein; glutamate synthase; glutamine amidotransferase class-II; KEGG: eca:ECA0312 glutamate synthase subunit alpha.
  
  
 0.450
PC1_1343
PFAM: Myo-inositol catabolism IolB domain protein; KEGG: eca:ECA1465 hypothetical protein.
  
  
 0.443
Your Current Organism:
Pectobacterium carotovorum
NCBI taxonomy Id: 561230
Other names: P. carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum str. PC1, Pectobacterium carotovorum subsp. carotovorum strain PC1
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