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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
DIP2247Putative amidase; Similar to Rhodococcus sp enantiomerase-selective amidase AmdA TR:Q53116 (EMBL:M74531) (462 aa) fasta scores: E(): 6.2e-15, 30.19% id in 414 aa, and to Mycobacterium smegmatis nicotinamidase/pyrazinamidase PzaA TR:Q9ZHK8 (EMBL:AF058285) (468 aa) fasta scores: E(): 6.4e-14, 30.55% id in 360 aa, and to Rhodococcus erythropolis amidase AmdA SW:AMID_RHOER (P22984) (520 aa) fasta scores: E(): 2.8e-11, 33.61% id in 238 aa; Belongs to the amidase family. (401 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA(Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 
 0.983
gatC
glutamyl-tRNA(Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 
 0.956
DIP2248
Similar to Streptomyces coelicolor putative integral membrane protein SC10A9.14c TR:Q9AK90 (EMBL:AL583943) (275 aa) fasta scores: E(): 1.6e-17, 41.12% id in 248 aa.
       0.836
pheA
Prephenate dehydratase; Similar to Corynebacterium glutamicum prephenate dehydratase PheA SW:PHEA_CORGL (P10341) (315 aa) fasta scores: E(): 8.6e-50, 52.75% id in 290 aa, and to Streptomyces coelicolor prephenate dehydratase SCD78.29c TR:Q9ZBX0 (EMBL:AL034355) (310 aa) fasta scores: E(): 6.4e-31, 39.63% id in 270 aa.
  
  
 0.714
DIP2245
Similar to Mycobacterium leprae putative phosphoglycerate mutase ML0079 TR:Q9CDC3 (EMBL:AL583917) (231 aa) fasta scores: E(): 4e-11, 33.64% id in 214 aa, and to Schizosaccharomyces pombe phosphoglycerate mutase Gpm1 or SPAC26F1.06 SW:PMGY_SCHPO (P36623) (211 aa) fasta scores: E(): 0.28, 24.4% id in 209 aa.
       0.661
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 
 0.564
DIP1504
Putative phospholipid biosynthesis; Similar to Mycobacterium tuberculosis phosphatidate cytidylyltransferase CdsA or Rv2881c or MT2948 or MTCY274.12c SW:CDSA_MYCTU (Q10807) (306 aa) fasta scores: E(): 2.4e-51, 51.73% id in 288 aa, and to Escherichia coli phosphatidate cytidylyltransferase CdsA or Cds or B0175 or Z0186 or ECS0177 SW:CDSA_ECOLI (P06466) (249 aa) fasta scores: E(): 1.9e-14, 35.35% id in 198 aa; Belongs to the CDS family.
  
    0.540
gluQ
Putative glutamyl-tRNA synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
  
 
 0.487
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
  
 
 0.487
pyrB
Similar to Mycobacterium leprae aspartate carbamoyltransferase PyrB or ML0532 SWALL:PYRB_MYCLE (SWALL:Q9CCR5) (321 aa) fasta scores: E(): 5.4e-79, 66.98% id in 312 aa, and to Bacillus subtilis aspartate carbamoyltransferase PyrB SWALL:PYRB_BACSU (SWALL:P05654) (304 aa) fasta scores: E(): 3.2e-32, 39.53% id in 301 aa; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
  
    0.484
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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