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
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Textmining
[Homology]
Score
bioBHypothetical protein; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (346 aa)    
Predicted Functional Partners:
bioD-2
Hypothetical protein; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family.
 
 
 0.999
bioD
Hypothetical protein; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Belongs to the dethiobiotin synthetase family.
 
 
 0.995
bioA
Hypothetical protein; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
  
 0.992
bioC
Hypothetical protein; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
 
  
 0.982
bioF
Hypothetical protein; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
  
 0.982
birA
Hypothetical protein; 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.
  
 
 0.948
CKO_05002
Hypothetical protein; KEGG: stm:STM3644 0. bisC; biotin sulfoxide reductase K08351; COG: COG0243 Anaerobic dehydrogenases, typically selenocysteine-containing; Psort location: Periplasmic, score:9.44; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
     
  0.900
CKO_04884
Hypothetical protein; KEGG: eca:ECA2053 6.6e-167 gabT, goaG; 4-aminobutyrate aminotransferase K00823:K07250; COG: COG0160 4-aminobutyrate aminotransferase and related aminotransferases; Psort location: Cytoplasmic, score:8.96; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
 
  
 0.874
kbl
Hypothetical protein; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
  
 0.872
thiC
Hypothetical protein; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
 
  
 0.632
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.