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
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Gene Fusion
Cooccurrence
Coexpression
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[Homology]
Score
BirAPutative Biotin--acetyl-CoA-carboxylase ligase; Citation: Howard et al. (1985) Gene 35:321-331; Alternative locus ID: PMED4_04801. (249 aa)    
Predicted Functional Partners:
BioB
Biotin synthase; 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.
  
 
 0.936
accC,
acetyl-CoA carboxylase, biotin carboxylase subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
 
  
 0.919
accB,fabE
Biotin / Lipoyl attachment:Acetyl-CoA biotin carboxyl carrier subunit; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
   
 
 0.875
PMM0539
Biotin/lipoate A/B protein ligase family; Alternative locus ID: PMED4_05881.
  
  
 0.815
lipB
Putative lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
  
  
 0.806
BioD
Putative Dethiobiotin synthase; 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.
  
  
 0.688
BioA
Putative diaminopelargonic acid synthase; Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585; Kack et al. (1999) J. Mol. Biol. 291:857-876; Alternative locus ID: PMED4_16811; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
  
  
 0.675
bioF
Putative 8-amino-7-oxononanoate synthase; Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585; Alexeev et al. (1998) J. Mol. Biol. 284:401-419; Alternative locus ID: PMED4_16771.
  
  
 0.658
PMM0432
Conserved hypothetical protein; Alternative locus ID: PMED4_04791.
  
    0.652
ribA/ribB
Possible GTP cyclohydrolase II / 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
     
 0.556
Your Current Organism:
Prochlorococcus marinus pastoris
NCBI taxonomy Id: 59919
Other names: P. marinus subsp. pastoris str. CCMP1986, Prochlorococcus marinus MED4, Prochlorococcus marinus subsp. pastoris str. CCMP1378, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. CCMP1378, Prochlorococcus sp. MED4
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