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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
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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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Toce_1804Endoribonuclease L-PSP; COGs: COG0251 Putative translation initiation inhibitor yjgF family; InterPro IPR006056:IPR006175; KEGG: tit:Thit_1447 endoribonuclease L-PSP; PFAM: Endoribonuclease L-PSP; SPTR: Putative endoribonuclease L-PSP; TIGRFAM: endoribonuclease L-PSP; PFAM: Endoribonuclease L-PSP; TIGRFAM: endoribonuclease L-PSP, putative. (125 aa)    
Predicted Functional Partners:
Toce_1803
L-threonine ammonia-lyase; COGs: COG1171 Threonine dehydratase; InterPro IPR005789:IPR001926:IPR002912:IPR000634; KEGG: chy:CHY_2459 threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; amino acid-binding ACT domain protein; SPTR: Threonine dehydratase; TIGRFAM: threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine ammonia-lyase, biosynthetic, long form; threonine dehydratase, medium form.
 
 
 0.890
apt
Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
 
  
 0.792
fusA
Translation elongation factor 2 (EF-2/EF-G); Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. [...]
  
 0.739
Toce_2128
COGs: COG0480 Translation elongation factors (GTPase); InterProIPR000795:IPR004540:IPR005225:IPR004161:IPR 005517:IPR000640; KEGG: tte:TTE2333 elongation factor G; PFAM: protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; elongation factor G domain IV; elongation factor G domain protein; SPTR: Translation elongation factor G; TIGRFAM: translation elongation factor G; small GTP-binding protein; PFAM: Elongation factor Tu domain 2; Elongation factor G C-terminus; Elongation factor Tu GTP binding domain; Elongation factor G, domain IV; TIGRFAM: translation elongat [...]
  
 0.739
Toce_1805
YheO domain protein; COGs: COG2964 conserved hypothetical protein; InterPro IPR013559; KEGG: chy:CHY_2461 PAC domain-containing protein; PFAM: YheO domain protein; SPTR: Putative PAC domain protein; PFAM: YheO-like PAS domain.
     
 0.705
Toce_0646
COGs: COG1929 Glycerate kinase; InterPro IPR004381; KEGG: chy:CHY_1268 glycerate kinase 2; PFAM: glycerate kinase; PRIAM: Glycerate kinase; SPTR: Glycerate kinase 2; TIGRFAM: glycerate kinase; PFAM: Glycerate kinase family; TIGRFAM: glycerate kinase; Belongs to the glycerate kinase type-1 family.
      0.682
tpiA
Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
  
 
 0.650
nnrD
Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
  
  
 0.616
rph
RNAse PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
 
 0.576
Toce_1802
COGs: COG1760 L-serine deaminase; InterPro IPR004643:IPR005131:IPR002912; KEGG: tit:Thit_0968 L-serine dehydratase, iron-sulfur-dependent, beta subunit; PFAM: serine dehydratase beta chain; amino acid-binding ACT domain protein; PRIAM: L-serine ammonia-lyase; SPTR: L-serine dehydratase, iron-sulfur-dependent, beta subunit; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, beta subunit; manually curated; PFAM: ACT domain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, beta subunit.
     
 0.575
Your Current Organism:
Thermosediminibacter oceani
NCBI taxonomy Id: 555079
Other names: T. oceani DSM 16646, Thermosediminibacter oceani DSM 16646, Thermosediminibacter oceani JW/IW-1228P, Thermosediminibacter oceani str. DSM 16646, Thermosediminibacter oceani strain DSM 16646
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