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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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racXAmino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...] (227 aa)    
Predicted Functional Partners:
pbpE
Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.
  
  
 0.997
cdoA
Cysteine dioxygenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
     
 0.954
yhdR
Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
     
 0.932
dat
D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...]
    
 0.916
aspB
Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
     
 0.907
cysK
Cysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
     
 0.903
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
    
  0.903
metC
Cystathionine beta-lyase; Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the trans-sulfuration enzymes family.
     
 0.901
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity).
    
  0.901
mccB
Cystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
     
 0.901
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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