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
bioAAdenosylmethionine-8-amino-7-oxononanoate aminotransferase; 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. (436 aa)    
Predicted Functional Partners:
bioF
8-amino-7-oxononanoate synthase; 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.
 
 
 0.999
bioD
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.
 
 
 0.999
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.
  
 0.997
ML1463
Possible NAD synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
   
 
 0.861
birA
Biotin apo-protein ligase; Similar to Mycobacterium tuberculosis birA OR RV3279C OR MTCY71.19C TR:P96884 (EMBL:Z92771) fasta scores: E(): 0, 71.2% id in 271 aa, and to Escherichia coli birA bifunctional protein [includes: biotin operon repressor; biotin--[acetyl-coa-carboxylase] synthetase birA OR bioR OR dhbB SW:BIRA_ECOLI (P06709) fasta scores: E(): 2e-10, 31.3% id in 256 aa. Lacks the N-terminal helix-turn-helix domain, so may not act as a repressor. Contains Pfam match to entry PF01317 BPL, Biotin protein ligase.
     
 0.718
panC
Putative pantoate-[beta]-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family.
   
  
 0.678
ML1612
Similar in parts to many proposed signal peptidases e.g. Bacillus subtilis SW:LEPT_BACSU (P71013) (193 aa); Fasta score E(): 1.1e-07, 31.0% identity in 226 aa overlap and Mycobacterium tuberculosis RV2903C SW:LEP_MYCTU (Q1078) (294 aa); Fasta score E(): 0, 69.8% identity in 301 aa overlap. Contains a possible membrane spanning hydrophobic domain. Contains 2 Pfam matches to entry PF00461 Peptidase_S26, Signal peptidase I. Contains PS00501 Signal peptidases I serine active site. Contains PS00761 Signal peptidases I signature 3.
     
 0.579
prcB
Proteasome [beta]-type subunit 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.
      
 0.488
aceA
Isocitrate lyase; Involved in the persistence and virulence of Mycobacterium. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
      
 0.481
ribA
Putative 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.
   
  
 0.472
Your Current Organism:
Mycobacterium leprae
NCBI taxonomy Id: 272631
Other names: M. leprae TN, Mycobacterium leprae TN, Mycobacterium leprae str. TN, Mycobacterium leprae strain TN
Server load: medium (52%) [HD]