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
comCMalate dehydrogenase; Catalyzes the reduction of sulfopyruvate to (R)-sulfolactate much more efficiently than the reverse reaction. Also catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and to a much lower extent, KHTCA, but not pyruvate. Involved in the biosynthesis of both coenzyme M (with (R)-sulfolactate) and methanopterin (with alpha- ketoglutarate). (344 aa)    
Predicted Functional Partners:
comB
Conserved hypothetical protein; Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)- phospholactate and (S)-phosphoglycerate.
     
 0.992
mdh
L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily.
    
 0.990
endA
tRNA intron endonuclease (endA); Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp.
       0.931
comA
Conserved hypothetical protein; Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL).
     
 0.895
MJ_1426
Inosine-5'-monophosphate dehydrogenase, (guaB); Similar to GP:1001427 percent identity: 38.93; identified by sequence similarity; putative.
  
    0.787
thrC
Threonine synthase (thrC); Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.
     
 0.761
MJ_1428
O-linked GlnNAc transferase; Similar to GB:AE000666 percent identity: 34.08; identified by sequence similarity; putative.
  
  
 0.563
htpX
Heat shock protein HtpX, possibly protease (htpX); Similar to GB:M58470 SP:P23894 PID:146412 GB:U00096 PID:1736470 percent identity: 34.96; identified by sequence similarity; putative; Belongs to the peptidase M48B family.
     
 0.552
MJ_1427
Hypothetical protein; Catalyzes the condensation of 4-aminobenzoate (pABA) with 5- phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta- ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
       0.542
herA
Conserved hypothetical protein; Involved in DNA double-strand break (DSB) repair (By similarity). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (By similarity); Belongs to the HerA family.
       0.528
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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