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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[Homology]
Score
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (429 aa)    
Predicted Functional Partners:
folD
Methylenetetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate.
  
 0.989
purH
Similar to Mycobacterium tuberculosis bifunctional purine biosynthesis protein PurH [includes: phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3); IMP cyclohydorlase (EC 3.5.4.10)] or Rv0957 or MT0984 or MTCY10D7.17c SW:PUR9_MYCTU (P71553) (523 aa) fasta scores: E(): 1e-137, 68.06% id in 526 aa, and to Escherichia coli bifunctional purine biosynthesis protein [includes: phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3); IMP cyclohydrolase (EC 3.5.4.10)] PurH or B4006 SW:PUR9_ECOLI (P15639) (529 aa) fasta scores: E(): 1e-58, 45.25% id in 537 aa.
  
 0.988
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
 
 0.978
purN
5'-phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
  
 0.973
fhs
Formyltetrahydrofolate synthetase; Similar to Staphylococcus aureus (strain N315) formyltetrahydrofolate synthetase Fhs or SA1553 or SAV1732 SWALL:Q99TD2 (EMBL:AP003134) (555 aa) fasta scores: E(): 1.2e-125, 59.34% id in 551 aa, and to Moorella thermoacetica formate--tetrahydrofolate ligase Fhs SWALL:FTHS_MOOTH (SWALL:P21164) (559 aa) fasta scores: E(): 4.9e-116, 55.57% id in 556 aa.
  
 0.972
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
     
 0.969
DIP2130
Full length similarity to Streptococcus pneumoniae phosphoribosylformylglycinamidine synthase, putative SP0045 TR:AAK74234 (EMBL:AE007322) (1241 aa) fasta scores: E(): 7.8e-167, 47.73% id in 1259 aa. Second two thirds similar to many others e.g. Mycobacterium tuberculosis phosphoribosylformylglycinamidine synthase II PurL or Rv0803 or MT0823 or MTCY07H7A.06c SW:PURL_MYCTU (P54876) (754 aa) fasta scores: E(): 8.3e-22, 26.35% id in 740 aa.
  
  
 0.965
sdaA
L-serine dehydratase 1; Similar to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SW:SDHL_ECOLI (P16095) (454 aa) fasta scores: E(): 4.8e-113, 63.08% id in 447 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
 
 0.959
ilvA
Threonine dehydratase biosynthetic; 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.
     
 0.959
sdaB
L-serine dehydratase; Similar to Pseudomonas aeruginosa L-serine dehydratase SdaB or PA5379 SWALL:Q9HTI5 (EMBL:AE004950) (458 aa) fasta scores: E(): 3.5e-84, 53.99% id in 463 aa, and to Escherichia coli L-serine dehydratase 1 SdaA or B1814 SWALL:SDHL_ECOLI (SWALL:P16095) (454 aa) fasta scores: E(): 3e-70, 49.24% id in 461 aa; Belongs to the iron-sulfur dependent L-serine dehydratase family.
  
 
 0.956
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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